Author: "Akio Kihara" / Topic: humans - Searchworks@Jio Institute Digital Library Search Results

76 results on '"Akio Kihara"'

1. Amlexanox enhances the antitumor effect of anti-PD-1 antibody

Author: Koji Yano, Kaoru Yamada, Akio Kihara, and Kazuhiko Takeda
Subjects: 0301 basic medicine, Cytotoxic T cell, medicine.drug_class, T cell, medicine.medical_treatment, Programmed Cell Death 1 Receptor, Biophysics, Aminopyridines, Cancer immunotherapy, Monoclonal antibody, Biochemistry, Jurkat cells, B7-H1 Antigen, Interferon-gamma, Jurkat Cells, 03 medical and health sciences, 0302 clinical medicine, Interferon, Cell Line, Tumor, Antineoplastic Combined Chemotherapy Protocols, medicine, Animals, Humans, Molecular Biology, Cancer, Mice, Inbred BALB C, Chemistry, Immunity, Antibodies, Monoclonal, Dendritic Cells, Neoplasms, Experimental, Cell Biology, Mixed lymphocyte reaction, Mice, Inbred C57BL, 030104 developmental biology, medicine.anatomical_structure, Amlexanox, 030220 oncology & carcinogenesis, Cancer research, Female, Interferon-γ, Lymphocyte Culture Test, Mixed, T-Lymphocytes, Cytotoxic, medicine.drug
Abstract: Cancer immunotherapy, especially treatment with monoclonal antibodies (mAbs) that block programmed cell death-1 (PD-1)/programmed cell death-ligand 1 (PD-L1) signaling, has attracted attention as a new therapeutic option for cancer. However, only a limited number of patients have responded to this treatment approach. In this study, we searched for compounds that enhance the efficacy of anti-PD-1 mAb using mixed lymphocyte reaction (MLR), which is a mixed culture system of the two key cells (dendritic and T cells) involved in tumor immunity. We found that amlexanox enhanced production of interferon (IFN)-gamma, an indicator of T cell activation, by anti-PD-1 mAb. Amlexanox also induced PD-L1 expression in dendritic cells in MLR, whereas it did not stimulate interleukin-2 production by Jurkat T cells. These results suggest that amlexanox acts on dendritic cells, not T cells, in MLR. Furthermore, it enhanced the antitumor effect of the anti-PD-1 mAb in vivo in a mouse tumor-bearing model. The combination of amlexanox and anti-PD-1 mAb increased the expression of Ifng encoding IFN-gamma, IFN-gamma-related genes, Cd274 encoding PD-L1, and cytotoxic T cell-related genes in tumors. In conclusion, amlexanox stimulates the antitumor effect of anti-PD-1 mAb by acting on dendritic cells, which in turn activates cytotoxic T cells in tumors.
Published: 2021

2. Ceramide profiling of stratum corneum in Sjögren-Larsson syndrome

Author: Ayami Arai, Takuya Takeichi, Hiroyuki Wakamoto, Takayuki Sassa, Yasutoshi Ito, Yuya Murase, Tomoo Ogi, Masashi Akiyama, and Akio Kihara
Subjects: Sjogren-Larsson Syndrome, Fatty Acids, Humans, Ichthyosis, Female, Dermatology, Epidermis, Ceramides, Molecular Biology, Biochemistry, Ichthyosis, Lamellar
Abstract: Sjögren-Larsson syndrome (SLS) is a neurocutaneous disorder whose causative gene is the fatty aldehyde dehydrogenase ALDH3A2 and of which ichthyosis is the major skin symptom. The stratum corneum contains a variety of ceramides, among which ω-O-acylceramides (acylceramides) and protein-bound ceramides are essential for skin permeability barrier formation.To determine the ceramide classes/species responsible for SLS pathogenesis and the enzymes that are impaired in SLS.Genomic DNA was collected from peripheral blood samples from an SLS patient and her parents, and whole-genome sequencing and Sanger sequencing were performed. Lipids were extracted from stratum corneum samples from the SLS patient and healthy volunteers and subjected to ceramide profiling via liquid chromatography coupled with tandem mass spectrometry.A duplication (c.55_130dup) and a missense mutation (p.Lys447Glu) were found in the patient's ALDH3A2 gene. The patient had reduced levels of all acylceramide classes, with total acylceramide levels at 25 % of healthy controls. Reductions were also observed for several nonacylated ceramides: ceramides with phytosphingosine or 6-hydroxysphingosine in the long-chain base moiety were reduced to 24 % and 41 % of control levels, respectively, and ceramides with an α-hydroxy fatty acid as the fatty acid moiety were reduced to 29 %. The fatty acid moiety was shortened in many nonacylated ceramide classes.These results suggest that reduced acylceramide levels are a primary cause of the ichthyosis symptoms of SLS, but reductions in other ceramide classes may also be involved.
Published: 2022

3. Impaired production of skin barrier lipid acylceramides and abnormal localization of PNPLA1 due to ichthyosis-causing mutations in PNPLA1

Author: Tomohiro Nohara, Yusuke Ohno, and Akio Kihara
Subjects: Ichthyosis, Dermatology, Lipase, 1-Acylglycerol-3-Phosphate O-Acyltransferase, Ceramides, Biochemistry, Linoleic Acid, Mutation, Humans, Molecular Biology, Acyltransferases, Ichthyosis, Lamellar, Triglycerides, Skin
Abstract: PNPLA1 is a causative gene of autosomal recessive congenital ichthyosis. The transacylase PNPLA1 produces ω-O-acylceramides (acylceramides), lipids essential for the skin barrier function, by catalyzing the transfer of a linoleic acid from triglycerides to ω-hydroxyceramides.We aimed to validate the involvement of PNPLA1 mutations found in ichthyosis patients in the pathogenesis and elucidate the correlation between the effects of these mutations on acylceramide-producing activity and ichthyosis pathology.Acylceramide-producing activity of PNPLA1 mutants was investigated using a cell-based assay system, in which wild-type PNPLA1 or each PNPLA1 mutant was co-overexpressed with the enzymes involved in acylceramide synthesis. The effect of each mutation on the ABHD5-dependent lipid droplet localization of PNPLA1 was examined through indirect immunofluorescence microscopy.Of 16 PNPLA1 missense mutations, 15 mutations, except the C216R mutation, resulted in a complete loss of acylceramide-producing activity, while the C216R mutation weakly affected this activity. Intracellular localization of mutants with no activity varied among mutants. Two mutants (S19L and D172N) localized in lipid droplets, and eight mutants (S53L, S53W, A59V, T125N, D129E, R166C, P234S, and P235L) partially localized there. Five mutants (A34P, A34T, S53P, K141E, and P163L) localized throughout the cytosol.The PNPLA1 missense mutations examined in this study are responsible for ichthyosis pathology. The weak effect of C216R mutation on acylceramide-producing activity correlates with the mild symptoms of the ichthyosis patient. Sixteen PNPLA1 mutants were classified into four groups based on their acylceramide-producing activity and localization.
Published: 2022

4. Comprehensive stratum corneum ceramide profiling reveals reduced acylceramides in ichthyosis patient with CERS3 mutations

Author: Yasutomo Imai, Kiyofumi Yamanishi, Hiroyasu Uemura, Takayuki Sassa, Masaaki Kugo, Akio Kihara, Hideki Hayashi, Yuki Kyono, and Moe Yamamoto
Subjects: medicine.medical_specialty, Ceramide, Nonsense mutation, acylceramide, Dermatology, Ceramides, 030207 dermatology & venereal diseases, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Internal medicine, Congenital ichthyosis, medicine, Stratum corneum, Humans, stratum corneum, ceramide, biology, Sphingosine, Ichthyosis, Ceramide synthase 3, General Medicine, medicine.disease, Sphingolipid, medicine.anatomical_structure, Endocrinology, chemistry, 030220 oncology & carcinogenesis, Mutation, biology.protein, ichthyosis, sphingolipid, Epidermis, Ichthyosis, Lamellar
Abstract: The stratum corneum (SC) of the epidermis acts as a skin permeability barrier, and abnormalities in SC formation lead to several skin disorders. Lipids, especially the epidermis-specific ceramide classes omega-O-acylceramides (acylceramides) and protein-bound ceramides, are essential for skin barrier formation. Ceramide synthase 3 (CERS3) is involved in the synthesis of acylceramides and protein-bound ceramides, and CERS3 mutations cause autosomal recessive congenital ichthyosis. In the present study, we measured ceramide synthase activity and performed comprehensive SC ceramide profiling in an ichthyosis patient with compound heterozygous CERS3 mutations: nonsense mutation p.Arg75* and missense mutation p.Arg229His. The activity of p.Arg75* and p.Arg229His mutant CERS3 proteins was reduced to 4% and 56%, respectively, of the wild-type protein. In the patient's SC, acylceramide levels were greatly reduced, but the levels of protein-bound ceramides remained almost unchanged. Non-acylated ceramide levels were also affected in the patient; in particular, the levels of ceramides composed of sphingosine and non-hydroxy or alpha-hydroxy fatty acid were substantially higher than in healthy controls. These results suggest that a reduction in acylceramide levels alone leads to ichthyosis. Although protein-bound ceramides are synthesized from acylceramides, levels of acylceramides and protein-bound ceramides are not necessarily correlated.
Published: 2021

5. Comparative profiling and comprehensive quantification of stratum corneum ceramides in humans and mice by LC/MS/MS[S]

Author: Momoko Kawana, Yusuke Ohno, Akio Kihara, and Masatoshi Miyamoto
Subjects: 0301 basic medicine, Skin barrier, Ceramide, QD415-436, 030204 cardiovascular system & hematology, Ceramides, Biochemistry, Pathogenesis, Mice, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Endocrinology, Tandem Mass Spectrometry, epidermis, Lipidomics, Stratum corneum, medicine, Animals, Humans, skin barrier, Research Articles, Barrier function, mass spectrometry, chemistry.chemical_classification, sphingolipids, Fatty acid, Cell Biology, Sphingolipid, 030104 developmental biology, medicine.anatomical_structure, chemistry, lipidomics, fatty acid, Chromatography, Liquid
Abstract: Ceramides are the predominant lipids in the stratum corneum (SC) and are crucial components for normal skin barrier function. Although the composition of various ceramide classes in the human SC has been reported, that in mice is still unknown, despite mice being widely used as animal models of skin barrier function. Here, we performed LC/MS/MS analyses using recently available ceramide class standards to measure 25 classes of free ceramides and 5 classes of protein-bound ceramides from human and mouse SC. Phytosphingosine- and 6-hydroxy sphingosine-type ceramides, which both contain an additional hydroxyl group, were abundant in the human SC (35% and 45% of total ceramides, respectively). In contrast, in mice, phytosph-ingosine- and 6-hydroxy sphingosine-type ceramides were present at similar to 1% and undetectable levels, respectively, and sphingosine-type ceramides accounted for similar to 90%. In humans, ceramides containing alpha-hydroxy FA were abundant, whereas ceramides containing beta-hydroxy or omega-hydroxy FA were abundant in mice. The hydroxylated beta-carbon in beta-hydroxy ceramides was in the (R) configuration. Genetic knockout of beta-hydroxy acyl-CoA dehydratases in HAP1 cells increased beta-hydroxy ceramide levels, suggesting that beta-hydroxy acyl-CoA, an FA-elongation cycle intermediate in the ER, is a substrate for beta-hydroxy ceramide synthesis. We anticipate that our methods and findings will help to elucidate the role of each ceramide class in skin barrier formation and in the pathogenesis of skin disorders.
Published: 2020

6. Hypomyelinating spastic dyskinesia and ichthyosis caused by a homozygous splice site mutation leading to exon skipping in ELOVL1

Author: Taiko Takahashi, Sevcan Mercan, Takayuki Sassa, Günseli Bayram Akçapınar, Kanay Yararbaş, Seda Süsgün, Sibel Aylin Uğur İşeri, Akio Kihara, Nihan Hande Akçakaya, and SÜSGÜN, Seda
Subjects: Sulfonamides, Dyskinesias, Fatty Acid Elongases, Cerebral Palsy, Fatty Acids, Imidazoles, Ichthyosis, General Medicine, Exons, Thiophenes, Takahashi T., Mercan S., Sassa T., Akçapınar G. B. , Yararbaş K., Süsgün S., İşeri S. A. U. , Kihara A., Akçakaya N. H. , -Hypomyelinating spastic dyskinesia and ichthyosis caused by a homozygous splice site mutation leading to exon skipping in ELOVL1.-, Brain & development, 2022, Ceramides, Pedigree, Developmental Neuroscience, Muscle Spasticity, Tandem Mass Spectrometry, Pediatrics, Perinatology and Child Health, Mutation, Humans, Neurology (clinical), Chromatography, Liquid
Abstract: Next generation sequencing technologies allow detection of very rare pathogenic gene variants and uncover cerebral palsy. Herein, we describe two siblings with cerebral palsy due to ELOVL1 splice site mutation in autosomal recessive manner. ELOVL1 catalyzes fatty acid elongation to produce very long-chain fatty acids (VLCFAs; ≥C21), most of which are components of sphingolipids such as ceramides and sphingomyelins. Ichthyotic keratoderma, spasticity, hypomyelination, and dysmorphic facies (MIM: 618527) stem from ELOVL1 gene deficiency in human.We have studied a consanguineous family with whole exome sequencing (WES) and performed in depth analysis of cryptic splicing on the molecular level using RNA. Comprehensive analysis of ceramides in the skin stratum corneum of patients using liquid chromatography-tandem mass spectrometry (LC-MS/MS). ELOVL1 protein structure was computationally modelled.The novel c.376-2A G (ENST00000372458.8) homozygous variant in the affected siblings causes exon skipping. Comprehensive analysis of ceramides in the skin stratum corneum of patients using LC-MS/MS demonstrated significant shortening of fatty acid moieties and severe reduction in the levels of acylceramides.It has recently been shown that disease associated variants of ELOVL1 segregate in an autosomal dominant manner. However, our study for the first time demonstrates an alternative autosomal recessive inheritance model for ELOVL1. In conclusion, we suggest that in ultra-rare diseases, being able to identify the inheritance patterns of the disease-associated gene or genes can be an important guide to identifying the molecular mechanism of genetic cerebral palsy.
Published: 2021

7. Impaired production of the skin barrier lipid acylceramide by CYP4F22 ichthyosis mutations

Author: Akio Kihara, Yusuke Ohno, and Tomohiro Nohara
Subjects: Skin barrier, medicine.medical_specialty, Ichthyosis, Mutation, Missense, Membrane Proteins, Dermatology, Biology, Ceramides, Endoplasmic Reticulum, medicine.disease, Severity of Illness Index, Biochemistry, Recombinant Proteins, HEK293 Cells, CYP4F22, Cytochrome P-450 Enzyme System, Sphingosine N-Acyltransferase, medicine, Humans, Eye Proteins, Molecular Biology, Ichthyosis, Lamellar
Published: 2021

8. Whole picture of human stratum corneum ceramides, including the chain-length diversity of long-chain bases

Author: Madoka Suzuki, Yusuke Ohno, and Akio Kihara
Subjects: Serine C-Palmitoyltransferase, long-chain base, Cell Biology, Ceramides, Biochemistry, Permeability, Endocrinology, Tandem Mass Spectrometry, epidermis, Humans, lipidomics, stratum corneum, ceramide, skin barrier, sphingolipid, mass spectrometry
Abstract: Ceramides are essential lipids for skin permeability barrier function, and a wide variety of ceramide species exist in the stratum corneum (SC). Although ceramides with long-chain bases (LCBs) of various lengths have been identified in the human SC, a quantitative analysis that distinguishes ceramide species with different LCB chain lengths has not been yet published. Therefore, the whole picture of human SC ceramides remains unclear. Here, we conducted LC/MS/MS analyses to detect individual ceramide species differing in both the LCB and FA chain lengths and quantified 1,327 unbound ceramides and 254 protein-bound ceramides: the largest number of ceramide species reported to date. Ceramides containing an LCB whose chain length was C16-26 were present in the human SC. Of these, C18 (28.6%) was the most abundant, followed by C20 (24.8%) and C22 (12.8%). Each ceramide class had a characteristic distribution of LCB chain lengths and was divided into five groups according to this distribution. There was almost no difference in FA composition between the ceramide species containing LCBs of different chain lengths. Furthermore, we demonstrated that one of the serine palmitoyltransferase (SPT) complexes, SPTLC1/SPTLC3/SPTSSB, was able to produce C16-24 LCBs. The expression levels of all subunits constituting the SPT complexes increased during keratinocyte differentiation, resulting in the observed chain-length diversity of LCBs in the human SC. This study provides a molecular basis for elucidating human SC ceramide diversity and the pathogenesis of skin disorders.
Published: 2022

9. Widespread tissue distribution and synthetic pathway of polyunsaturated C24:2 sphingolipids in mammals

Author: Megumi Sawai, Mai Edagawa, Akio Kihara, and Yusuke Ohno
Subjects: 0301 basic medicine, Ceramide, Lipid microdomain, Fatty Acid Elongases, Linoleic acid, Ceramides, Sphingolipid, Cell Line, Linoleic Acid, Mice, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Acetyltransferases, Tandem Mass Spectrometry, Sphingosine N-Acyltransferase, Animals, Humans, Tissue Distribution, Molecular Biology, Ceramide synthase, chemistry.chemical_classification, Sphingolipids, Fatty acid, Biological membrane, Cell Biology, Lipid, Biosynthetic Pathways, Polyunsaturated fatty acid, 030104 developmental biology, Gene Expression Regulation, Liver, chemistry, Biochemistry, Fatty Acids, Unsaturated, lipids (amino acids, peptides, and proteins), Sphingomyelin, Spleen, 030217 neurology & neurosurgery, Chromatography, Liquid, HeLa Cells
Abstract: Sphingolipids are multifunctional lipids and a major constituent of the cell membranes of eukaryotes. Although the fatty acid (FA) moiety of sphingolipids is usually a saturated or monounsaturated FA, polyunsaturated FA (PUFA)-containing species also exist in mammalian tissues. In the present study, we showed that C24:2 PUFA-containing ceramide is one of the seven major ceramide species in a wide range of tissues. C24:2 ceramide levels were especially high in spleen and small intestine; in the former, it was the fourth most abundant ceramide species. However, both the synthetic pathway and the physiological function of C24:2 ceramide had yet to be identified. Tracer analysis using deuterium-labeled linoleic acid (C18:2) revealed that C24:2 ceramide is produced via elongation of linoleic acid. We also found that the FA elongase ELOVL1 and the ceramide synthase CERS2 were involved in C24:2 ceramide production. Sphingolipids are known to form lipid microdomains in membranes; however, in a detergent-resistant membrane (DRM) assay, we observed a lower proportion of C24:2 sphingomyelin in the DRM fraction than of saturated sphingomyelins, suggesting that C24:2 sphingolipids may act to negatively regulate lipid microdomain formation. Our findings expand our knowledge of sphingolipid diversity, and provide insight into how different sphingolipid molecular species play different functions in biological membranes.
Published: 2018

10. Molecular mechanism of the ichthyosis pathology of Chanarin–Dorfman syndrome: Stimulation of PNPLA1-catalyzed ω-O-acylceramide production by ABHD5

Author: Atsuki Nara, Yusuke Ohno, Shota Nakamichi, and Akio Kihara
Subjects: 0301 basic medicine, Immunoelectron microscopy, Linoleic acid, Dermatology, Ceramides, Endoplasmic Reticulum, Biochemistry, Lipid Metabolism, Inborn Errors, 03 medical and health sciences, chemistry.chemical_compound, Muscular Diseases, Lipid droplet, medicine, Humans, Microscopy, Immunoelectron, Molecular Biology, Triglycerides, Ichthyosis, Vesicle, Endoplasmic reticulum, Lipase, Lipid Droplets, 1-Acylglycerol-3-Phosphate O-Acyltransferase, Ichthyosiform Erythroderma, Congenital, medicine.disease, Staining, Cell biology, HEK293 Cells, 030104 developmental biology, chemistry, Knockout mouse, HeLa Cells
Abstract: Background ABHD5 mutations cause Chanarin–Dorfman syndrome accompanied by ichthyosis. ω- O -Acylceramide (acylceramide) is essential for skin permeability barrier formation. Acylceramide production is impaired in Abhd5 knockout mice. The transacylase PNPLA1 catalyzes the final step of acylceramide production: transfer of linoleic acid in triglyceride to ω-hydroxyceramide. Objective We aimed to elucidate the role of ABHD5 in acylceramide production and the molecular mechanism of the ichthyosis symptoms of Chanarin–Dorfman syndrome. Methods We investigated how ABHD5 influences acylceramide production using an acylceramide-producing cell system. The effects of ABHD5 and PNPLA1 expression on the morphology of lipid droplets were examined by indirect immunofluorescent microscopy and immunoelectron microscopy. Results When ABHD5 was expressed in the acylceramide-producing cell system, acylceramide synthesis by PNPLA1 was enhanced. Dispersed localization of PNPLA1 was observed by immunofluorescent microscopy in HeLa cells under lipid droplet-forming conditions. Co-expression with ABHD5 caused PNPLA1 to localize on the lipid droplet membranes or their periphery. This staining pattern was observed in cells where PNPLA1 and ABHD5 were expressed at low levels. In contrast, lipid droplets disappeared in cells where PNPLA1 and ABHD5 were highly expressed. Immunoelectron microscopic analyses suggested that lipid droplets underwent morphological changes, transforming into vesicles or becoming incorporated into the endoplasmic reticulum. ABHD5 mutations found in Chanarin–Dorfman syndrome patients reduced ABHD5’s ability to promote PNPLA1-dependent acylceramide production. Conclusion ABHD5 enhances PNPLA1-catalyzed acylceramide production. We speculate that ABHD5 retains triglycerides in the endoplasmic reticulum, and presents them to PNPLA1 to promote substrate recognition.
Published: 2018

11. Production of branched-chain very-long-chain fatty acids by fatty acid elongases and their tissue distribution in mammals

Author: Honoka Tanno, Megumi Sawai, Takayuki Sassa, and Akio Kihara
Subjects: 0301 basic medicine, Male, Ceramide, Fatty Acid Elongases, Very long chain fatty acid, Meibomian gland, Mice, Transgenic, Ceramides, Isozyme, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Mice, 0302 clinical medicine, medicine, Animals, Humans, Molecular Biology, Skin, chemistry.chemical_classification, Wax, Meibomian Glands, Cell Biology, Aldehyde Oxidoreductases, Wax ester, Mice, Inbred C57BL, 030104 developmental biology, Enzyme, medicine.anatomical_structure, HEK293 Cells, chemistry, Biochemistry, Gene Expression Regulation, Liver, visual_art, Lipidomics, Cholesteryl ester, visual_art.visual_art_medium, lipids (amino acids, peptides, and proteins), Acyl Coenzyme A, Cholesterol Esters, 030217 neurology & neurosurgery, Acyltransferases, Amino Acids, Branched-Chain, Sterol O-Acyltransferase
Abstract: Although most mammalian fatty acids (FAs) are straight-chain, there also exist branched-chain FAs such as iso- and anteiso-FAs, especially in the meibomian glands. Meibum lipids, which are secreted from the meibomian glands and are important for dry eye prevention, contain abundant branched-chain lipids, such as cholesteryl esters and wax esters with chain-lengths of ≥C21 (very-long-chain; VLC). However, the exact tissue distribution of branched-chain lipids or the enzymes involved in the production of branched-chain VLCFAs has remained poorly understood. Here, we revealed that FA elongases ELOVL1, ELOVL3, and ELOVL7, of the seven mammalian ELOVL isozymes, elongated saturated branched-chain acyl-CoAs. ELOVL3 was highly active toward iso-C17:0 and anteiso-C17:0 acyl-CoAs and elongated them up to iso-C23:0 and anteiso-C25:0 acyl-CoAs, respectively. ELOVL1 elongated both iso- and anteiso-C23:0 acyl-CoAs to C25:0 acyl-CoAs. By establishing a liquid chromatography-tandem mass spectrometry method capable of separating branched- and straight-chain lipids, we showed that essentially all of the cholesteryl esters and 88% of the wax esters in the mouse meibomian glands are branched. In Elovl1 mutant mice, the levels of ≥C24:0 branched-chain cholesteryl esters and ≥C25:0 branched-chain wax esters were decreased, indicating that ELOVL1 indeed elongates branched-chain VLC acyl-CoAs in vivo. In addition, substantial amounts of ceramides containing branched-chain FAs were present in the skin, meibomian glands, and liver. Our findings provide new insights into the molecular mechanisms that create FA and lipid diversity.
Published: 2020

12. Skin permeability barrier formation by the ichthyosis-causative gene FATP4 through formation of the barrier lipid ω-O-acylceramide

Author: Akio Kihara, Miku Hattori, Yusuke Ohno, Walee Chamulitrat, and Haruka Yamamoto
Subjects: Male, Ceramide, Infant, Premature, Diseases, Ceramides, Permeability, chemistry.chemical_compound, medicine, Animals, Humans, Ichthyosis prematurity syndrome, Skin, chemistry.chemical_classification, Mice, Knockout, Gene knockdown, Multidisciplinary, Chemistry, Ichthyosis, Fatty Acids, Fatty acid, Causative gene, Biological Sciences, medicine.disease, Fatty Acid Transport Proteins, Sphingolipid, Molecular biology, In vitro, Female, Epidermis
Abstract: The epidermis-specific lipid acylceramide plays a pivotal role in the formation of the permeability barrier in the skin; abrogation of its synthesis causes the skin disorder ichthyosis. However, the acylceramide synthetic pathway has not yet been fully elucidated: Namely, the acyl-CoA synthetase (ACS) involved in this pathway remains to be identified. Here, we hypothesized it to be encoded by FATP4/ACSVL4, the causative gene of ichthyosis prematurity syndrome (IPS). In vitro experiments revealed that FATP4 exhibits ACS activity toward an ω-hydroxy fatty acid (FA), an intermediate of the acylceramide synthetic pathway. Fatp4 knockout (KO) mice exhibited severe skin barrier dysfunction and morphological abnormalities in the epidermis. The total amount of acylceramide in Fatp4 KO mice was reduced to ∼10% of wild-type mice. Decreased levels and shortening of chain lengths were observed in the saturated, nonacylated ceramides. FA levels were not decreased in the epidermis of Fatp4 KO mice. The expression levels of the FA elongase Elovl1 were reduced in Fatp4 KO epidermis, partly accounting for the reduction and shortening of saturated, nonacylated ceramides. A decrease in acylceramide levels was also observed in human keratinocytes with FATP4 knockdown. From these results, we conclude that skin barrier dysfunction observed in IPS patients and Fatp4 KO mice is caused mainly by reduced acylceramide production. Our findings further elucidate the molecular mechanism governing acylceramide synthesis and IPS pathology.
Published: 2020

13. Neural symptoms in a gene knockout mouse model of Sjögren‐Larsson syndrome are associated with a decrease in 2‐hydroxygalactosylceramide

Author: Takuya Kitamura, Akio Kihara, Takayuki Sassa, Tsukasa Kanetake, Koki Nojiri, Megumi Sawai, Satoko Hattori, and Tsuyoshi Miyakawa
Subjects: 0301 basic medicine, medicine.medical_specialty, Light, Galactosylceramides, Anxiety, Motor Activity, Biochemistry, Mice, 03 medical and health sciences, Myelin, 0302 clinical medicine, Internal medicine, Genetics, medicine, Animals, Humans, Molecular Biology, Gene, Mice, Knockout, Sjögren–Larsson syndrome, Behavior, Animal, integumentary system, Depression, business.industry, food and beverages, Lipid Metabolism, medicine.disease, Aldehyde Oxidoreductases, Sphingolipid, Mice, Inbred C57BL, Sjogren-Larsson Syndrome, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, nervous system, Knockout mouse, sense organs, business, 030217 neurology & neurosurgery, Biotechnology
Abstract: Insulation by myelin lipids is essential to fast action potential conductivity: changes in their quality or amount can cause several neurologic disorders. Sjögren-Larsson syndrome (SLS) is one such disorder, which is caused by mutations in the fatty aldehyde dehydrogenase ALDH3A2. To date, the molecular mechanism underlying SLS pathology has remained unknown. In this study, we found that Aldh3a2 is expressed in oligodendrocytes and neurons in the mouse brain, and neurons of Aldh3a2 knockout (KO) mice exhibited impaired metabolism of the long-chain base, a component of sphingolipids. Aldh3a2 KO mice showed several abnormalities corresponding to SLS symptoms in behavioral tests, including increased paw slips on a balance beam and light-induced anxiety. In their brain tissue, 2-hydroxygalactosylceramide, an important lipid for myelin function and maintenance, was reduced by the inactivation of fatty acid 2-hydroxylase. Our findings provide important new insights into the molecular mechanisms responsible for neural pathogenesis caused by lipid metabolism abnormalities.-Kanetake, T., Sassa, T., Nojiri, K., Sawai, M., Hattori, S., Miyakawa, T., Kitamura, T., Kihara, A. Neural symptoms in a gene knockout mouse model of Sjögren-Larsson syndrome are associated with a decrease in 2-hydroxygalactosylceramide.
Published: 2018

14. The 3-hydroxyacyl-CoA dehydratases HACD1 and HACD2 exhibit functional redundancy and are active in a wide range of fatty acid elongation pathways

Author: Masatoshi Miyamoto, Takayuki Sassa, Chieko Nishioka, Yukiko Uchida, Shigeyoshi Itohara, Megumi Sawai, Yusuke Ohno, and Akio Kihara
Subjects: 0301 basic medicine, Male, Myoblasts, Skeletal, Recombinant Fusion Proteins, Very long chain fatty acid, Biochemistry, Gene Expression Regulation, Enzymologic, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Muscular Diseases, Catalytic Domain, Cell Line, Tumor, medicine, Animals, Humans, Muscle, Skeletal, Molecular Biology, Cells, Cultured, Hydro-Lyases, chemistry.chemical_classification, Mice, Knockout, 030102 biochemistry & molecular biology, Fatty acid metabolism, Molecular Structure, Fatty Acids, Fatty acid, Skeletal muscle, Membrane Proteins, Cell Biology, Lipids, Yeast, Isoenzymes, Molecular Weight, 030104 developmental biology, medicine.anatomical_structure, chemistry, Dehydratase, Fatty acid elongation, Elongation, CRISPR-Cas Systems, Protein Tyrosine Phosphatases
Abstract: Differences among fatty acids (FAs) in chain length and number of double bonds create lipid diversity. FA elongation proceeds via a four-step reaction cycle, in which the 3-hydroxyacyl-CoA dehydratases (HACDs) HACD1-4 catalyze the third step. However, the contribution of each HACD to 3-hydroxyacyl-CoA dehydratase activity in certain tissues or in different FA elongation pathways remains unclear. HACD1 is specifically expressed in muscles and is a myopathy-causative gene. Here, we generated Hacd1 KO mice and observed that these mice had reduced body and skeletal muscle weights. In skeletal muscle, HACD1 mRNA expression was by far the highest among the HACDs. However, we observed only an similar to 40% reduction in HACD activity and no changes in membrane lipid composition in Hacd1-KO skeletal muscle, suggesting that some HACD activities are redundant. Moreover, when expressed in yeast, both HACD1 and HACD2 participated in saturated and monounsaturated FA elongation pathways. Disruption of HACD2 in the haploid human cell line HAP1 significantly reduced FA elongation activities toward both saturated and unsaturated FAs, and HACD1 HACD2 double disruption resulted in a further reduction. Overexpressed HACD3 exhibited weak activity in saturated and monounsaturated FA elongation pathways, and no activity was detected for HACD4. We therefore conclude that HACD1 and HACD2 exhibit redundant activities in a wide range of FA elongation pathways, including those for saturated to polyunsaturated FAs, with HACD2 being the major 3-hydroxyacyl-CoA dehydratase. Our findings are important for furthering the understanding of the molecular mechanisms in FA elongation and diversity.
Published: 2017

15. PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide

Author: Akio Kihara, Yusuke Ohno, Nozomi Kamiyama, and Shota Nakamichi
Subjects: 0301 basic medicine, Acylation, Linoleic acid, Science, Cell, Mutant, General Physics and Astronomy, Ceramides, Article, General Biochemistry, Genetics and Molecular Biology, Substrate Specificity, Linoleic Acid, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, medicine, Humans, Diacylglycerol O-Acyltransferase, Triglycerides, Skin, Multidisciplinary, biology, Triglyceride, integumentary system, Ichthyosis, HEK 293 cells, Lipase, General Chemistry, medicine.disease, Enzyme assay, In vitro, Sjogren-Larsson Syndrome, HEK293 Cells, 030104 developmental biology, medicine.anatomical_structure, Biochemistry, chemistry, 030220 oncology & carcinogenesis, Biocatalysis, biology.protein
Abstract: Lipids are the primary components of the skin permeability barrier, which is the body's most powerful defensive mechanism against pathogens. Acylceramide (ω-O-acylceramide) is a specialized lipid essential for skin barrier formation. Here, we identify PNPLA1 as the long-sought gene involved in the final step of acylceramide synthesis, esterification of ω-hydroxyceramide with linoleic acid, by cell-based assays. We show that increasing triglyceride levels by overproduction of the diacylglycerol acyltransferase DGAT2 stimulates acylceramide production, suggesting that triglyceride may act as a linoleic acid donor. Indeed, the in vitro analyses confirm that PNPLA1 catalyses acylceramide synthesis using triglyceride as a substrate. Mutant forms of PNPLA1 found in patients with ichthyosis exhibit reduced or no enzyme activity in either cell-based or in vitro assays. Altogether, our results indicate that PNPLA1 is directly involved in acylceramide synthesis as a transacylase, and provide important insights into the molecular mechanisms of skin barrier formation and of ichthyosis pathogenesis., Loss-of-function mutations in an enzyme of unknown function, PNPLA1, cause dry and scaling skin in humans. Here Ohno et al. show that PNPLA1 is a transacylase that acts in the final step of acylceramide production- esterification between ω-hydroxyceramide and linoleic acid acylceramide, yielding a lipid essential for skin barrier function.
Published: 2017

16. Biallelic Mutations in KDSR Disrupt Ceramide Synthesis and Result in a Spectrum of Keratinization Disorders Associated with Thrombocytopenia

Author: Maria Luisa Lozano, Pablo Fernández-Crehuet, Junko Ishikawa, Vicente Vicente, Kazumitsu Sugiura, Jemima E. Mellerio, Daiei Kojima, Masashi Akiyama, Yusuke Ohno, Antonio Torrelo, David P. Kelsell, Yoichiro Toi, Yuka Yasuda, Michael A. Simpson, Takuya Takeichi, Yusuke Okuno, Ana Belén Rodrigo, José Rivera, Takatoshi Murase, Lu Liu, John A. McGrath, Yasushi Ogawa, W.H. Irwin McLean, Akio Kihara, John Y.W. Lee, and Yutaka Nishimura
Subjects: 0301 basic medicine, Male, Ceramide, Adolescent, Hyperkeratosis, Dermatology, KDS, 3-ketodihydrosphingosine, Biology, In Vitro Techniques, Compound heterozygosity, medicine.disease_cause, Ceramides, Biochemistry, Severity of Illness Index, Article, Sampling Studies, 03 medical and health sciences, chemistry.chemical_compound, Young Adult, Keratoderma, Palmoplantar, medicine, Humans, Genetic Predisposition to Disease, Sphingosine-1-phosphate, Allele, Child, Molecular Biology, Alleles, S1P, sphingosine-1-phosphate, Genetics, Mutation, integumentary system, Ichthyosis, Biopsy, Needle, Cell Biology, medicine.disease, Prognosis, Phenotype, Immunohistochemistry, Thrombocytopenia, 3. Good health, Pedigree, Alcohol Oxidoreductases, 030104 developmental biology, chemistry, Cancer research, DHS, dihydrosphingosine
Abstract: Mutations in ceramide biosynthesis pathways have been implicated in a few Mendelian disorders of keratinization although ceramides are known to have key roles in several biological processes in skin and other tissues. Using whole-exome sequencing in four probands with undiagnosed skin hyperkeratosis/ichthyosis, we identified compound heterozygosity for mutations in KDSR, encoding an enzyme in the de novo synthesis pathway of ceramides. Two individuals had hyperkeratosis confined to palms and soles as well as anogenital skin, whereas the other two had more severe, generalized harlequin ichthyosis-like skin. Of note, thrombocytopenia was present in all cases. The mutations in KDSR were associated with reduced ceramide levels in skin and impaired platelet function. KDSR enzymatic activity was variably reduced in all cases resulting in defective acylceramide synthesis. Mutations in KDSR have recently been reported in inherited recessive forms of progressive symmetric erythrokeratoderma, but our study demonstrates that biallelic mutations in KDSR are implicated in an extended spectrum of disorders of keratinization in which thrombocytopenia is also part of the phenotype. Mutations in KDSR cause defective ceramide biosynthesis, underscoring the importance of ceramide and sphingosine synthesis pathways in skin and platelet biology.
Published: 2017

17. Severe Skin Permeability Barrier Dysfunction in Knockout Mice Deficient in a Fatty Acid ω-Hydroxylase Crucial to Acylceramide Production

Author: Megumi Sawai, Masatoshi Miyamoto, Narumi Itoh, Akio Kihara, and Takayuki Sassa
Subjects: 0301 basic medicine, Male, Ceramide, medicine.medical_specialty, Dermatology, Ceramides, Biochemistry, Severity of Illness Index, Permeability, 03 medical and health sciences, chemistry.chemical_compound, Mice, 0302 clinical medicine, CYP4F22, Internal medicine, Congenital ichthyosis, medicine, Stratum corneum, Animals, Humans, Cytochrome P450 Family 4, Molecular Biology, chemistry.chemical_classification, Mice, Knockout, Transepidermal water loss, integumentary system, Ichthyosis, Fatty acid, Cell Biology, Desmosomes, medicine.disease, Disease Models, Animal, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, chemistry, Epidermal Cells, 030220 oncology & carcinogenesis, Knockout mouse, Female, Epidermis
Abstract: The skin permeability barrier is indispensable for maintaining water inside the body and preventing the invasion of pathogens and allergens; abnormalities lead to skin disorders such as atopic dermatitis and ichthyosis. Acylceramide is an essential lipid for skin barrier formation, and CYP4F22 is a fatty acid ω-hydroxylase involved in its synthesis. Mutations in CYP4F22 cause autosomal recessive congenital ichthyosis, although the symptoms vary among mutation sites and types. Here, we generated knockout mice deficient in Cyp4f39, the mouse ortholog of human CYP4F22, to investigate the effects of completely abrogating the function of the fatty acid ω-hydroxylase involved in acylceramide production on skin barrier formation. Cyp4f39 knockout mice died within 8 hours of birth. Large increases in transepidermal water loss and penetration of a dye from outside the body were observed, indicating severe skin barrier dysfunction. Histologic analyses of the epidermis revealed impairment of lipid lamella formation, accumulation of corneodesmosomes in the stratum corneum, and persistence of periderm. In addition, lipid analyses by mass spectrometry showed almost complete loss of acylceramide and its precursor ω-hydroxy ceramide. In conclusion, our findings provide clues to the molecular mechanisms of skin barrier abnormalities and the pathogenesis of ichthyosis caused by Cyp4f39 and CYP4F22 by association.
Published: 2019

18. The very-long-chain fatty acid elongase Elo2 rescues lethal defects associated with loss of the nuclear barrier function in fission yeast cells

Author: Yasuha, Kinugasa, Yasuhiro, Hirano, Megumi, Sawai, Yusuke, Ohno, Tomoko, Shindo, Haruhiko, Asakawa, Yuji, Chikashige, Shinsuke, Shibata, Akio, Kihara, Tokuko, Haraguchi, and Yasushi, Hiraoka
Subjects: Saccharomyces cerevisiae Proteins, Acetyltransferases, Fatty Acid Elongases, Nuclear Envelope, Schizosaccharomyces, Humans, Membrane Proteins, Schizosaccharomyces pombe Proteins
Abstract: In eukaryotic cells, chromosomes are confined to the nucleus, which is compartmentalized by the nuclear membranes; these are continuous with the endoplasmic reticulum membranes. Maintaining the homeostasis of these membranes is an important cellular activity performed by lipid metabolic enzymes. However, how lipid metabolic enzymes affect nuclear membrane functions remains to be elucidated. We found that the very-long-chain fatty acid elongase Elo2 is located in the nuclear membrane and prevents lethal defects associated with nuclear membrane ruptures in mutants of the nuclear membrane proteins Lem2 and Bqt4 in the fission yeast
Published: 2018

19. Structure-inspired design of a sphingolipid mimic sphingosine-1-phosphate receptor agonist from a naturally occurring sphingomyelin synthase inhibitor

Author: Yoshiko Suga, Keisuke Jojima, Mahadeva M. M. Swamy, Min Yao, Akio Kihara, Yasuyuki Igarashi, Yuta Murai, Susumu Mitsutake, Kenji Monde, Masaki Anetai, Jian Yu, and Yusuke Ohno
Subjects: 0301 basic medicine, Agonist, Ceramide, medicine.drug_class, media_common.quotation_subject, Transferases (Other Substituted Phosphate Groups), CHO Cells, Catalysis, 03 medical and health sciences, chemistry.chemical_compound, Structure-Activity Relationship, Cricetulus, Sphingomyelin synthase, Materials Chemistry, medicine, Animals, Humans, Enzyme Inhibitors, Receptor, Internalization, media_common, Biological Products, Sphingolipids, Sphingosine, biology, Dose-Response Relationship, Drug, Molecular Structure, Metals and Alloys, General Chemistry, Sphingolipid, Salicylates, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Molecular Docking Simulation, Receptors, Lysosphingolipid, 030104 developmental biology, chemistry, Biochemistry, Docking (molecular), Drug Design, Ceramics and Composites, biology.protein, lipids (amino acids, peptides, and proteins)
Abstract: Ginkgolic acid obtained as a sphingomyelin synthase inhibitor from a plant extract library inspired the concept of sphingolipid mimics. Ginkgolic acid-derived N-acyl anilines and ginkgolic acid 2-phosphate (GA2P) respectively mimic ceramide and sphingosine 1-phosphate (S1P) in structure and function. The GA2P-induced phosphorylation of ERK and internalization of S1P receptor 1 (S1P(1)) indicated potent agonist activity. Docking studies revealed that GA2P adopts a similar binding conformation to the bound ligand ML5, which is a strong antagonist of S1P(1).
Published: 2018

20. Direct uptake of sphingosine-1-phosphate independent of phospholipid phosphatases

Author: Hirotaka Goto, Masatoshi Miyamoto, and Akio Kihara
Subjects: 0301 basic medicine, S1PR, sphingosine-1-phosphate receptor, channel, MEDEP, mouse ES cell-derived erythroid progenitor line, Biochemistry, chemistry.chemical_compound, Gene Knockout Techniques, PC, phosphatidylcholine, Sph, sphingosine, Sphingosine, HUVEC, human umbilical vein endothelial cell, PA, phosphatidic acid, CERS, ceramide synthase, PS, phosphatidylserine, PLPP, phospholipid phosphatase, Cell biology, Endothelial stem cell, transporter, endothelial cell, phospholipid phosphatase, lipids (amino acids, peptides, and proteins), TKO, triple KO, Research Article, Pi, orthophosphoric acid, SPNS2, sphingolipid transporter 2, Ceramide, HDL, high-density lipoprotein, PE, phosphatidylethanolamine, PI, phosphatidylinositol, Cell Line, Dephosphorylation, 03 medical and health sciences, FBS, fetal bovine serum, lipid, Extracellular, Animals, Humans, Sphingosine-1-phosphate, ceramide, Molecular Biology, S1P, sphingosine-1-phosphate, 030102 biochemistry & molecular biology, organic chemicals, Biological Transport, MFSD2B, major facilitator superfamily domain containing 2B, Cell Biology, Lipid signaling, Sphingolipid, PAP, phosphatidic acid phosphatase, Phosphoric Monoester Hydrolases, 030104 developmental biology, chemistry, phosphatidylethanolamine, LPP, lipid phosphate phosphatase, sphingosine-1-phosphate, BSA, bovine serum albumin, erythrocyte, sphingolipid, Lysophospholipids, UPLC, ultra–high performance liquid chromatography, HA, hemagglutinin
Abstract: Sphingosine-1-phosphate (S1P) is a lipid mediator that is relatively abundant in plasma and plays an important role in the vascular and immune systems. To date, the only known mechanism for removing S1P from plasma has been dephosphorylation by phospholipid phosphatases (PLPPs) on the surface of cells in contact with the plasma. However, there remains a possibility that PLPP-independent dephosphorylation or direct S1P uptake into cells could occur. To examine these possibilities, here we generated triple KO (TKO) HAP1 cells that lacked all PLPPs (PLPP1-3) present in mammals. In the TKO cells, the intracellular metabolism of externally added deuterium-labeled S1P to ceramide was reduced to 17% compared with the WT cells, indicating that most extracellular S1P is dephosphorylated by PLPPs and then taken up into cells. However, this result also reveals the existence of a PLPP-independent S1P uptake pathway. Tracer experiments using [P-32]S1P showed the existence of a direct S1P uptake pathway that functions without prior dephosphorylation. Overexpression of sphingolipid transporter 2 (SPNS2) or of major facilitator superfamily domain containing 2B (MFSD2B), both known S1P efflux transporters, in TKO cells increased the direct uptake of S1P, whereas KO of MFSD2B in TKO cells reduced this uptake. These results suggest that these are channel-type transporters and capable of not only exporting but also importing S1P. Furthermore, we observed that erythroid cells expressing MFSD2B, exhibited high S1P uptake activity. Our findings describing direct S1P uptake may contribute to the elucidation of the molecular mechanisms that regulate plasma S1P concentration.
Published: 2021

21. Enzyme Activities of the Ceramide Synthases CERS2-6 Are Regulated by Phosphorylation in the C-terminal Region

Author: Akio Kihara, Takayuki Sassa, and Taisuke Hirayama
Subjects: 0301 basic medicine, Ceramide, Biochemistry, Substrate Specificity, Dephosphorylation, Mice, 03 medical and health sciences, Enzyme activator, chemistry.chemical_compound, 0302 clinical medicine, Sphingosine N-Acyltransferase, Animals, Humans, Protein phosphorylation, Naphthyridines, Phosphorylation, Casein Kinase II, Molecular Biology, Ceramide synthase, Sphingolipids, Brain, Cell Biology, Lipid signaling, Lipids, Sphingolipid, Protein Structure, Tertiary, Enzyme Activation, HEK293 Cells, 030104 developmental biology, chemistry, Phenazines, 030217 neurology & neurosurgery
Abstract: Ceramide and complex sphingolipids regulate important cellular functions including cell growth, apoptosis, and signaling. Dysregulation of sphingolipid metabolism leads to pathological consequences such as sphingolipidoses and insulin resistance. Ceramides in mammals vary greatly in their acyl-chain composition: six different ceramide synthase isozymes (CERS1-6) that exhibit distinct substrate specificity and tissue distribution account for this diversity. In the present study, we demonstrated that CERS2-6 were phosphorylated at the cytoplasmic C-terminal regions. Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing its V-max value. Phosphorylation modestly increased the catalytic activities of CERS4 and -5 and mildly increased those of CERS3 and -6. Dephosphorylation of endogenous ceramide synthases in the mouse brain led to severely reduced activity toward the Cers2 substrates C22:0/C24:0-CoAs and modestly reduced activity toward the Cers5/6 substrate C16:0-CoA. These results suggest that the phosphorylation of ceramide synthases may be a key regulatory point in the control of the distribution and levels of sphingolipids of various acyl-chain lengths.
Published: 2016

22. A role of the sphingosine-1-phosphate (S1P)–S1P receptor 2 pathway in epithelial defense against cancer (EDAC)

Author: Yusuke Ohba, Yasuyuki Fujita, Akio Kihara, Yuta Yako, Yoichiro Fujioka, Sayaka Yamamoto, Yusuke Ohno, Susumu Ishikawa, Shunsuke Kon, Mihoko Kajita, and Takeshi Kameyama
Subjects: 0301 basic medicine, Carcinogenesis, Pyridines, Filamins, Cell, Mutation, Missense, Biology, Bioinformatics, medicine.disease_cause, Filamin, Madin Darby Canine Kidney Cells, Proto-Oncogene Proteins p21(ras), 03 medical and health sciences, chemistry.chemical_compound, Dogs, Cell Movement, Sphingosine, Neoplasms, medicine, Animals, Humans, Sphingosine-1-phosphate, Cell Interactions, Receptor, Sphingosine-1-Phosphate Receptors, Molecular Biology, S1PR2, rho-Associated Kinases, Epithelial Cells, Articles, Cell Biology, Cell biology, Enzyme Activation, Receptors, Lysosphingolipid, 030104 developmental biology, medicine.anatomical_structure, chemistry, Pyrazoles, Lysophospholipids, Signal transduction, Signal Transduction
Abstract: Normal epithelial cells have an ability to sense and actively eliminate neighboring transformed cells, a process called epithelial defense against cancer (EDAC). Exogenous S1P plays a crucial role in EDAC; the S1P–S1PR2 pathway regulates Rho–Rho kinase–filamin in the surrounding normal cells, promoting apical extrusion of RasV12-transformed cells from epithelia., At the initial step of carcinogenesis, transformation occurs in single cells within epithelia, where the newly emerging transformed cells are surrounded by normal epithelial cells. A recent study revealed that normal epithelial cells have an ability to sense and actively eliminate the neighboring transformed cells, a process named epithelial defense against cancer (EDAC). However, the molecular mechanism of this tumor-suppressive activity is largely unknown. In this study, we investigated a role for the sphingosine-1-phosphate (S1P)–S1P receptor 2 (S1PR2) pathway in EDAC. First, we show that addition of the S1PR2 inhibitor significantly suppresses apical extrusion of RasV12-transformed cells that are surrounded by normal cells. In addition, knockdown of S1PR2 in normal cells induces the same effect, indicating that S1PR2 in the surrounding normal cells plays a positive role in the apical elimination of the transformed cells. Of importance, not endogenous S1P but exogenous S1P is involved in this process. By using FRET analyses, we demonstrate that S1PR2 mediates Rho activation in normal cells neighboring RasV12-transformed cells, thereby promoting accumulation of filamin, a crucial regulator of EDAC. Collectively these data indicate that S1P is a key extrinsic factor that affects the outcome of cell competition between normal and transformed epithelial cells.
Published: 2016

23. The role of PNPLA1 in ω-O-acylceramide synthesis and skin barrier function

Author: Tetsuya Hirabayashi, Makoto Murakami, and Akio Kihara
Subjects: 0301 basic medicine, Ceramide, Phospholipase, Ceramides, 030207 dermatology & venereal diseases, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Phospholipase A2, Congenital ichthyosis, Animals, Humans, Molecular Biology, Gene knockout, Skin, biology, Chemistry, Lipid metabolism, Cell Differentiation, Cell Biology, Lipase, Sphingolipid, 030104 developmental biology, Biochemistry, Mutation, biology.protein, Epidermis, Function (biology), Ichthyosis, Lamellar
Abstract: The human genome encodes nine enzymes belonging to the patatin-like phospholipase domain-containing lipase (PNPLA)/Ca2+-independent phospholipase A2 (iPLA2) family. Although most PNPLA/iPLA2 enzymes are widely distributed and act on phospholipids or neutral lipids as (phospho)lipases to play homeostatic roles in lipid metabolism, the function of PNPLA1 remained a mystery until a few years ago. However, the recent finding that mutations in the human PNPLA1 gene are linked to autosomal recessive congenital ichthyosis (ARCI), as well as evidence obtained from biochemical and gene knockout studies, has shed light on the function of this enzyme in skin-specific sphingolipid metabolism rather than glycerophospholipid metabolism. PNPLA1 is specifically expressed in differentiated keratinocytes and plays a crucial role in the biosynthesis of ω-O-acylceramide, a particular class of sphingolipids that is essential for skin barrier function. PNPLA1 acts as a unique transacylase that specifically transfers linoleic acid from triglyceride to ω-hydroxy fatty acid in ceramide, thus giving rise to ω-O-acylceramide. In this review, we overview the biosynthetic route and biological role of epidermal ω-O-acylceramide, highlight the function of PNPLA1 as a bona fide acylceramide synthase required for proper skin barrier function and keratinocyte differentiation, and summarize the mutations of PNPLA1 currently identified in ARCI patients. This article is part of a Special Issue entitled Novel functions of phospholipase A2 Guest Editors: Makoto Murakami and Gerard Lambeau
Published: 2018

24. Sphingosine 1-phosphate receptor modulator ONO-4641 stimulates CD11b

Author: Takanori, Asakura, Makoto, Ishii, Ho, Namkoong, Shoji, Suzuki, Shizuko, Kagawa, Kazuma, Yagi, Takaki, Komiya, Takafumi, Hashimoto, Satoshi, Okamori, Hirofumi, Kamata, Sadatomo, Tasaka, Akio, Kihara, Ahmed E, Hegab, Naoki, Hasegawa, and Tomoko, Betsuyaku
Subjects: CD11b Antigen, T-Lymphocytes, Receptors, Cell Surface, Naphthalenes, Adoptive Transfer, Mice, Inbred C57BL, Disease Models, Animal, Mice, Pulmonary Disease, Chronic Obstructive, Receptors, Lysosphingolipid, Pulmonary Emphysema, Cell Movement, Animals, Azetidines, Humans, Female, Lung, Cells, Cultured, Cell Proliferation
Abstract: Sphingolipids play a pivotal role in the pathogenesis of chronic obstructive pulmonary disease (COPD). However, little is known about the precise roles of sphingosine-1-phosphate (S1P), a bioactive sphingolipid metabolite, and its receptor modulation in COPD. In this study, we demonstrated that the S1P receptor modulator ONO-4641 induced the expansion of lung CD11b
Published: 2017

25. Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification

Author: Shuyu Takagi, Tatsuro Naganuma, Akio Kihara, and Takuya Kitamura
Subjects: Aldehyde dehydrogenase, lipid droplet, medicine.disease_cause, Biochemistry, Mice, Structure-Activity Relationship, Prenylation, aldehyde dehydrogenase, lipid, Lipid droplet, Protein targeting, medicine, protein targeting, Animals, Humans, Molecular Biology, lipid modification, Aldehydes, biology, Tryptophan, Cell Biology, Lipid Droplets, prenylation, Subcellular localization, Aldehyde Oxidoreductases, Lipids, Enzyme assay, Protein Transport, HEK293 Cells, biology.protein, Lipid modification, HeLa Cells
Abstract: Aldehyde dehydrogenases (ALDHs) catalyse the conversion of toxic aldehydes into non-toxic carboxylic acids. Of the 21 ALDHs in mice, it is the ALDH3 family members (ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2 and ALDH3B3) that are responsible for the removal of lipid-derived aldehydes. However, ALDH3B2 and ALDH3B3 have yet to be characterized. In the present study, we examined the enzyme activity, tissue distribution and subcellular localization of ALDH3B2 and ALDH3B3. Both were found to exhibit broad substrate preferences from medium- to long-chain aldehydes, resembling ALDH3A2 and ALDH3B1. Although ALDH3B2 and ALDH3B3 share extremely high sequence similarity, their localizations differ, with ALDH3B2 found in lipid droplets and ALDH3B3 localized to the plasma membrane. Both were modified by prenylation at their C-termini; this modification greatly influenced their membrane localization and enzymatic activity towards hexadecanal. We found that their C-terminal regions, particularly the two tryptophan residues (Trp462 and Trp469) of ALDH3B2 and the two arginine residues (Arg462 and Arg463) of ALDH3B3, were important for the determination of their specific localization. Abnormal quantity and perhaps quality of lipid droplets are implicated in several metabolic diseases. We speculate that ALDH3B2 acts to remove lipid-derived aldehydes in lipid droplets generated via oxidative stress as a quality control mechanism.
Published: 2015

26. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author: Daniel J. Klionsky, Kotb Abdelmohsen, Akihisa Abe, Md Joynal Abedin, Hagai Abeliovich, Abraham Acevedo Arozena, Hiroaki Adachi, Christopher M. Adams, Peter D. Adams, Khosrow Adeli, Peter J. Adhihetty, Sharon G. Adler, Galila Agam, Rajesh Agarwal, Manish K. Aghi, Maria Agnello, Patrizia Agostinis, Patricia V. Aguilar, Julio Aguirre Ghiso, Edoardo M. Airoldi, Slimane Ait Si Ali, Takahiko Akematsu, Emmanuel T. Akporiaye, Mohamed Al Rubeai, Guillermo M. Albaiceta, Chris Albanese, Diego Albani, Matthew L. Albert, Jesus Aldudo, Hana Algül, Mehrdad Alirezaei, Iraide Alloza, Alexandru Almasan, Maylin Almonte Beceril, Emad S. Alnemri, Covadonga Alonso, Nihal Altan Bonnet, Dario C. Altieri, Silvia Alvarez, Lydia Alvarez Erviti, Sandro Alves, Giuseppina Amadoro, Atsuo Amano, Consuelo Amantini, Santiago Ambrosio, Ivano Amelio, Amal O. Amer, Mohamed Amessou, Angelika Amon, Zhenyi An, Frank A. Anania, Stig U. Andersen, Usha P. Andley, Catherine K. Andreadi, Nathalie Andrieu Abadie, Alberto Anel, David K. Ann, Shailendra Anoopkumar Dukie, Manuela Antonioli, Hiroshi Aoki, Nadezda Apostolova, Saveria Aquila, Katia Aquilano, Koichi Araki, Eli Arama, Agustin Aranda, Jun Araya, Alexandre Arcaro, Esperanza Arias, Hirokazu Arimoto, Aileen R. Ariosa, Jane L. Armstrong, Thierry Arnould, Ivica Arsov, Katsuhiko Asanuma, Valerie Askanas, Eric Asselin, Ryuichiro Atarashi, Sally S. Atherton, Julie D. Atkin, Laura D. Attardi, Patrick Auberger, Georg Auburger, Laure Aurelian, Riccardo Autelli, Laura Avagliano, Maria Laura Avantaggiati, Limor Avrahami, Suresh Awale, Neelam Azad, Tiziana Bachetti, Jonathan M. Backer, Dong Hun Bae, Jae sung Bae, Ok Nam Bae, Soo Han Bae, Eric H. Baehrecke, Seung Hoon Baek, Stephen Baghdiguian, Agnieszka Bagniewska Zadworna, Hua Bai, Jie Bai, Xue Yuan Bai, Yannick Bailly, Kithiganahalli Narayanaswamy Balaji, Walter Balduini, Andrea Ballabio, Rena Balzan, Rajkumar Banerjee, Gábor Bánhegyi, Haijun Bao, Benoit Barbeau, Maria D. Barrachina, Esther Barreiro, Bonnie Bartel, Alberto Bartolomé, Diane C. Bassham, Maria Teresa Bassi, Robert C. Bast Jr, Alakananda Basu, Maria Teresa Batista, Henri Batoko, Maurizio Battino, Kyle Bauckman, Bradley L. Baumgarner, K. Ulrich Bayer, Rupert Beale, Jean François Beaulieu, George R. Beck Jr, Christoph Becker, J. David Beckham, Pierre André Bédard, Patrick J. Bednarski, Thomas J. Begley, Christian Behl, Christian Behrends, Georg MN Behrens, Kevin E. Behrns, Eloy Bejarano, Amine Belaid, Francesca Belleudi, Giovanni Bénard, Guy Berchem, Daniele Bergamaschi, Matteo Bergami, Ben Berkhout, Laura Berliocchi, Amélie Bernard, Monique Bernard, Francesca Bernassola, Anne Bertolotti, Amanda S. Bess, Sébastien Besteiro, Saverio Bettuzzi, Savita Bhalla, Shalmoli Bhattacharyya, Sujit K. Bhutia, Caroline Biagosch, Michele Wolfe Bianchi, Martine Biard Piechaczyk, Viktor Billes, Claudia Bincoletto, Baris Bingol, Sara W. Bird, Marc Bitoun, Ivana Bjedov, Craig Blackstone, Lionel Blanc, Guillermo A. Blanco, Heidi Kiil Blomhoff, Emilio Boada Romero, Stefan Böckler, Marianne Boes, Kathleen Boesze Battaglia, Lawrence H. Boise, Alessandra Bolino, Andrea Boman, Paolo Bonaldo, Matteo Bordi, Jürgen Bosch, Luis M. Botana, Joelle Botti, German Bou, Marina Bouché, Marion Bouchecareilh, Marie Josée Boucher, Michael E. Boulton, Sebastien G. Bouret, Patricia Boya, Michaël Boyer Guittaut, Peter V. Bozhkov, Nathan Brady, Vania MM Braga, Claudio Brancolini, Gerhard H. Braus, José M. Bravo San Pedro, Lisa A. Brennan, Emery H. Bresnick, Patrick Brest, Dave Bridges, MarieAgnès Bringer, Marisa Brini, Glauber C. Brito, Bertha Brodin, Paul S. Brookes, Eric J. Brown, Karen Brown, Hal E. Broxmeyer, Alain Bruhat, Patricia Chakur Brum, John H. Brumell, Nicola Brunetti Pierri, Robert J. Bryson Richardson, Shilpa Buch, Alastair M. Buchan, Hikmet Budak, Dmitry V. Bulavin, Scott J. Bultman, Geert Bultynck, Vladimir Bumbasirevic, Yan Burelle, Robert E. Burke, Margit Burmeister, Peter Bütikofer, Laura Caberlotto, Ken Cadwell, Monika Cahova, Dongsheng Cai, Jingjing Cai, Qian Cai, Sara Calatayud, Nadine Camougrand, Michelangelo Campanella, Grant R. Campbell, Matthew Campbell, Silvia Campello, Robin Candau, Isabella Caniggia, Lavinia Cantoni, Lizhi Cao, Allan B. Caplan, Michele Caraglia, Claudio Cardinali, Sandra Morais Cardoso, Jennifer S. Carew, Laura A. Carleton, Cathleen R. Carlin, Silvia Carloni, Sven R. Carlsson, Didac Carmona Gutierrez, Leticia AM Carneiro, Oliana Carnevali, Serena Carra, Alice Carrier, Bernadette Carroll, Caty Casas, Josefina Casas, Giuliana Cassinelli, Perrine Castets, Susana Castro Obregon, Gabriella Cavallini, Isabella Ceccherini, Francesco Cecconi, Arthur I. Cederbaum, Valentín Ceña, Simone Cenci, Claudia Cerella, Davide Cervia, CETRULLO, SILVIA, Hassan Chaachouay, Han Jung Chae, Andrei S. Chagin, Chee Yin Chai, Gopal Chakrabarti, Georgios Chamilos, Edmond YW Chan, Matthew TV Chan, Dhyan Chandra, Pallavi Chandra, Chih Peng Chang, Raymond Chuen Chung Chang, Ta Yuan Chang, John C. Chatham, Saurabh Chatterjee, Santosh Chauhan, Yongsheng Che, Michael E. Cheetham, Rajkumar Cheluvappa, Chun Jung Chen, Gang Chen, Guang Chao Chen, Guoqiang Chen, Hongzhuan Chen, Jeff W. Chen, Jian Kang Chen, Min Chen, Mingzhou Chen, Peiwen Chen, Qi Chen, Quan Chen, Shang Der Chen, Si Chen, Steve S. L. Chen, Wei Chen, Wei Jung Chen, Wen Qiang Chen, Wenli Chen, Xiangmei Chen, Yau Hung Chen, Ye Guang Chen, Yin Chen, Yingyu Chen, Yongshun Chen, Yu Jen Chen, Yue Qin Chen, Yujie Chen, Zhen Chen, Zhong Chen, Alan Cheng, Christopher HK Cheng, Hua Cheng, Heesun Cheong, Sara Cherry, Jason Chesney, Chun Hei Antonio Cheung, Eric Chevet, Hsiang Cheng Chi, Sung Gil Chi, Fulvio Chiacchiera, Hui Ling Chiang, Roberto Chiarelli, Mario Chiariello, Marcello Chieppa, Lih Shen Chin, Mario Chiong, Gigi NC Chiu, Dong Hyung Cho, Ssang Goo Cho, William C. Cho, Yong Yeon Cho, Young Seok Cho, Augustine MK Choi, Eui Ju Choi, Eun Kyoung Choi, Jayoung Choi, Mary E. Choi, Seung Il Choi, Tsui Fen Chou, Salem Chouaib, Divaker Choubey, Vinay Choubey, Kuan Chih Chow, Kamal Chowdhury, Charleen T. Chu, Tsung Hsien Chuang, Taehoon Chun, Hyewon Chung, Taijoon Chung, Yuen Li Chung, Yong Joon Chwae, Valentina Cianfanelli, Roberto Ciarcia, Iwona A. Ciechomska, Maria Rosa Ciriolo, Mara Cirone, Sofie Claerhout, Michael J. Clague, Joan Clària, Peter GH Clarke, Robert Clarke, Emilio Clementi, Cédric Cleyrat, Miriam Cnop, Eliana M. Coccia, Tiziana Cocco, Patrice Codogno, Jörn Coers, Ezra EW Cohen, David Colecchia, Luisa Coletto, Núria S. Coll, Emma Colucci Guyon, Sergio Comincini, Maria Condello, Katherine L. Cook, Graham H. Coombs, Cynthia D. Cooper, J. Mark Cooper, Isabelle Coppens, Maria Tiziana Corasaniti, Marco Corazzari, Ramon Corbalan, Elisabeth Corcelle Termeau, Mario D. Cordero, Cristina Corral Ramos, Olga Corti, Andrea Cossarizza, Paola Costelli, Safia Costes, Susan L. Cotman, Ana Coto Montes, Sandra Cottet, Eduardo Couve, Lori R. Covey, L. Ashley Cowart, Jeffery S. Cox, Fraser P. Coxon, Carolyn B. Coyne, Mark S. Cragg, Rolf J. Craven, Tiziana Crepaldi, Jose L. Crespo, Alfredo Criollo, Valeria Crippa, Maria Teresa Cruz, Ana Maria Cuervo, Jose M. Cuezva, Taixing Cui, Pedro R. Cutillas, Mark J. Czaja, Maria F. Czyzyk Krzeska, Ruben K. Dagda, Uta Dahmen, Chunsun Dai, Wenjie Dai, Yun Dai, Kevin N. Dalby, Luisa Dalla Valle, Guillaume Dalmasso, Marcello D'Amelio, Markus Damme, Arlette Darfeuille Michaud, Catherine Dargemont, Victor M. Darley Usmar, Srinivasan Dasarathy, Biplab Dasgupta, Srikanta Dash, Crispin R. Dass, Hazel Marie Davey, Lester M. Davids, David Dávila, Roger J. Davis, Ted M. Dawson, Valina L. Dawson, Paula Daza, Jackie de Belleroche, Paul de Figueiredo, Regina Celia Bressan Queiroz de Figueiredo, José de la Fuente, Luisa De Martino, Antonella De Matteis, Guido RY De Meyer, Angelo De Milito, Mauro De Santi, Wanderley de Souza, Vincenzo De Tata, Daniela De Zio, Jayanta Debnath, Reinhard Dechant, Jean Paul Decuypere, Shane Deegan, Benjamin Dehay, Barbara Del Bello, Dominic P. Del Re, Régis Delage Mourroux, Lea MD Delbridge, Louise Deldicque, Elizabeth Delorme Axford, Yizhen Deng, Joern Dengjel, Melanie Denizot, Paul Dent, Channing J. Der, Vojo Deretic, Benoît Derrien, Eric Deutsch, Timothy P. Devarenne, Rodney J. Devenish, Sabrina Di Bartolomeo, Nicola Di Daniele, Fabio Di Domenico, Alessia Di Nardo, Simone Di Paola, Antonio Di Pietro, Livia Di Renzo, Aaron DiAntonio, Guillermo Díaz Araya, Ines Díaz Laviada, Maria T. Diaz Meco, Javier Diaz Nido, Chad A. Dickey, Robert C. Dickson, Marc Diederich, Paul Digard, Ivan Dikic, Savithrama P. Dinesh Kumar, Chan Ding, Wen Xing Ding, Zufeng Ding, Luciana Dini, Jörg HW Distler, Abhinav Diwan, Mojgan Djavaheri Mergny, Kostyantyn Dmytruk, Renwick CJ Dobson, Volker Doetsch, Karol Dokladny, Svetlana Dokudovskaya, Massimo Donadelli, X. Charlie Dong, Xiaonan Dong, Zheng Dong, Terrence M. Donohue Jr, Kelly S. Doran, Gabriella D'Orazi, Gerald W. Dorn II, Victor Dosenko, Sami Dridi, Liat Drucker, Jie Du, Li Lin Du, Lihuan Du, André du Toit, Priyamvada Dua, Lei Duan, Pu Duann, Vikash Kumar Dubey, Michael R. Duchen, Michel A. Duchosal, Helene Duez, Isabelle Dugail, Verónica I. Dumit, Mara C. Duncan, Elaine A. Dunlop, William A. Dunn Jr, Nicolas Dupont, Luc Dupuis, Raúl V. Durán, Thomas M. Durcan, Stéphane Duvezin Caubet, Umamaheswar Duvvuri, Vinay Eapen, Darius Ebrahimi Fakhari, Arnaud Echard, Leopold Eckhart, Charles L. Edelstein, Aimee L. Edinger, Ludwig Eichinger, Tobias Eisenberg, Avital Eisenberg Lerner, N. Tony Eissa, Wafik S. El Deiry, Victoria El Khoury, Zvulun Elazar, Hagit Eldar Finkelman, Chris JH Elliott, Enzo Emanuele, Urban Emmenegger, Nikolai Engedal, Anna Mart Engelbrecht, Simone Engelender, Jorrit M. Enserink, Ralf Erdmann, Jekaterina Erenpreisa, Rajaraman Eri, Jason L. Eriksen, Andreja Erman, Ricardo Escalante, Eeva Liisa Eskelinen, Lucile Espert, Lorena Esteban Martínez, Thomas J. Evans, Mario Fabri, Gemma Fabrias, Cinzia Fabrizi, Antonio Facchiano, Nils J. Færgeman, Alberto Faggioni, W. Douglas Fairlie, Chunhai Fan, Daping Fan, Jie Fan, Shengyun Fang, Manolis Fanto, Alessandro Fanzani, Thomas Farkas, Mathias Faure, Francois B. Favier, Howard Fearnhead, Massimo Federici, Erkang Fei, Tania C. Felizardo, Hua Feng, Yibin Feng, Yuchen Feng, Thomas A. Ferguson, Álvaro F. Fernández, Maite G. Fernandez Barrena, Jose C. Fernandez Checa, Arsenio Fernández López, Martin E. Fernandez Zapico, Olivier Feron, Elisabetta Ferraro, Carmen Veríssima Ferreira Halder, Laszlo Fesus, Ralph Feuer, Fabienne C. Fiesel, Eduardo C. Filippi Chiela, Giuseppe Filomeni, Gian Maria Fimia, John H. Fingert, Steven Finkbeiner, Toren Finkel, Filomena Fiorito, Paul B. Fisher, Marc Flajolet, FLAMIGNI, FLAVIO, Oliver Florey, Salvatore Florio, R. Andres Floto, Marco Folini, Carlo Follo, Edward A. Fon, Francesco Fornai, Franco Fortunato, Alessandro Fraldi, Rodrigo Franco, Arnaud Francois, Aurélie François, Lisa B. Frankel, Iain DC Fraser, Norbert Frey, Damien G. Freyssenet, Christian Frezza, Scott L. Friedman, Daniel E. Frigo, Dongxu Fu, José M. Fuentes, Juan Fueyo, Yoshio Fujitani, Yuuki Fujiwara, Mikihiro Fujiya, Mitsunori Fukuda, Simone Fulda, Carmela Fusco, Bozena Gabryel, Matthias Gaestel, Philippe Gailly, Malgorzata Gajewska, Sehamuddin Galadari, Gad Galili, Inmaculada Galindo, Maria F. Galindo, Giovanna Galliciotti, Lorenzo Galluzzi, Luca Galluzzi, Vincent Galy, Noor Gammoh, Sam Gandy, Anand K. Ganesan, Swamynathan Ganesan, Ian G. Ganley, Monique Gannagé, Fen Biao Gao, Feng Gao, Jian Xin Gao, Lorena García Nannig, Eleonora García Véscovi, Marina Garcia Macía, Carmen Garcia Ruiz, Abhishek D. Garg, Pramod Kumar Garg, Ricardo Gargini, Nils Christian Gassen, Damián Gatica, Evelina Gatti, Julie Gavard, Evripidis Gavathiotis, Liang Ge, Pengfei Ge, Shengfang Ge, Po Wu Gean, Vania Gelmetti, Armando A. Genazzani, Jiefei Geng, Pascal Genschik, Lisa Gerner, Jason E. Gestwicki, David A. Gewirtz, Saeid Ghavami, Eric Ghigo, Debabrata Ghosh, Anna Maria Giammarioli, Francesca Giampieri, Claudia Giampietri, Alexandra Giatromanolaki, Derrick J. Gibbings, Lara Gibellini, Spencer B. Gibson, Vanessa Ginet, Antonio Giordano, Flaviano Giorgini, Elisa Giovannetti, Stephen E. Girardin, Suzana Gispert, Sandy Giuliano, Candece L. Gladson, Alvaro Glavic, Martin Gleave, Nelly Godefroy, Robert M. Gogal Jr, Kuppan Gokulan, Gustavo H. Goldman, Delia Goletti, Michael S. Goligorsky, Aldrin V. Gomes, Ligia C. Gomes, Hernando Gomez, Candelaria Gomez Manzano, Rubén Gómez Sánchez, Dawit AP Gonçalves, Ebru Goncu, Qingqiu Gong, Céline Gongora, Carlos B. Gonzalez, Pedro Gonzalez Alegre, Pilar Gonzalez Cabo, Rosa Ana González Polo, Ing Swie Goping, Carlos Gorbea, Nikolai V. Gorbunov, Daphne R. Goring, Adrienne M. Gorman, Sharon M. Gorski, Sandro Goruppi, Shino Goto Yamada, Cecilia Gotor, Roberta A. Gottlieb, Illana Gozes, Devrim Gozuacik, Yacine Graba, Martin Graef, Giovanna E. Granato, Gary Dean Grant, Steven Grant, Giovanni Luca Gravina, Douglas R. Green, Alexander Greenhough, Michael T. Greenwood, Benedetto Grimaldi, Frédéric Gros, Charles Grose, Jean Francois Groulx, Florian Gruber, Paolo Grumati, Tilman Grune, Jun Lin Guan, Kun Liang Guan, Barbara Guerra, Carlos Guillen, Kailash Gulshan, Jan Gunst, Chuanyong Guo, Lei Guo, Ming Guo, Wenjie Guo, Xu Guang Guo, Andrea A. Gust, Åsa B. Gustafsson, Elaine Gutierrez, Maximiliano G. Gutierrez, Ho Shin Gwak, Albert Haas, James E. Haber, Shinji Hadano, Monica Hagedorn, David R. Hahn, Andrew J. Halayko, Anne Hamacher Brady, Kozo Hamada, Ahmed Hamai, Andrea Hamann, Maho Hamasaki, Isabelle Hamer, Qutayba Hamid, Ester M. Hammond, Feng Han, Weidong Han, James T. Handa, John A. Hanover, Malene Hansen, Masaru Harada, Ljubica Harhaji Trajkovic, J. Wade Harper, Abdel Halim Harrath, Adrian L. Harris, James Harris, Udo Hasler, Peter Hasselblatt, Kazuhisa Hasui, Robert G. Hawley, Teresa S. Hawley, Congcong He, Cynthia Y. He, Fengtian He, Gu He, Rong Rong He, Xian Hui He, You Wen He, Yu Ying He, Joan K. Heath, Marie Josée Hébert, Robert A. Heinzen, Gudmundur Vignir Helgason, Michael Hensel, Elizabeth P. Henske, Chengtao Her, Paul K. Herman, Agustín Hernández, Carlos Hernandez, Sonia Hernández Tiedra, Claudio Hetz, P. Robin Hiesinger, Katsumi Higaki, Sabine Hilfiker, Bradford G. Hill, Joseph A. Hill, William D. Hill, Keisuke Hino, Daniel Hofius, Paul Hofman, Günter U. Höglinger, Jörg Höhfeld, Marina K. Holz, Yonggeun Hong, David A. Hood, Jeroen JM Hoozemans, Thorsten Hoppe, Chin Hsu, Chin Yuan Hsu, Li Chung Hsu, Dong Hu, Guochang Hu, Hong Ming Hu, Hongbo Hu, Ming Chang Hu, Yu Chen Hu, Zhuo Wei Hu, Fang Hua, Ya Hua, Canhua Huang, Huey Lan Huang, Kuo How Huang, Kuo Yang Huang, Shile Huang, Shiqian Huang, Wei Pang Huang, Yi Ran Huang, Yong Huang, Yunfei Huang, Tobias B. Huber, Patricia Huebbe, Won Ki Huh, Juha J. Hulmi, Gang Min Hur, James H. Hurley, Zvenyslava Husak, Sabah NA Hussain, Salik Hussain, Jung Jin Hwang, Seungmin Hwang, Thomas IS Hwang, Atsuhiro Ichihara, Yuzuru Imai, Carol Imbriano, Megumi Inomata, Takeshi Into, Valentina Iovane, Juan L. Iovanna, Renato V. Iozzo, Nancy Y. Ip, Javier E. Irazoqui, Pablo Iribarren, Yoshitaka Isaka, Aleksandra J. Isakovic, Harry Ischiropoulos, Jeffrey S. Isenberg, Mohammad Ishaq, Hiroyuki Ishida, Isao Ishii, Jane E. Ishmael, Ciro Isidoro, Ken ichi Isobe, Erika Isono, Shohreh Issazadeh Navikas, Koji Itahana, Eisuke Itakura, Andrei I. Ivanov, Anand Krishnan V. Iyer, José M. Izquierdo, Yotaro Izumi, Valentina Izzo, Marja Jäättelä, Nadia Jaber, Daniel John Jackson, William T. Jackson, Tony George Jacob, Thomas S. Jacques, Chinnaswamy Jagannath, Ashish Jain, Nihar Ranjan Jana, Byoung Kuk Jang, Alkesh Jani, Bassam Janji, Paulo Roberto Jannig, Patric J. Jansson, Steve Jean, Marina Jendrach, Ju Hong Jeon, Niels Jessen, Eui Bae Jeung, Kailiang Jia, Lijun Jia, Hong Jiang, Hongchi Jiang, Liwen Jiang, Teng Jiang, Xiaoyan Jiang, Xuejun Jiang, Ying Jiang, Yongjun Jiang, Alberto Jiménez, Cheng Jin, Hongchuan Jin, Lei Jin, Meiyan Jin, Shengkan Jin, Umesh Kumar Jinwal, Eun Kyeong Jo, Terje Johansen, Daniel E. Johnson, Gail VW Johnson, James D. Johnson, Eric Jonasch, Chris Jones, Leo AB Joosten, Joaquin Jordan, Anna Maria Joseph, Bertrand Joseph, Annie M. Joubert, Dianwen Ju, Jingfang Ju, Hsueh Fen Juan, Katrin Juenemann, Gábor Juhász, Hye Seung Jung, Jae U. Jung, Yong Keun Jung, Heinz Jungbluth, Matthew J. Justice, Barry Jutten, Nadeem O. Kaakoush, Kai Kaarniranta, Allen Kaasik, Tomohiro Kabuta, Bertrand Kaeffer, Katarina Kågedal, Alon Kahana, Shingo Kajimura, Or Kakhlon, Manjula Kalia, Dhan V. Kalvakolanu, Yoshiaki Kamada, Konstantinos Kambas, Vitaliy O. Kaminskyy, Harm H. Kampinga, Mustapha Kandouz, Chanhee Kang, Rui Kang, Tae Cheon Kang, Tomotake Kanki, Thirumala Devi Kanneganti, Haruo Kanno, Anumantha G. Kanthasamy, Marc Kantorow, Maria Kaparakis Liaskos, Orsolya Kapuy, Vassiliki Karantza, Md Razaul Karim, Parimal Karmakar, Arthur Kaser, Susmita Kaushik, Thomas Kawula, A. Murat Kaynar, Po Yuan Ke, Zun Ji Ke, John H. Kehrl, Kate E. Keller, Jongsook Kim Kemper, Anne K. Kenworthy, Oliver Kepp, Andreas Kern, Santosh Kesari, David Kessel, Robin Ketteler, Isis do Carmo Kettelhut, Bilon Khambu, Muzamil Majid Khan, Vinoth KM Khandelwal, Sangeeta Khare, Juliann G. Kiang, Amy A. Kiger, Akio Kihara, Arianna L. Kim, Cheol Hyeon Kim, Deok Ryong Kim, Do Hyung Kim, Eung Kweon Kim, Hye Young Kim, Hyung Ryong Kim, Jae Sung Kim, Jeong Hun Kim, Jin Cheon Kim, Jin Hyoung Kim, Kwang Woon Kim, Michael D. Kim, Moon Moo Kim, Peter K. Kim, Seong Who Kim, Soo Youl Kim, Yong Sun Kim, Yonghyun Kim, Adi Kimchi, Alec C. Kimmelman, Tomonori Kimura, Jason S. King, Karla Kirkegaard, Vladimir Kirkin, Lorrie A. Kirshenbaum, Shuji Kishi, Yasuo Kitajima, Katsuhiko Kitamoto, Yasushi Kitaoka, Kaio Kitazato, Rudolf A. Kley, Walter T. Klimecki, Michael Klinkenberg, Jochen Klucken, Helene Knævelsrud, Erwin Knecht, Laura Knuppertz, Jiunn Liang Ko, Satoru Kobayashi, Jan C. Koch, Christelle Koechlin Ramonatxo, Ulrich Koenig, Young Ho Koh, Katja Köhler, Sepp D. Kohlwein, Masato Koike, Masaaki Komatsu, Eiki Kominami, Dexin Kong, Hee Jeong Kong, Eumorphia G. Konstantakou, Benjamin T. Kopp, Tamas Korcsmaros, Laura Korhonen, Viktor I. Korolchuk, Nadya V. Koshkina, Yanjun Kou, Michael I. Koukourakis, Constantinos Koumenis, Attila L. Kovács, Tibor Kovács, Werner J. Kovacs, Daisuke Koya, Claudine Kraft, Dimitri Krainc, Helmut Kramer, Tamara Kravic Stevovic, Wilhelm Krek, Carole Kretz Remy, Roswitha Krick, Malathi Krishnamurthy, Janos Kriston Vizi, Guido Kroemer, Michael C. Kruer, Rejko Kruger, Nicholas T. Ktistakis, Kazuyuki Kuchitsu, Christian Kuhn, Addanki Pratap Kumar, Anuj Kumar, Ashok Kumar, Deepak Kumar, Dhiraj Kumar, Rakesh Kumar, Sharad Kumar, Mondira Kundu, Hsing Jien Kung, Atsushi Kuno, Sheng Han Kuo, Jeff Kuret, Tino Kurz, Terry Kwok, Taeg Kyu Kwon, Yong Tae Kwon, Irene Kyrmizi, Albert R. La Spada, Frank Lafont, Tim Lahm, Aparna Lakkaraju, Truong Lam, Trond Lamark, Steve Lancel, Terry H. Landowski, Darius JR Lane, Jon D. Lane, Cinzia Lanzi, Pierre Lapaquette, Louis R. Lapierre, Jocelyn Laporte, Johanna Laukkarinen, Gordon W. Laurie, Sergio Lavandero, Lena Lavie, Matthew J. LaVoie, Betty Yuen Kwan Law, Helen Ka wai Law, Kelsey B. Law, Robert Layfield, Pedro A. Lazo, Laurent Le Cam, Karine G. Le Roch, Hervé Le Stunff, Vijittra Leardkamolkarn, Marc Lecuit, Byung Hoon Lee, Che Hsin Lee, Erinna F. Lee, Gyun Min Lee, He Jin Lee, Hsinyu Lee, Jae Keun Lee, Jongdae Lee, Juhyun Lee, Jun Hee Lee, Michael Lee, Myung Shik Lee, Patty J. Lee, Sam W. Lee, Seung Jae Lee, Shiow Ju Lee, Stella Y. Lee, Sug Hyung Lee, Sung Sik Lee, Sung Joon Lee, Sunhee Lee, Ying Ray Lee, Yong J. Lee, Young H. Lee, Christiaan Leeuwenburgh, Sylvain Lefort, Renaud Legouis, Jinzhi Lei, Qun Ying Lei, David A. Leib, Gil Leibowitz, Istvan Lekli, Stéphane D. Lemaire, John J. Lemasters, Marius K. Lemberg, Antoinette Lemoine, Shuilong Leng, Guido Lenz, Paola Lenzi, Lilach O. Lerman, Daniele Lettieri Barbato, Julia I. Ju Leu, Hing Y. Leung, Beth Levine, Patrick A. Lewis, Frank Lezoualc'h, Chi Li, Faqiang Li, Feng Jun Li, Jun Li, Ke Li, Lian Li, Min Li, Qiang Li, Rui Li, Sheng Li, Wei Li, Xiaotao Li, Yumin Li, Jiqin Lian, Chengyu Liang, Qiangrong Liang, Yulin Liao, Joana Liberal, Pawel P. Liberski, Pearl Lie, Andrew P. Lieberman, Hyunjung Jade Lim, Kah Leong Lim, Kyu Lim, Raquel T. Lima, Chang Shen Lin, Chiou Feng Lin, Fang Lin, Fangming Lin, Fu Cheng Lin, Kui Lin, Kwang Huei Lin, Pei Hui Lin, Tianwei Lin, Wan Wan Lin, Yee Shin Lin, Yong Lin, Rafael Linden, Dan Lindholm, Lisa M. Lindqvist, Paul Lingor, Andreas Linkermann, Lance A. Liotta, Marta M. Lipinski, Vitor A. Lira, Michael P. Lisanti, Paloma B. Liton, Bo Liu, Chong Liu, Chun Feng Liu, Fei Liu, Hung Jen Liu, Jianxun Liu, Jing Jing Liu, Jing Lan Liu, Ke Liu, Leyuan Liu, Liang Liu, Quentin Liu, Rong Yu Liu, Shiming Liu, Shuwen Liu, Wei Liu, Xian De Liu, Xiangguo Liu, Xiao Hong Liu, Xinfeng Liu, Xu Liu, Xueqin Liu, Yang Liu, Yule Liu, Zexian Liu, Zhe Liu, Juan P. Liuzzi, Gérard Lizard, Mila Ljujic, Irfan J. Lodhi, Susan E. Logue, Bal L. Lokeshwar, Yun Chau Long, Sagar Lonial, Benjamin Loos, Carlos López Otín, Cristina López Vicario, Mar Lorente, Philip L. Lorenzi, Péter Lõrincz, Marek Los, Michael T. Lotze, Penny E. Lovat, Binfeng Lu, Bo Lu, Jiahong Lu, Qing Lu, She Min Lu, Shuyan Lu, Yingying Lu, Frédéric Luciano, Shirley Luckhart, John Milton Lucocq, Paula Ludovico, Aurelia Lugea, Nicholas W. Lukacs, Julian J. Lum, Anders H. Lund, Honglin Luo, Jia Luo, Shouqing Luo, Claudio Luparello, Timothy Lyons, Jianjie Ma, Yi Ma, Yong Ma, Zhenyi Ma, Juliano Machado, Glaucia M. Machado Santelli, Fernando Macian, Gustavo C. MacIntosh, Jeffrey P. MacKeigan, Kay F. Macleod, John D. MacMicking, Lee Ann MacMillan Crow, Frank Madeo, Muniswamy Madesh, Julio Madrigal Matute, Akiko Maeda, Tatsuya Maeda, Gustavo Maegawa, Emilia Maellaro, Hannelore Maes, Marta Magariños, Kenneth Maiese, Tapas K. Maiti, Luigi Maiuri, Maria Chiara Maiuri, Carl G. Maki, Roland Malli, Walter Malorni, Alina Maloyan, Fathia Mami Chouaib, Na Man, Joseph D. Mancias, Eva Maria Mandelkow, Michael A. Mandell, Angelo A. Manfredi, Serge N. Manié, Claudia Manzoni, Kai Mao, Zixu Mao, Zong Wan Mao, Philippe Marambaud, Anna Maria Marconi, Zvonimir Marelja, Gabriella Marfe, Marta Margeta, Eva Margittai, Muriel Mari, Francesca V. Mariani, Concepcio Marin, Sara Marinelli, Guillermo Mariño, Ivanka Markovic, Rebecca Marquez, MARTELLI, ALBERTO MARIA, Sascha Martens, Katie R. Martin, Seamus J. Martin, Shaun Martin, Miguel A. Martin Acebes, Paloma Martín Sanz, Camille Martinand Mari, Wim Martinet, Jennifer Martinez, Nuria Martinez Lopez, Ubaldo Martinez Outschoorn, Moisés Martínez Velázquez, Marta Martinez Vicente, Waleska Kerllen Martins, Hirosato Mashima, James A. Mastrianni, Giuseppe Matarese, Paola Matarrese, Roberto Mateo, Satoaki Matoba, Naomichi Matsumoto, Takehiko Matsushita, Akira Matsuura, Takeshi Matsuzawa, Mark P. Mattson, Soledad Matus, Norma Maugeri, Caroline Mauvezin, Andreas Mayer, Dusica Maysinger, Guillermo D. Mazzolini, Mary Kate McBrayer, Kimberly McCall, Craig McCormick, Gerald M. McInerney, Skye C. McIver, Sharon McKenna, John J. McMahon, Iain A. McNeish, Fatima Mechta Grigoriou, Jan Paul Medema, Diego L. Medina, Klara Megyeri, Maryam Mehrpour, Jawahar L. Mehta, Yide Mei, Ute Christiane Meier, Alfred J. Meijer, Alicia Meléndez, Gerry Melino, Sonia Melino, Edesio Jose Tenorio de Melo, Maria A. Mena, Marc D. Meneghini, Javier A. Menendez, Regina Menezes, Liesu Meng, Ling hua Meng, Songshu Meng, Rossella Menghini, A. Sue Menko, Rubem FS Menna Barreto, Manoj B. Menon, Marco A. Meraz Ríos, Giuseppe Merla, Luciano Merlini, Angelica M. Merlot, Andreas Meryk, Stefania Meschini, Joel N. Meyer, Man tian Mi, Chao Yu Miao, Lucia Micale, Simon Michaeli, Carine Michiels, FRANCO MIGLIACCIO, ANNA RITA, Anastasia Susie Mihailidou, Dalibor Mijaljica, Katsuhiko Mikoshiba, Enrico Milan, Leonor Miller Fleming, Gordon B. Mills, Ian G. Mills, Georgia Minakaki, Berge A. Minassian, Xiu Fen Ming, Farida Minibayeva, Elena A. Minina, Justine D. Mintern, Saverio Minucci, Antonio Miranda Vizuete, Claire H. Mitchell, Shigeki Miyamoto, Keisuke Miyazawa, Noboru Mizushima, Katarzyna Mnich, Baharia Mograbi, Simin Mohseni, Luis Ferreira Moita, Marco Molinari, Maurizio Molinari, Andreas Buch Møller, Bertrand Mollereau, Faustino Mollinedo, Marco Mongillo, Martha M. Monick, Serena Montagnaro, Craig Montell, Darren J. Moore, Michael N. Moore, Rodrigo Mora Rodriguez, Paula I. Moreira, Etienne Morel, Maria Beatrice Morelli, Sandra Moreno, Michael J. Morgan, Arnaud Moris, Yuji Moriyasu, Janna L. Morrison, Lynda A. Morrison, Eugenia Morselli, Jorge Moscat, Pope L. Moseley, Serge Mostowy, Elisa Motori, Denis Mottet, Jeremy C. Mottram, Charbel E. H. Moussa, Vassiliki E. Mpakou, Hasan Mukhtar, Jean M. Mulcahy Levy, Sylviane Muller, Raquel Muñoz Moreno, Cristina Muñoz Pinedo, Christian Münz, Maureen E. Murphy, James T. Murray, Aditya Murthy, Indira U. Mysorekar, Ivan R. Nabi, Massimo Nabissi, Gustavo A. Nader, Yukitoshi Nagahara, Yoshitaka Nagai, Kazuhiro Nagata, Anika Nagelkerke, Péter Nagy, Samisubbu R. Naidu, Sreejayan Nair, Hiroyasu Nakano, Hitoshi Nakatogawa, Meera Nanjundan, Gennaro Napolitano, Naweed I. Naqvi, Roberta Nardacci, Derek P. Narendra, Masashi Narita, Anna Chiara Nascimbeni, Ramesh Natarajan, Luiz C. Navegantes, Steffan T. Nawrocki, Taras Y. Nazarko, Volodymyr Y. Nazarko, Thomas Neill, Luca M. Neri, Mihai G. Netea, Romana T. Netea Maier, Bruno M. Neves, Paul A. Ney, Ioannis P. Nezis, Hang TT Nguyen, Huu Phuc Nguyen, Anne Sophie Nicot, Hilde Nilsen, Per Nilsson, Mikio Nishimura, Ichizo Nishino, Mireia Niso Santano, Hua Niu, Ralph A. Nixon, Vincent CO Njar, Takeshi Noda, Angelika A. Noegel, Elsie Magdalena Nolte, Erik Norberg, Koenraad K. Norga, Sakineh Kazemi Noureini, Shoji Notomi, Lucia Notterpek, Karin Nowikovsky, Nobuyuki Nukina, Thorsten Nürnberger, Valerie B. O'Donnell, Tracey O'Donovan, Peter J. O'Dwyer, Ina Oehme, Clara L. Oeste, Michinaga Ogawa, Besim Ogretmen, Yuji Ogura, Young J. Oh, Masaki Ohmuraya, Takayuki Ohshima, Rani Ojha, Koji Okamoto, Toshiro Okazaki, F. Javier Oliver, Karin Ollinger, Stefan Olsson, Daniel P. Orban, Paulina Ordonez, Idil Orhon, Laszlo Orosz, Eyleen J. O'Rourke, Helena Orozco, Angel L. Ortega, Elena Ortona, Laura D. Osellame, Junko Oshima, Shigeru Oshima, Heinz D. Osiewacz, Takanobu Otomo, Kinya Otsu, Jing hsiung James Ou, Tiago F. Outeiro, Dong yun Ouyang, Hongjiao Ouyang, Michael Overholtzer, Michelle A. Ozbun, P. Hande Ozdinler, Bulent Ozpolat, Consiglia Pacelli, Paolo Paganetti, Guylène Page, Gilles Pages, Ugo Pagnini, Beata Pajak, Stephen C. Pak, Karolina Pakos Zebrucka, Nazzy Pakpour, Zdena Palková, Francesca Palladino, Kathrin Pallauf, Nicolas Pallet, Marta Palmieri, Søren R. Paludan, Camilla Palumbo, Silvia Palumbo, Olatz Pampliega, Hongming Pan, Wei Pan, Theocharis Panaretakis, Aseem Pandey, Areti Pantazopoulou, Zuzana Papackova, Daniela L. Papademetrio, Issidora Papassideri, Alessio Papini, Nirmala Parajuli, Julian Pardo, Vrajesh V. Parekh, Giancarlo Parenti, Jong In Park, Junsoo Park, Ohkmae K. Park, Roy Parker, Rosanna Parlato, Jan B. Parys, Katherine R. Parzych, Jean Max Pasquet, Benoit Pasquier, Kishore BS Pasumarthi, Daniel Patschan, Cam Patterson, Sophie Pattingre, Scott Pattison, Arnim Pause, Hermann Pavenstädt, Flaminia Pavone, Zully Pedrozo, Fernando J. Peña, Miguel A. Peñalva, Mario Pende, Jianxin Peng, Fabio Penna, Josef M. Penninger, Anna Pensalfini, Salvatore Pepe, Gustavo JS Pereira, Paulo C. Pereira, Verónica Pérez de la Cruz, María Esther Pérez Pérez, Diego Pérez Rodríguez, Dolores Pérez Sala, Celine Perier, Andras Perl, David H. Perlmutter, Ida Perrotta, Shazib Pervaiz, Maija Pesonen, Jeffrey E. Pessin, Godefridus J. Peters, Morten Petersen, Irina Petrache, Basil J. Petrof, Goran Petrovski, James M. Phang, Mauro Piacentini, Marina Pierdominici, Philippe Pierre, Valérie Pierrefite Carle, Federico Pietrocola, Felipe X. Pimentel Muiños, Mario Pinar, Benjamin Pineda, Ronit Pinkas Kramarski, Marcello Pinti, Paolo Pinton, Bilal Piperdi, James M. Piret, Leonidas C. Platanias, Harald W. Platta, Edward D. Plowey, Stefanie Pöggeler, Marc Poirot, Peter Polčic, Angelo Poletti, Audrey H. Poon, Hana Popelka, Blagovesta Popova, Izabela Poprawa, Shibu M. Poulose, Joanna Poulton, Scott K. Powers, Ted Powers, Mercedes Pozuelo Rubio, Krisna Prak, Reinhild Prange, Mark Prescott, Muriel Priault, Sharon Prince, Richard L. Proia, Tassula Proikas Cezanne, Holger Prokisch, Vasilis J. Promponas, Karin Przyklenk, Rosa Puertollano, Subbiah Pugazhenthi, Luigi Puglielli, Aurora Pujol, Julien Puyal, Dohun Pyeon, Xin Qi, Wen bin Qian, Zheng Hong Qin, Yu Qiu, Ziwei Qu, Joe Quadrilatero, Frederick Quinn, Nina Raben, Hannah Rabinowich, Flavia Radogna, Michael J. Ragusa, Mohamed Rahmani, Komal Raina, Sasanka Ramanadham, Rajagopal Ramesh, Abdelhaq Rami, Sarron Randall Demllo, Felix Randow, Hai Rao, V. Ashutosh Rao, Blake B. Rasmussen, Tobias M. Rasse, Edward A. Ratovitski, Pierre Emmanuel Rautou, Swapan K. Ray, Babak Razani, Bruce H. Reed, Fulvio Reggiori, Markus Rehm, Andreas S. Reichert, Theo Rein, David J. Reiner, Eric Reits, Jun Ren, Xingcong Ren, Maurizio Renna, Jane EB Reusch, Jose L. Revuelta, Leticia Reyes, Alireza R. Rezaie, Robert I. Richards, Des R. Richardson, Clémence Richetta, Michael A. Riehle, Bertrand H. Rihn, Yasuko Rikihisa, Brigit E. Riley, Gerald Rimbach, Maria Rita Rippo, Konstantinos Ritis, Federica Rizzi, Elizete Rizzo, Peter J. Roach, Jeffrey Robbins, Michel Roberge, Gabriela Roca, Maria Carmela Roccheri, Sonia Rocha, Cecilia MP Rodrigues, Clara I. Rodríguez, Santiago Rodriguez de Cordoba, Natalia Rodriguez Muela, Jeroen Roelofs, Vladimir V. Rogov, Troy T. Rohn, Bärbel Rohrer, Davide Romanelli, Luigina Romani, Patricia Silvia Romano, M. Isabel G. Roncero, Jose Luis Rosa, Alicia Rosello, Kirill V. Rosen, Philip Rosenstiel, Magdalena Rost Roszkowska, Kevin A. Roth, Gael Roué, Mustapha Rouis, Kasper M. Rouschop, Daniel T. Ruan, Diego Ruano, David C. Rubinsztein, Edmund B. Rucker III, Assaf Rudich, Emil Rudolf, Ruediger Rudolf, Markus A. Ruegg, Carmen Ruiz Roldan, Avnika Ashok Ruparelia, Paola Rusmini, David W. Russ, Gian Luigi Russo, Giuseppe Russo, Rossella Russo, Tor Erik Rusten, Victoria Ryabovol, Kevin M. Ryan, Stefan W. Ryter, David M. Sabatini, Michael Sacher, Carsten Sachse, Michael N. Sack, Junichi Sadoshima, Paul Saftig, Ronit Sagi Eisenberg, Sumit Sahni, Pothana Saikumar, Tsunenori Saito, Tatsuya Saitoh, Koichi Sakakura, Machiko Sakoh Nakatogawa, Yasuhito Sakuraba, María Salazar Roa, Paolo Salomoni, Ashok K. Saluja, Paul M. Salvaterra, Rosa Salvioli, Afshin Samali, Anthony MJ Sanchez, José A. Sánchez Alcázar, Ricardo Sanchez Prieto, Marco Sandri, Miguel A. Sanjuan, Stefano Santaguida, Laura Santambrogio, Giorgio Santoni, Claudia Nunes dos Santos, Shweta Saran, Marco Sardiello, Graeme Sargent, Pallabi Sarkar, Sovan Sarkar, Maria Rosa Sarrias, Minnie M. Sarwal, Chihiro Sasakawa, Motoko Sasaki, Miklos Sass, Ken Sato, Miyuki Sato, Joseph Satriano, Niramol Savaraj, Svetlana Saveljeva, Liliana Schaefer, Ulrich E. Schaible, Michael Scharl, Hermann M. Schatzl, Randy Schekman, Wiep Scheper, Alfonso Schiavi, Hyman M. Schipper, Hana Schmeisser, Jens Schmidt, Ingo Schmitz, Bianca E. Schneider, E. Marion Schneider, Jaime L. Schneider, Eric A. Schon, Miriam J. Schönenberger, Axel H. Schönthal, Daniel F. Schorderet, Bernd Schröder, Sebastian Schuck, Ryan J. Schulze, Melanie Schwarten, Thomas L. Schwarz, Sebastiano Sciarretta, Kathleen Scotto, A. Ivana Scovassi, Robert A. Screaton, Mark Screen, Hugo Seca, Simon Sedej, Laura Segatori, Nava Segev, Per O. Seglen, Jose M. Seguí Simarro, Juan Segura Aguilar, Ekihiro Seki, Iban Seiliez, Christian Sell, Clay F. Semenkovich, Gregg L. Semenza, Utpal Sen, Andreas L. Serra, Ana Serrano Puebla, Hiromi Sesaki, Takao Setoguchi, Carmine Settembre, John J. Shacka, Ayesha N. Shajahan Haq, Irving M. Shapiro, Shweta Sharma, Hua She, C. K. James Shen, Chiung Chyi Shen, Han Ming Shen, Sanbing Shen, Weili Shen, Rui Sheng, Xianyong Sheng, Zu Hang Sheng, Trevor G. Shepherd, Junyan Shi, Qiang Shi, Qinghua Shi, Yuguang Shi, Shusaku Shibutani, Kenichi Shibuya, Yoshihiro Shidoji, Jeng Jer Shieh, Chwen Ming Shih, Yohta Shimada, Shigeomi Shimizu, Dong Wook Shin, Mari L. Shinohara, Michiko Shintani, Takahiro Shintani, Tetsuo Shioi, Ken Shirabe, Ronit Shiri Sverdlov, Orian Shirihai, Gordon C. Shore, Chih Wen Shu, Deepak Shukla, Andriy A. Sibirny, Valentina Sica, Christina J. Sigurdson, Einar M. Sigurdsson, Puran Singh Sijwali, Beata Sikorska, Wilian A. Silveira, Sandrine Silvente Poirot, Gary A. Silverman, Jan Simak, Thomas Simmet, Anna Katharina Simon, Hans Uwe Simon, Cristiano Simone, Matias Simons, Anne Simonsen, Rajat Singh, Shivendra V. Singh, Shrawan K. Singh, Debasish Sinha, Sangita Sinha, Frank A. Sinicrope, Agnieszka Sirko, Kapil Sirohi, Balindiwe JN Sishi, Annie Sittler, Parco M. Siu, Efthimios Sivridis, Anna Skwarska, Ruth Slack, Iva Slaninová, Nikolai Slavov, Soraya S. Smaili, Keiran SM Smalley, Duncan R. Smith, Stefaan J. Soenen, Scott A. Soleimanpour, Anita Solhaug, Kumaravel Somasundaram, Jin H. Son, Avinash Sonawane, Chunjuan Song, Fuyong Song, Hyun Kyu Song, Ju Xian Song, Wei Song, Kai Y. Soo, Anil K. Sood, Tuck Wah Soong, Virawudh Soontornniyomkij, Maurizio Sorice, Federica Sotgia, David R. Soto Pantoja, Areechun Sotthibundhu, Maria João Sousa, Herman P. Spaink, Paul N. Span, Anne Spang, Janet D. Sparks, Peter G. Speck, Stephen A. Spector, Claudia D. Spies, Wolfdieter Springer, Daret St Clair, Alessandra Stacchiotti, Bart Staels, Michael T. Stang, Daniel T. Starczynowski, Petro Starokadomskyy, Clemens Steegborn, John W. Steele, Leonidas Stefanis, Joan Steffan, Christine M. Stellrecht, Harald Stenmark, Tomasz M. Stepkowski, Stęphan T. Stern, Craig Stevens, Brent R. Stockwell, Veronika Stoka, Zuzana Storchova, Björn Stork, Vassilis Stratoulias, Dimitrios J. Stravopodis, Pavel Strnad, Anne Marie Strohecker, Anna Lena Ström, Per Stromhaug, Jiri Stulik, Yu Xiong Su, Zhaoliang Su, Carlos S. Subauste, Srinivasa Subramaniam, Carolyn M. Sue, Sang Won Suh, Xinbing Sui, Supawadee Sukseree, David Sulzer, Fang Lin Sun, Jiaren Sun, Jun Sun, Shi Yong Sun, Yang Sun, Yi Sun, Yingjie Sun, Vinod Sundaramoorthy, Joseph Sung, Hidekazu Suzuki, Kuninori Suzuki, Naoki Suzuki, Tadashi Suzuki, Yuichiro J. Suzuki, Michele S. Swanson, Charles Swanton, Karl Swärd, Ghanshyam Swarup, Sean T. Sweeney, Paul W. Sylvester, Zsuzsanna Szatmari, Eva Szegezdi, Peter W. Szlosarek, Heinrich Taegtmeyer, Marco Tafani, Emmanuel Taillebourg, Stephen WG Tait, Krisztina Takacs Vellai, Yoshinori Takahashi, Szabolcs Takáts, Genzou Takemura, Nagio Takigawa, Nicholas J. Talbot, Elena Tamagno, Jerome Tamburini, Cai Ping Tan, Lan Tan, Mei Lan Tan, Ming Tan, Yee Joo Tan, Keiji Tanaka, Masaki Tanaka, Daolin Tang, Dingzhong Tang, Guomei Tang, Isei Tanida, Kunikazu Tanji, Bakhos A. Tannous, Jose A. Tapia, Inmaculada Tasset Cuevas, Marc Tatar, Iman Tavassoly, Nektarios Tavernarakis, Allen Taylor, Graham S. Taylor, Gregory A. Taylor, J. Paul Taylor, Mark J. Taylor, Elena V. Tchetina, Andrew R. Tee, Fatima Teixeira Clerc, Sucheta Telang, Tewin Tencomnao, Ba Bie Teng, Ru Jeng Teng, Faraj Terro, Gianluca Tettamanti, Arianne L. Theiss, Anne E. Theron, Kelly Jean Thomas, Marcos P. Thomé, Paul G. Thomes, Andrew Thorburn, Jeremy Thorner, Thomas Thum, Michael Thumm, Teresa LM Thurston, Ling Tian, Andreas Till, Jenny Pan yun Ting, Vladimir I. Titorenko, Lilach Toker, Stefano Toldo, Sharon A. Tooze, Ivan Topisirovic, Maria Lyngaas Torgersen, Liliana Torosantucci, Alicia Torriglia, Maria Rosaria Torrisi, Cathy Tournier, Roberto Towns, Vladimir Trajkovic, Leonardo H. Travassos, Gemma Triola, Durga Nand Tripathi, Daniela Trisciuoglio, Rodrigo Troncoso, Ioannis P. Trougakos, Anita C. Truttmann, Kuen Jer Tsai, Mario P. Tschan, Yi Hsin Tseng, Takayuki Tsukuba, Allan Tsung, Andrey S. Tsvetkov, Shuiping Tu, Hsing Yu Tuan, Marco Tucci, David A. Tumbarello, Boris Turk, Vito Turk, Robin FB Turner, Anders A. Tveita, Suresh C. Tyagi, Makoto Ubukata, Yasuo Uchiyama, Andrej Udelnow, Takashi Ueno, Midori Umekawa, Rika Umemiya Shirafuji, Benjamin R. Underwood, Christian Ungermann, Rodrigo P. Ureshino, Ryo Ushioda, Vladimir N. Uversky, Néstor L. Uzcátegui, Thomas Vaccari, Maria I. Vaccaro, Libuše Váchová, Helin Vakifahmetoglu Norberg, Rut Valdor, Enza Maria Valente, Francois Vallette, Angela M. Valverde, Greet Van den Berghe, Ludo Van Den Bosch, Gijs R. van den Brink, F. Gisou van der Goot, Ida J. van der Klei, Luc JW van der Laan, Wouter G. van Doorn, Marjolein van Egmond, Kenneth L. van Golen, Luc Van Kaer, Menno van Lookeren Campagne, Peter Vandenabeele, Wim Vandenberghe, Ilse Vanhorebeek, Isabel Varela Nieto, M. Helena Vasconcelos, Radovan Vasko, Demetrios G. Vavvas, Ignacio Vega Naredo, Guillermo Velasco, Athanassios D. Velentzas, Panagiotis D. Velentzas, Tibor Vellai, Edo Vellenga, Mikkel Holm Vendelbo, Kartik Venkatachalam, Natascia Ventura, Salvador Ventura, Patrícia ST Veras, Mireille Verdier, Beata G. Vertessy, Andrea Viale, Michel Vidal, Helena LA Vieira, Richard D. Vierstra, Nadarajah Vigneswaran, Neeraj Vij, Miquel Vila, Margarita Villar, Victor H. Villar, Joan Villarroya, Cécile Vindis, Giampietro Viola, Maria Teresa Viscomi, Giovanni Vitale, Dan T. Vogl, Olga V. Voitsekhovskaja, Clarissa von Haefen, Karin von Schwarzenberg, Daniel E. Voth, Valérie Vouret Craviari, Kristina Vuori, Jatin M. Vyas, Christian Waeber, Cheryl Lyn Walker, Mark J. Walker, Jochen Walter, Lei Wan, Xiangbo Wan, Bo Wang, Caihong Wang, Chao Yung Wang, Chengshu Wang, Chenran Wang, Chuangui Wang, Dong Wang, Fen Wang, Fuxin Wang, Guanghui Wang, Hai jie Wang, Haichao Wang, Hong Gang Wang, Hongmin Wang, Horng Dar Wang, Jing Wang, Junjun Wang, Mei Wang, Mei Qing Wang, Pei Yu Wang, Peng Wang, Richard C. Wang, Shuo Wang, Ting Fang Wang, Xian Wang, Xiao jia Wang, Xiao Wei Wang, Xin Wang, Xuejun Wang, Yan Wang, Yanming Wang, Ying Wang, Ying Jan Wang, Yipeng Wang, Yu Wang, Yu Tian Wang, Yuqing Wang, Zhi Nong Wang, Pablo Wappner, Carl Ward, Diane McVey Ward, Gary Warnes, Hirotaka Watada, Yoshihisa Watanabe, Kei Watase, Timothy E. Full Terms, Conditions of access, use can be found at h.t.t.p.:././.w.w.w. t.a.n.d.f.o.n.l.i.n.e. com/action/journalInformation?journalCode=kaup20 Download by: [Alma Mater Studiorum Università di Bologna] Date: 23 September 2016, At: 06:43 Weaver, Colin D. Weekes, Jiwu Wei, Thomas Weide, Conrad C. Weihl, Günther Weindl, Simone Nardin Weis, Longping Wen, Xin Wen, Yunfei Wen, Benedikt Westermann, Cornelia M. Weyand, Anthony R. White, Eileen White, J. Lindsay Whitton, Alexander J. Whitworth, Joëlle Wiels, Franziska Wild, Manon E. Wildenberg, Tom Wileman, Deepti Srinivas Wilkinson, Simon Wilkinson, Dieter Willbold, Chris Williams, Katherine Williams, Peter R. Williamson, Konstanze F. Winklhofer, Steven S. Witkin, Stephanie E. Wohlgemuth, Thomas Wollert, Ernst J. Wolvetang, Esther Wong, G. William Wong, Richard W. Wong, Vincent Kam Wai Wong, Elizabeth A. Woodcock, Karen L. Wright, Chunlai Wu, Defeng Wu, Gen Sheng Wu, Jian Wu, Junfang Wu, Mian Wu, Min Wu, Shengzhou Wu, William KK Wu, Yaohua Wu, Zhenlong Wu, Cristina PR Xavier, Ramnik J. Xavier, Gui Xian Xia, Tian Xia, Weiliang Xia, Yong Xia, Hengyi Xiao, Jian Xiao, Shi Xiao, Wuhan Xiao, Chuan Ming Xie, Zhiping Xie, Zhonglin Xie, Maria Xilouri, Yuyan Xiong, Chuanshan Xu, Congfeng Xu, Feng Xu, Haoxing Xu, Hongwei Xu, Jian Xu, Jianzhen Xu, Jinxian Xu, Liang Xu, Xiaolei Xu, Yangqing Xu, Ye Xu, Zhi Xiang Xu, Ziheng Xu, Yu Xue, Takahiro Yamada, Ai Yamamoto, Koji Yamanaka, Shunhei Yamashina, Shigeko Yamashiro, Bing Yan, Bo Yan, Xianghua Yan, Zhen Yan, Yasuo Yanagi, Dun Sheng Yang, Jin Ming Yang, Liu Yang, Minghua Yang, Pei Ming Yang, Peixin Yang, Qian Yang, Wannian Yang, Wei Yuan Yang, Xuesong Yang, Yi Yang, Ying Yang, Zhifen Yang, Zhihong Yang, Meng Chao Yao, Pamela J. Yao, Xiaofeng Yao, Zhenyu Yao, Zhiyuan Yao, Linda S. Yasui, Mingxiang Ye, Barry Yedvobnick, Behzad Yeganeh, Elizabeth S. Yeh, Patricia L. Yeyati, Fan Yi, Long Yi, Xiao Ming Yin, Calvin K. Yip, Yeong Min Yoo, Young Hyun Yoo, Seung Yong Yoon, Ken Ichi Yoshida, Tamotsu Yoshimori, Ken H. Young, Huixin Yu, Jane J. Yu, Jin Tai Yu, Jun Yu, Li Yu, W. Haung Yu, Xiao Fang Yu, Zhengping Yu, Junying Yuan, Zhi Min Yuan, Beatrice YJT Yue, Jianbo Yue, Zhenyu Yue, David N. Zacks, Eldad Zacksenhaus, Nadia Zaffaroni, Tania Zaglia, Zahra Zakeri, Vincent Zecchini, Jinsheng Zeng, Min Zeng, Qi Zeng, Antonis S. Zervos, Donna D. Zhang, Fan Zhang, Guo Zhang, Guo Chang Zhang, Hao Zhang, Hong Zhang, Hongbing Zhang, Jian Zhang, Jiangwei Zhang, Jianhua Zhang, Jing pu Zhang, Li Zhang, Lin Zhang, Long Zhang, Ming Yong Zhang, Xiangnan Zhang, Xu Dong Zhang, Yan Zhang, Yang Zhang, Yanjin Zhang, Yingmei Zhang, Yunjiao Zhang, Mei Zhao, Wei Li Zhao, Xiaonan Zhao, Yan G. Zhao, Ying Zhao, Yongchao Zhao, Yu xia Zhao, Zhendong Zhao, Zhizhuang J. Zhao, Dexian Zheng, Xi Long Zheng, Xiaoxiang Zheng, Boris Zhivotovsky, Qing Zhong, Guang Zhou Zhou, Guofei Zhou, Huiping Zhou, Shu Feng Zhou, Xu jie Zhou, Hongxin Zhu, Hua Zhu, Wei Guo Zhu, Wenhua Zhu, Xiao Feng Zhu, Yuhua Zhu, Shi Mei Zhuang, Xiaohong Zhuang, Elio Ziparo, Christos E. Zois, Teresa Zoladek, Wei Xing Zong, Antonio Zorzano, Susu M. Zughaier, Life Sciences Institute and Department of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan [Ann Arbor], University of Michigan System-University of Michigan System, Tokyo Medical University, The Hebrew University of Jerusalem (HUJ), Mammalian Genetics Unit, Medical Research Council Harwell, University of Occupational and Environmental Health School of Medicine, Partenaires INRAE, University of Toronto, Ben-Gurion University of the Negev (BGU), University of Colorado [Boulder], Cell Death Research & Therapy (CDRT) Lab, Université Catholique de Louvain = Catholic University of Louvain (UCL), University of Vienna [Vienna], Conway Institute of Biomolecular and Biomedical Research and School of Chemical and Bioprocess Engineering, University College Dublin [Dublin] (UCD), Georgetown University, Candiolo Cancer Institute (IRCCS), Centro de Investigacion Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Instituto de Salud Carlos III [Madrid] (ISC), Ikerbasque - Basque Foundation for Science, Cleveland Clinic, Sidney Kimmel Cancer Center, Jefferson (Philadelphia University + Thomas Jefferson University), Universidad de Buenos Aires (UBA), Department of Clinical Neurosciences, University College of London [London] (UCL)-Institute of Neurology, Thérapie génique, Génomique et Epigénomique (U 1169), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Consiglio Nazionale delle Ricerche (CNR), Osaka University, Department of Experimental Medicine and Public Health, University of Camerino, University of Barcelona, Institut Universitaire d'Hématologie (IUH), Université Paris Diderot - Paris 7 (UPD7), Génomique Fonctionnelle des Tumeurs Solides (U1162), Université Paris 13 (UP13)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris Descartes - Paris 5 (UPD5), Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Physics, Technical University of Denmark [Lyngby] (DTU), University of Zaragoza - Universidad de Zaragoza [Zaragoza], Department of Pharmaco-Biology, Università della Calabria [Arcavacata di Rende] (Unical), Fondation Universitaire Notre Dame de la Paix (FUNDP), Facultés Universitaires Notre Dame de la Paix (FUNDP), USC Neuromuscular Center, Department of Neurology, University of Southern California (USC), Physiopathologie de la survie et de la mort cellulaire et infection virale, Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Giannina Gaslini Institute, Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche pour le développement [IRD] : UR226, Inner Mongolia Agricultural University (IMAU), Politecnico di Milano [Milan] (POLIMI), Department of Civil, Geological, and Mining Engineering, École Polytechnique de Montréal (EPM)-NSERC Industrial Chair on Drinking Water, Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Department of Molecular Medicine, Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Physiopathologie du système nerveux central - Institut François Magendie, Université Bordeaux Segalen - Bordeaux 2-IFR8-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratory of Experimental Virology - Department of Medical Microbiology [Amsterdam, The Netherlands], Academic Medical Center - Academisch Medisch Centrum [Amsterdam] (AMC), University of Amsterdam [Amsterdam] (UvA)-University of Amsterdam [Amsterdam] (UvA)-Center for Infection and Immunity Amsterdam - CINIMA [Amsterdam, The Netherlands], Centre de résonance magnétique biologique et médicale (CRMBM), Aix Marseille Université (AMU)-Assistance Publique - Hôpitaux de Marseille (APHM)-Centre National de la Recherche Scientifique (CNRS), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1), Department of Internal Medicine, Hospital Universitario Infanta Sofía, Celullar and Molecular Medicine, Infection bactérienne, inflammation, et carcinogenèse digestive, University of Edinburgh, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Faculty of Engineering and Natural Sciences, Sabanci University [Istanbul], University of Science and Technology Beijing [Beijing] (USTB), Centre for Computational and Systems Biology (COSBI), Sun Yat-Sen University [Guangzhou] (SYSU), Dynamique Musculaire et Métabolisme (DMEM), Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), CAS Institute of Oceanology (IOCAS), Chinese Academy of Sciences [Beijing] (CAS), Polytechnic University of Marche, Centre de Recherche en Cancérologie de Marseille (CRCM), Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Cell Biology, Physiology and Immunology, Department of Experimental Oncology and Molecular Medicine, Fondazione IRCCS Istituto Nazionale dei Tumori, University of Pisa - Università di Pisa, Dulbecco Telethon Institute/Department of Biology, Fondation de Recherche Cancer et Sang - Hôpital Kirchberg, China University of Petroleum, Unilever R&D, University of Queensland [Brisbane], University of Minnesota [Twin Cities] (UMN), University of Minnesota System, Laboratoire de Génie des Procédés et Matériaux - EA 4038 (LGPM), CentraleSupélec, Institute for Advanced Study [Tsinghua], Tsinghua University [Beijing] (THU), Nanayang Technological University (NTU), Nanayang Technological University, Institute of Microelectronics [Beijing] (IMETU), Laboratoire de photonique et de nanostructures (LPN), Centre National de la Recherche Scientifique (CNRS), Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Northwestern Polytechnical University [Xi'an] (NPU), University of Pennsylvania [Philadelphia], City University of Hong Kong (CityU), Department of Mathematics [Berkeley], University of California [Berkeley], University of California-University of California, ZJU-ENS Joint Laboratory of Medicinal Chemistry, Zhejiang University, University of Cincinnati (UC), Réponses immunes : régulation et développement, Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), The University of New Mexico [Albuquerque], Centre de Recherche de l'Institut du Cerveau et de la Moelle épinière (CRICM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Dipartimento di Scienze Biomediche, Università degli Studi di Modena e Reggio Emilia (UNIMORE), Department of Experimental Medicine and Oncology, University of Turin, Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), CNV, University of Valparaiso, Université Paris 1 Panthéon-Sorbonne - UFR d'Arts plastiques et sciences de l'art (UP1 UFR04), Université Paris 1 Panthéon-Sorbonne (UP1), Department of General, Visceral and Vascular Surgery [Jena], Friedrich-Schiller-Universität Jena, Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 (RNMCD), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut National de la Santé et de la Recherche Médicale (INSERM), Réseau International des Instituts Pasteur (RIIP), Macrophages et Développement de l’Immunité, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Immunobiologie des Cellules Dendritiques, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre d'infectiologie Necker-Pasteur [CHU Necker], Institut Pasteur [Paris]-CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Institut Pasteur [Paris], Trafic membranaire et Division cellulaire - Membrane Traffic and Cell Division, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Cibles thérapeutiques, formulation et expertise pré-clinique du médicament (CITHEFOR), Université de Lorraine (UL), This work was supported in part by the National Institutes of Health, including Public Health Service grant GM053396 to D.J.K. Due to space and other limitations, it is not possible to include all other sources of financial support., In a rapidly expanding and highly dynamic field such as autophagy, it is possible that some authors who should have been included on this article have been missed. D.J.K. extends his apologies to researchers in the field of autophagy who, due to oversight or any other reason, could not be included on this article. I also note that two of our colleagues on this manuscript have passed away: Arlette Darfeuille-Michaud and Wouter van Doorn., Life Sciences Institute [Ann Arbor, MI, USA], Laboratoire de Biogenèse Membranaire, CNRS UMR 5200, Université de Bordeaux, INRA Bordeaux Aquitaine, Villenave d'Ornon, France., Amelio, Ivano [0000-0002-9126-5391], Beale, Rupert [0000-0002-6705-8560], Floto, Andres [0000-0002-2188-5659], Frezza, Christian [0000-0002-3293-7397], Ktistakis, Nicholas [0000-0001-9397-2914], Melino, Gerry [0000-0001-9428-5972], Narita, Masashi [0000-0001-7764-577X], Rubinsztein, David [0000-0001-5002-5263], Underwood, Benjamin [0000-0003-3427-9487], Whitworth, Alex [0000-0002-1154-6629], Apollo - University of Cambridge Repository, Université Catholique de Louvain, Facultés Universitaires Notre-Dame de la Paix, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR50-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Nice Sophia Antipolis (... - 2019) (UNS), Department of Clinical and Molecular Medicine, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Sun Yat-Sen University (SYSU), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), University of Minnesota [Twin Cities], Tsinghua University [Beijing], Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Université Panthéon-Sorbonne - UFR d'Arts plastiques et sciences de l'art (UP1 UFR04), Université Panthéon-Sorbonne (UP1), Récepteurs nucléaires, maladies cardiovasculaires et diabète (EGID), Université de Lille, Droit et Santé-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), CHU Necker - Enfants Malades [AP-HP], Trafic membranaire et Division cellulaire, Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS), Klionsky, D., Abdelmohsen, K., Abe, A., Abedin, M., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C., Adams, P., Adeli, K., Adhihetty, P., Adler, S., Agam, G., Agarwal, R., Aghi, M., Agnello, M., Agostinis, P., Aguilar, P., Aguirre-Ghiso, J., Airoldi, E., Ait-Si-Ali, S., Akematsu, T., Akporiaye, E., Al-Rubeai, M., Albaiceta, G., Albanese, C., Albani, D., Albert, M., Aldudo, J., Algül, H., Alirezaei, M., Alloza, I., Almasan, A., Almonte-Beceril, M., Alnemri, E., Alonso, C., Altan-Bonnet, N., Altieri, D., Alvarez, S., Alvarez-Erviti, L., Alves, S., Amadoro, G., Amano, A., Amantini, C., Ambrosio, S., Amelio, I., Amer, A., Amessou, M., Amon, A., An, Z., Anania, F., Andersen, S., Andley, U., Andreadi, C., Andrieu-Abadie, N., Anel, A., Ann, D., Anoopkumar-Dukie, S., Antonioli, M., Aoki, H., Apostolova, N., Aquila, S., Aquilano, K., Araki, K., Arama, E., Aranda, A., Araya, J., Arcaro, A., Arias, E., Arimoto, H., Ariosa, A., Armstrong, J., Arnould, T., Arsov, I., Asanuma, K., Askanas, V., Asselin, E., Atarashi, R., Atherton, S., Atkin, J., Attardi, L., Auberger, P., Auburger, G., Aurelian, L., Autelli, R., Avagliano, L., Avantaggiati, M., Avrahami, L., Awale, S., Azad, N., Bachetti, T., Backer, J., Bae, D., Bae, J., Bae, O., Bae, S., Baehrecke, E., Baek, S., Baghdiguian, S., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bailly, Y., Balaji, K., Balduini, W., Ballabio, A., Balzan, R., Banerjee, R., Bánhegyi, G., Bao, H., Barbeau, B., Barrachina, M., Barreiro, E., Bartel, B., Bartolomé, A., Bassham, D., Bassi, M., Bast, R., Basu, A., Batista, M., Batoko, H., Battino, M., Bauckman, K., Baumgarner, B., Bayer, K., Beale, R., Beaulieu, J., Beck, G., Becker, C., Beckham, J., Bédard, P., Bednarski, P., Begley, T., Behl, C., Behrends, C., Behrens, G., Behrns, K., Bejarano, E., Belaid, A., Belleudi, F., Bénard, G., Berchem, G., Bergamaschi, D., Bergami, M., Berkhout, B., Berliocchi, L., Bernard, A., Bernard, M., Bernassola, F., Bertolotti, A., Bess, A., Besteiro, S., Bettuzzi, S., Bhalla, S., Bhattacharyya, S., Bhutia, S., Biagosch, C., Bianchi, M., Biard-Piechaczyk, M., Billes, V., Bincoletto, C., Bingol, B., Bird, S., Bitoun, M., Bjedov, I., Blackstone, C., Blanc, L., Blanco, G., Blomhoff, H., Boada-Romero, E., Böckler, S., Boes, M., Boesze-Battaglia, K., Boise, L., Bolino, A., Boman, A., Bonaldo, P., Bordi, M., Bosch, J., Botana, L., Botti, J., Bou, G., Bouché, M., Bouchecareilh, M., Boucher, M., Boulton, M., Bouret, S., Boya, P., Boyer-Guittaut, M., Bozhkov, P., Brady, N., Braga, V., Brancolini, C., Braus, G., Bravo-San Pedro, J., Brennan, L., Bresnick, E., Brest, P., Bridges, D., Bringer, M., Brini, M., Brito, G., Brodin, B., Brookes, P., Brown, E., Brown, K., Broxmeyer, H., Bruhat, A., Brum, P., Brumell, J., Brunetti-Pierri, N., Bryson-Richardson, R., Buch, S., Buchan, A., Budak, H., Bulavin, D., Bultman, S., Bultynck, G., Bumbasirevic, V., Burelle, Y., Burke, R., Burmeister, M., Bütikofer, P., Caberlotto, L., Cadwell, K., Cahova, M., Cai, D., Cai, J., Cai, Q., Calatayud, S., Camougrand, N., Campanella, M., Campbell, G., Campbell, M., Campello, S., Candau, R., Caniggia, I., Cantoni, L., Cao, L., Caplan, A., Caraglia, M., Cardinali, C., Cardoso, S., Carew, J., Carleton, L., Carlin, C., Carloni, S., Carlsson, S., Carmona-Gutierrez, D., Carneiro, L., Carnevali, O., Carra, S., Carrier, A., Carroll, B., Casas, C., Casas, J., Cassinelli, G., Castets, P., Castro-Obregon, S., Cavallini, G., Ceccherini, I., Cecconi, F., Cederbaum, A., Ceña, V., Cenci, S., Cerella, C., Cervia, D., Cetrullo, S., Chaachouay, H., Chae, H., Chagin, A., Chai, C., Chakrabarti, G., Chamilos, G., Chan, E., Chan, M., Chandra, D., Chandra, P., Chang, C., Chang, R., Chang, T., Chatham, J., Chatterjee, S., Chauhan, S., Che, Y., Cheetham, M., Cheluvappa, R., Chen, C., Chen, G., Chen, H., Chen, J., Chen, M., Chen, P., Chen, Q., Chen, S., Chen, W., Chen, X., Chen, Y., Chen, Z., Cheng, A., Cheng, C., Cheng, H., Cheong, H., Cherry, S., Chesney, J., Cheung, C., Chevet, E., Chi, H., Chi, S., Chiacchiera, F., Chiang, H., Chiarelli, R., Chiariello, M., Chieppa, M., Chin, L., Chiong, M., Chiu, G., Cho, D., Cho, S., Cho, W., Cho, Y., Choi, A., Choi, E., Choi, J., Choi, M., Choi, S., Chou, T., Chouaib, S., Choubey, D., Choubey, V., Chow, K., Chowdhury, K., Chu, C., Chuang, T., Chun, T., Chung, H., Chung, T., Chung, Y., Chwae, Y., Cianfanelli, V., Ciarcia, R., Ciechomska, I., Ciriolo, M., Cirone, M., Claerhout, S., Clague, M., Clària, J., Clarke, P., Clarke, R., Clementi, E., Cleyrat, C., Cnop, M., Coccia, E., Cocco, T., Codogno, P., Coers, J., Cohen, E., Colecchia, D., Coletto, L., Coll, N., Colucci-Guyon, E., Comincini, S., Condello, M., Cook, K., Coombs, G., Cooper, C., Cooper, J., Coppens, I., Corasaniti, M., Corazzari, M., Corbalan, R., Corcelle-Termeau, E., Cordero, M., Corral-Ramos, C., Corti, O., Cossarizza, A., Costelli, P., Costes, S., Cotman, S., Coto-Montes, A., Cottet, S., Couve, E., Covey, L., Cowart, L., Cox, J., Coxon, F., Coyne, C., Cragg, M., Craven, R., Crepaldi, T., Crespo, J., Criollo, A., Crippa, V., Cruz, M., Cuervo, A., Cuezva, J., Cui, T., Cutillas, P., Czaja, M., Czyzyk-Krzeska, M., Dagda, R., Dahmen, U., Dai, C., Dai, W., Dai, Y., Dalby, K., Dalla Valle, L., Dalmasso, G., D'Amelio, M., Damme, M., Darfeuille-Michaud, A., Dargemont, C., Darley-Usmar, V., Dasarathy, S., Dasgupta, B., Dash, S., Dass, C., Davey, H., Davids, L., Dávila, D., Davis, R., Dawson, T., Dawson, V., Daza, P., de Belleroche, J., de Figueiredo, P., de Figueiredo, R., de la Fuente, J., De Martino, L., De Matteis, A., De Meyer, G., De Milito, A., De Santi, M., de Souza, W., De Tata, V., De Zio, D., Debnath, J., Dechant, R., Decuypere, J., Deegan, S., Dehay, B., Del Bello, B., Del Re, D., Delage-Mourroux, R., Delbridge, L., Deldicque, L., Delorme-Axford, E., Deng, Y., Dengjel, J., Denizot, M., Dent, P., Der, C., Deretic, V., Derrien, B., Deutsch, E., Devarenne, T., Devenish, R., Di Bartolomeo, S., Di Daniele, N., Di Domenico, F., Di Nardo, A., Di Paola, S., Di Pietro, A., Di Renzo, L., Diantonio, A., Díaz-Araya, G., Díaz-Laviada, I., Diaz-Meco, M., Diaz-Nido, J., Dickey, C., Dickson, R., Diederich, M., Digard, P., Dikic, I., Dinesh-Kumar, S., Ding, C., Ding, W., Ding, Z., Dini, L., Distler, J., Diwan, A., Djavaheri-Mergny, M., Dmytruk, K., Dobson, R., Doetsch, V., Dokladny, K., Dokudovskaya, S., Donadelli, M., Dong, X., Dong, Z., Donohue, T., Doran, K., D'Orazi, G., Dorn, G., Dosenko, V., Dridi, S., Drucker, L., Du, J., Du, L., du Toit, A., Dua, P., Duan, L., Duann, P., Dubey, V., Duchen, M., Duchosal, M., Duez, H., Dugail, I., Dumit, V., Duncan, M., Dunlop, E., Dunn, W., Dupont, N., Dupuis, L., Durán, R., Durcan, T., Duvezin-Caubet, S., Duvvuri, U., Eapen, V., Ebrahimi-Fakhari, D., Echard, A., Eckhart, L., Edelstein, C., Edinger, A., Eichinger, L., Eisenberg, T., Eisenberg-Lerner, A., Eissa, N., El-Deiry, W., El-Khoury, V., Elazar, Z., Eldar-Finkelman, H., Elliott, C., Emanuele, E., Emmenegger, U., Engedal, N., Engelbrecht, A., Engelender, S., Enserink, J., Erdmann, R., Erenpreisa, J., Eri, R., Eriksen, J., Erman, A., Escalante, R., Eskelinen, E., Espert, L., Esteban-Martínez, L., Evans, T., Fabri, M., Fabrias, G., Fabrizi, C., Facchiano, A., Færgeman, N., Faggioni, A., Fairlie, W., Fan, C., Fan, D., Fan, J., Fang, S., Fanto, M., Fanzani, A., Farkas, T., Faure, M., Favier, F., Fearnhead, H., Federici, M., Fei, E., Felizardo, T., Feng, H., Feng, Y., Ferguson, T., Fernández, Á., Fernandez-Barrena, M., Fernandez-Checa, J., Fernández-López, A., Fernandez-Zapico, M., Feron, O., Ferraro, E., Ferreira-Halder, C., Fesus, L., Feuer, R., Fiesel, F., Filippi-Chiela, E., Filomeni, G., Fimia, G., Fingert, J., Finkbeiner, S., Finkel, T., Fiorito, F., Fisher, P., Flajolet, M., Flamigni, F., Florey, O., Florio, S., Floto, R., Folini, M., Follo, C., Fon, E., Fornai, F., Fortunato, F., Fraldi, A., Franco, R., Francois, A., François, A., Frankel, L., Fraser, I., Frey, N., Freyssenet, D., Frezza, C., Friedman, S., Frigo, D., Fu, D., Fuentes, J., Fueyo, J., Fujitani, Y., Fujiwara, Y., Fujiya, M., Fukuda, M., Fulda, S., Fusco, C., Gabryel, B., Gaestel, M., Gailly, P., Gajewska, M., Galadari, S., Galili, G., Galindo, I., Galindo, M., Galliciotti, G., Galluzzi, L., Galy, V., Gammoh, N., Gandy, S., Ganesan, A., Ganesan, S., Ganley, I., Gannagé, M., Gao, F., Gao, J., García Nannig, L., García Véscovi, E., Garcia-Macía, M., Garcia-Ruiz, C., Garg, A., Garg, P., Gargini, R., Gassen, N., Gatica, D., Gatti, E., Gavard, J., Gavathiotis, E., Ge, L., Ge, P., Ge, S., Gean, P., Gelmetti, V., Genazzani, A., Geng, J., Genschik, P., Gerner, L., Gestwicki, J., Gewirtz, D., Ghavami, S., Ghigo, E., Ghosh, D., Giammarioli, A., Giampieri, F., Giampietri, C., Giatromanolaki, A., Gibbings, D., Gibellini, L., Gibson, S., Ginet, V., Giordano, A., Giorgini, F., Giovannetti, E., Girardin, S., Gispert, S., Giuliano, S., Gladson, C., Glavic, A., Gleave, M., Godefroy, N., Gogal, R., Gokulan, K., Goldman, G., Goletti, D., Goligorsky, M., Gomes, A., Gomes, L., Gomez, H., Gomez-Manzano, C., Gómez-Sánchez, R., Gonçalves, D., Goncu, E., Gong, Q., Gongora, C., Gonzalez, C., Gonzalez-Alegre, P., Gonzalez-Cabo, P., González-Polo, R., Goping, I., Gorbea, C., Gorbunov, N., Goring, D., Gorman, A., Gorski, S., Goruppi, S., Goto-Yamada, S., Gotor, C., Gottlieb, R., Gozes, I., Gozuacik, D., Graba, Y., Graef, M., Granato, G., Grant, G., Grant, S., Gravina, G., Green, D., Greenhough, A., Greenwood, M., Grimaldi, B., Gros, F., Grose, C., Groulx, J., Gruber, F., Grumati, P., Grune, T., Guan, J., Guan, K., Guerra, B., Guillen, C., Gulshan, K., Gunst, J., Guo, C., Guo, L., Guo, M., Guo, W., Guo, X., Gust, A., Gustafsson, Å., Gutierrez, E., Gutierrez, M., Gwak, H., Haas, A., Haber, J., Hadano, S., Hagedorn, M., Hahn, D., Halayko, A., Hamacher-Brady, A., Hamada, K., Hamai, A., Hamann, A., Hamasaki, M., Hamer, I., Hamid, Q., Hammond, E., Han, F., Han, W., Handa, J., Hanover, J., Hansen, M., Harada, M., Harhaji-Trajkovic, L., Harper, J., Harrath, A., Harris, A., Harris, J., Hasler, U., Hasselblatt, P., Hasui, K., Hawley, R., Hawley, T., He, C., He, F., He, G., He, R., He, X., He, Y., Heath, J., Hébert, M., Heinzen, R., Helgason, G., Hensel, M., Henske, E., Her, C., Herman, P., Hernández, A., Hernandez, C., Hernández-Tiedra, S., Hetz, C., Hiesinger, P., Higaki, K., Hilfiker, S., Hill, B., Hill, J., Hill, W., Hino, K., Hofius, D., Hofman, P., Höglinger, G., Höhfeld, J., Holz, M., Hong, Y., Hood, D., Hoozemans, J., Hoppe, T., Hsu, C., Hsu, L., Hu, D., Hu, G., Hu, H., Hu, M., Hu, Y., Hu, Z., Hua, F., Hua, Y., Huang, C., Huang, H., Huang, K., Huang, S., Huang, W., Huang, Y., Huber, T., Huebbe, P., Huh, W., Hulmi, J., Hur, G., Hurley, J., Husak, Z., Hussain, S., Hwang, J., Hwang, S., Hwang, T., Ichihara, A., Imai, Y., Imbriano, C., Inomata, M., Into, T., Iovane, V., Iovanna, J., Iozzo, R., Ip, N., Irazoqui, J., Iribarren, P., Isaka, Y., Isakovic, A., Ischiropoulos, H., Isenberg, J., Ishaq, M., Ishida, H., Ishii, I., Ishmael, J., Isidoro, C., Isobe, K., Isono, E., Issazadeh-Navikas, S., Itahana, K., Itakura, E., Ivanov, A., Iyer, A., Izquierdo, J., Izumi, Y., Izzo, V., Jäättelä, M., Jaber, N., Jackson, D., Jackson, W., Jacob, T., Jacques, T., Jagannath, C., Jain, A., Jana, N., Jang, B., Jani, A., Janji, B., Jannig, P., Jansson, P., Jean, S., Jendrach, M., Jeon, J., Jessen, N., Jeung, E., Jia, K., Jia, L., Jiang, H., Jiang, L., Jiang, T., Jiang, X., Jiang, Y., Jiménez, A., Jin, C., Jin, H., Jin, L., Jin, M., Jin, S., Jinwal, U., Jo, E., Johansen, T., Johnson, D., Johnson, G., Johnson, J., Jonasch, E., Jones, C., Joosten, L., Jordan, J., Joseph, A., Joseph, B., Joubert, A., Ju, D., Ju, J., Juan, H., Juenemann, K., Juhász, G., Jung, H., Jung, J., Jung, Y., Jungbluth, H., Justice, M., Jutten, B., Kaakoush, N., Kaarniranta, K., Kaasik, A., Kabuta, T., Kaeffer, B., Kågedal, K., Kahana, A., Kajimura, S., Kakhlon, O., Kalia, M., Kalvakolanu, D., Kamada, Y., Kambas, K., Kaminskyy, V., Kampinga, H., Kandouz, M., Kang, C., Kang, R., Kang, T., Kanki, T., Kanneganti, T., Kanno, H., Kanthasamy, A., Kantorow, M., Kaparakis-Liaskos, M., Kapuy, O., Karantza, V., Karim, M., Karmakar, P., Kaser, A., Kaushik, S., Kawula, T., Kaynar, A., Ke, P., Ke, Z., Kehrl, J., Keller, K., Kemper, J., Kenworthy, A., Kepp, O., Kern, A., Kesari, S., Kessel, D., Ketteler, R., Kettelhut, I., Khambu, B., Khan, M., Khandelwal, V., Khare, S., Kiang, J., Kiger, A., Kihara, A., Kim, A., Kim, C., Kim, D., Kim, E., Kim, H., Kim, J., Kim, K., Kim, M., Kim, P., Kim, S., Kim, Y., Kimchi, A., Kimmelman, A., Kimura, T., King, J., Kirkegaard, K., Kirkin, V., Kirshenbaum, L., Kishi, S., Kitajima, Y., Kitamoto, K., Kitaoka, Y., Kitazato, K., Kley, R., Klimecki, W., Klinkenberg, M., Klucken, J., Knævelsrud, H., Knecht, E., Knuppertz, L., Ko, J., Kobayashi, S., Koch, J., Koechlin-Ramonatxo, C., Koenig, U., Koh, Y., Köhler, K., Kohlwein, S., Koike, M., Komatsu, M., Kominami, E., Kong, D., Kong, H., Konstantakou, E., Kopp, B., Korcsmaros, T., Korhonen, L., Korolchuk, V., Koshkina, N., Kou, Y., Koukourakis, M., Koumenis, C., Kovács, A., Kovács, T., Kovacs, W., Koya, D., Kraft, C., Krainc, D., Kramer, H., Kravic-Stevovic, T., Krek, W., Kretz-Remy, C., Krick, R., Krishnamurthy, M., Kriston-Vizi, J., Kroemer, G., Kruer, M., Kruger, R., Ktistakis, N., Kuchitsu, K., Kuhn, C., Kumar, A., Kumar, D., Kumar, R., Kumar, S., Kundu, M., Kung, H., Kuno, A., Kuo, S., Kuret, J., Kurz, T., Kwok, T., Kwon, T., Kwon, Y., Kyrmizi, I., La Spada, A., Lafont, F., Lahm, T., Lakkaraju, A., Lam, T., Lamark, T., Lancel, S., Landowski, T., Lane, D., Lane, J., Lanzi, C., Lapaquette, P., Lapierre, L., Laporte, J., Laukkarinen, J., Laurie, G., Lavandero, S., Lavie, L., Lavoie, M., Law, B., Law, H., Law, K., Layfield, R., Lazo, P., Le Cam, L., Le Roch, K., Le Stunff, H., Leardkamolkarn, V., Lecuit, M., Lee, B., Lee, C., Lee, E., Lee, G., Lee, H., Lee, J., Lee, M., Lee, P., Lee, S., Lee, Y., Leeuwenburgh, C., Lefort, S., Legouis, R., Lei, J., Lei, Q., Leib, D., Leibowitz, G., Lekli, I., Lemaire, S., Lemasters, J., Lemberg, M., Lemoine, A., Leng, S., Lenz, G., Lenzi, P., Lerman, L., Lettieri Barbato, D., Leu, J., Leung, H., Levine, B., Lewis, P., Lezoualc'H, F., Li, C., Li, F., Li, J., Li, K., Li, L., Li, M., Li, Q., Li, R., Li, S., Li, W., Li, X., Li, Y., Lian, J., Liang, C., Liang, Q., Liao, Y., Liberal, J., Liberski, P., Lie, P., Lieberman, A., Lim, H., Lim, K., Lima, R., Lin, C., Lin, F., Lin, K., Lin, P., Lin, T., Lin, W., Lin, Y., Linden, R., Lindholm, D., Lindqvist, L., Lingor, P., Linkermann, A., Liotta, L., Lipinski, M., Lira, V., Lisanti, M., Liton, P., Liu, B., Liu, C., Liu, F., Liu, H., Liu, J., Liu, K., Liu, L., Liu, Q., Liu, R., Liu, S., Liu, W., Liu, X., Liu, Y., Liu, Z., Liuzzi, J., Lizard, G., Ljujic, M., Lodhi, I., Logue, S., Lokeshwar, B., Long, Y., Lonial, S., Loos, B., López-Otín, C., López-Vicario, C., Lorente, M., Lorenzi, P., Lõrincz, P., Los, M., Lotze, M., Lovat, P., Lu, B., Lu, J., Lu, Q., Lu, S., Lu, Y., Luciano, F., Luckhart, S., Lucocq, J., Ludovico, P., Lugea, A., Lukacs, N., Lum, J., Lund, A., Luo, H., Luo, J., Luo, S., Luparello, C., Lyons, T., Ma, J., Ma, Y., Ma, Z., Machado, J., Machado-Santelli, G., Macian, F., Macintosh, G., Mackeigan, J., Macleod, K., Macmicking, J., MacMillan-Crow, L., Madeo, F., Madesh, M., Madrigal-Matute, J., Maeda, A., Maeda, T., Maegawa, G., Maellaro, E., Maes, H., Magariños, M., Maiese, K., Maiti, T., Maiuri, L., Maiuri, M., Maki, C., Malli, R., Malorni, W., Maloyan, A., Mami-Chouaib, F., Man, N., Mancias, J., Mandelkow, E., Mandell, M., Manfredi, A., Manié, S., Manzoni, C., Mao, K., Mao, Z., Marambaud, P., Marconi, A., Marelja, Z., Marfe, G., Margeta, M., Margittai, E., Mari, M., Mariani, F., Marin, C., Marinelli, S., Mariño, G., Markovic, I., Marquez, R., Martelli, A., Martens, S., Martin, K., Martin, S., Martin-Acebes, M., Martín-Sanz, P., Martinand-Mari, C., Martinet, W., Martinez, J., Martinez-Lopez, N., Martinez-Outschoorn, U., Martínez-Velázquez, M., Martinez-Vicente, M., Martins, W., Mashima, H., Mastrianni, J., Matarese, G., Matarrese, P., Mateo, R., Matoba, S., Matsumoto, N., Matsushita, T., Matsuura, A., Matsuzawa, T., Mattson, M., Matus, S., Maugeri, N., Mauvezin, C., Mayer, A., Maysinger, D., Mazzolini, G., Mcbrayer, M., Mccall, K., Mccormick, C., Mcinerney, G., Mciver, S., Mckenna, S., Mcmahon, J., Mcneish, I., Mechta-Grigoriou, F., Medema, J., Medina, D., Megyeri, K., Mehrpour, M., Mehta, J., Mei, Y., Meier, U., Meijer, A., Meléndez, A., Melino, G., Melino, S., de Melo, E., Mena, M., Meneghini, M., Menendez, J., Menezes, R., Meng, L., Meng, S., Menghini, R., Menko, A., Menna-Barreto, R., Menon, M., Meraz-Ríos, M., Merla, G., Merlini, L., Merlot, A., Meryk, A., Meschini, S., Meyer, J., Mi, M., Miao, C., Micale, L., Michaeli, S., Michiels, C., Migliaccio, A., Mihailidou, A., Mijaljica, D., Mikoshiba, K., Milan, E., Miller-Fleming, L., Mills, G., Mills, I., Minakaki, G., Minassian, B., Ming, X., Minibayeva, F., Minina, E., Mintern, J., Minucci, S., Miranda-Vizuete, A., Mitchell, C., Miyamoto, S., Miyazawa, K., Mizushima, N., Mnich, K., Mograbi, B., Mohseni, S., Moita, L., Molinari, M., Møller, A., Mollereau, B., Mollinedo, F., Mongillo, M., Monick, M., Montagnaro, S., Montell, C., Moore, D., Moore, M., Mora-Rodriguez, R., Moreira, P., Morel, E., Morelli, M., Moreno, S., Morgan, M., Moris, A., Moriyasu, Y., Morrison, J., Morrison, L., Morselli, E., Moscat, J., Moseley, P., Mostowy, S., Motori, E., Mottet, D., Mottram, J., Moussa, C., Mpakou, V., Mukhtar, H., Mulcahy Levy, J., Muller, S., Muñoz-Moreno, R., Muñoz-Pinedo, C., Münz, C., Murphy, M., Murray, J., Murthy, A., Mysorekar, I., Nabi, I., Nabissi, M., Nader, G., Nagahara, Y., Nagai, Y., Nagata, K., Nagelkerke, A., Nagy, P., Naidu, S., Nair, S., Nakano, H., Nakatogawa, H., Nanjundan, M., Napolitano, G., Naqvi, N., Nardacci, R., Narendra, D., Narita, M., Nascimbeni, A., Natarajan, R., Navegantes, L., Nawrocki, S., Nazarko, T., Nazarko, V., Neill, T., Neri, L., Netea, M., Netea-Maier, R., Neves, B., Ney, P., Nezis, I., Nguyen, H., Nicot, A., Nilsen, H., Nilsson, P., Nishimura, M., Nishino, I., Niso-Santano, M., Niu, H., Nixon, R., Njar, V., Noda, T., Noegel, A., Nolte, E., Norberg, E., Norga, K., Noureini, S., Notomi, S., Notterpek, L., Nowikovsky, K., Nukina, N., Nürnberger, T., O'Donnell, V., O'Donovan, T., O'Dwyer, P., Oehme, I., Oeste, C., Ogawa, M., Ogretmen, B., Ogura, Y., Oh, Y., Ohmuraya, M., Ohshima, T., Ojha, R., Okamoto, K., Okazaki, T., Oliver, F., Ollinger, K., Olsson, S., Orban, D., Ordonez, P., Orhon, I., Orosz, L., O'Rourke, E., Orozco, H., Ortega, A., Ortona, E., Osellame, L., Oshima, J., Oshima, S., Osiewacz, H., Otomo, T., Otsu, K., Ou, J., Outeiro, T., Ouyang, D., Ouyang, H., Overholtzer, M., Ozbun, M., Ozdinler, P., Ozpolat, B., Pacelli, C., Paganetti, P., Page, G., Pages, G., Pagnini, U., Pajak, B., Pak, S., Pakos-Zebrucka, K., Pakpour, N., Palková, Z., Palladino, F., Pallauf, K., Pallet, N., Palmieri, M., Paludan, S., Palumbo, C., Palumbo, S., Pampliega, O., Pan, H., Pan, W., Panaretakis, T., Pandey, A., Pantazopoulou, A., Papackova, Z., Papademetrio, D., Papassideri, I., Papini, A., Parajuli, N., Pardo, J., Parekh, V., Parenti, G., Park, J., Park, O., Parker, R., Parlato, R., Parys, J., Parzych, K., Pasquet, J., Pasquier, B., Pasumarthi, K., Patschan, D., Patterson, C., Pattingre, S., Pattison, S., Pause, A., Pavenstädt, H., Pavone, F., Pedrozo, Z., Peña, F., Peñalva, M., Pende, M., Peng, J., Penna, F., Penninger, J., Pensalfini, A., Pepe, S., Pereira, G., Pereira, P., Pérez-de la Cruz, V., Pérez-Pérez, M., Pérez-Rodríguez, D., Pérez-Sala, D., Perier, C., Perl, A., Perlmutter, D., Perrotta, I., Pervaiz, S., Pesonen, M., Pessin, J., Peters, G., Petersen, M., Petrache, I., Petrof, B., Petrovski, G., Phang, J., Piacentini, M., Pierdominici, M., Pierre, P., Pierrefite-Carle, V., Pietrocola, F., Pimentel-Muiños, F., Pinar, M., Pineda, B., Pinkas-Kramarski, R., Pinti, M., Pinton, P., Piperdi, B., Piret, J., Platanias, L., Platta, H., Plowey, E., Pöggeler, S., Poirot, M., Polčic, P., Poletti, A., Poon, A., Popelka, H., Popova, B., Poprawa, I., Poulose, S., Poulton, J., Powers, S., Powers, T., Pozuelo-Rubio, M., Prak, K., Prange, R., Prescott, M., Priault, M., Prince, S., Proia, R., Proikas-Cezanne, T., Prokisch, H., Promponas, V., Przyklenk, K., Puertollano, R., Pugazhenthi, S., Puglielli, L., Pujol, A., Puyal, J., Pyeon, D., Qi, X., Qian, W., Qin, Z., Qiu, Y., Qu, Z., Quadrilatero, J., Quinn, F., Raben, N., Rabinowich, H., Radogna, F., Ragusa, M., Rahmani, M., Raina, K., Ramanadham, S., Ramesh, R., Rami, A., Randall-Demllo, S., Randow, F., Rao, H., Rao, V., Rasmussen, B., Rasse, T., Ratovitski, E., Rautou, P., Ray, S., Razani, B., Reed, B., Reggiori, F., Rehm, M., Reichert, A., Rein, T., Reiner, D., Reits, E., Ren, J., Ren, X., Renna, M., Reusch, J., Revuelta, J., Reyes, L., Rezaie, A., Richards, R., Richardson, D., Richetta, C., Riehle, M., Rihn, B., Rikihisa, Y., Riley, B., Rimbach, G., Rippo, M., Ritis, K., Rizzi, F., Rizzo, E., Roach, P., Robbins, J., Roberge, M., Roca, G., Roccheri, M., Rocha, S., Rodrigues, C., Rodríguez, C., de Cordoba, S., Rodriguez-Muela, N., Roelofs, J., Rogov, V., Rohn, T., Rohrer, B., Romanelli, D., Romani, L., Romano, P., Roncero, M., Rosa, J., Rosello, A., Rosen, K., Rosenstiel, P., Rost-Roszkowska, M., Roth, K., Roué, G., Rouis, M., Rouschop, K., Ruan, D., Ruano, D., Rubinsztein, D., Rucker, E., Rudich, A., Rudolf, E., Rudolf, R., Ruegg, M., Ruiz-Roldan, C., Ruparelia, A., Rusmini, P., Russ, D., Russo, G., Russo, R., Rusten, T., Ryabovol, V., Ryan, K., Ryter, S., Sabatini, D., Sacher, M., Sachse, C., Sack, M., Sadoshima, J., Saftig, P., Sagi-Eisenberg, R., Sahni, S., Saikumar, P., Saito, T., Saitoh, T., Sakakura, K., Sakoh-Nakatogawa, M., Sakuraba, Y., Salazar-Roa, M., Salomoni, P., Saluja, A., Salvaterra, P., Salvioli, R., Samali, A., Sanchez, A., Sánchez-Alcázar, J., Sanchez-Prieto, R., Sandri, M., Sanjuan, M., Santaguida, S., Santambrogio, L., Santoni, G., Dos Santos, C., Saran, S., Sardiello, M., Sargent, G., Sarkar, P., Sarkar, S., Sarrias, M., Sarwal, M., Sasakawa, C., Sasaki, M., Sass, M., Sato, K., Sato, M., Satriano, J., Savaraj, N., Saveljeva, S., Schaefer, L., Schaible, U., Scharl, M., Schatzl, H., Schekman, R., Scheper, W., Schiavi, A., Schipper, H., Schmeisser, H., Schmidt, J., Schmitz, I., Schneider, B., Schneider, E., Schneider, J., Schon, E., Schönenberger, M., Schönthal, A., Schorderet, D., Schröder, B., Schuck, S., Schulze, R., Schwarten, M., Schwarz, T., Sciarretta, S., Scotto, K., Scovassi, A., Screaton, R., Screen, M., Seca, H., Sedej, S., Segatori, L., Segev, N., Seglen, P., Seguí-Simarro, J., Segura-Aguilar, J., Seki, E., Sell, C., Selliez, I., Semenkovich, C., Semenza, G., Sen, U., Serra, A., Serrano-Puebla, A., Sesaki, H., Setoguchi, T., Settembre, C., Shacka, J., Shajahan-Haq, A., Shapiro, I., Sharma, S., She, H., Shen, C., Shen, H., Shen, S., Shen, W., Sheng, R., Sheng, X., Sheng, Z., Shepherd, T., Shi, J., Shi, Q., Shi, Y., Shibutani, S., Shibuya, K., Shidoji, Y., Shieh, J., Shih, C., Shimada, Y., Shimizu, S., Shin, D., Shinohara, M., Shintani, M., Shintani, T., Shioi, T., Shirabe, K., Shiri-Sverdlov, R., Shirihai, O., Shore, G., Shu, C., Shukla, D., Sibirny, A., Sica, V., Sigurdson, C., Sigurdsson, E., Sijwali, P., Sikorska, B., Silveira, W., Silvente-Poirot, S., Silverman, G., Simak, J., Simmet, T., Simon, A., Simon, H., Simone, C., Simons, M., Simonsen, A., Singh, R., Singh, S., Sinha, D., Sinha, S., Sinicrope, F., Sirko, A., Sirohi, K., Sishi, B., Sittler, A., Siu, P., Sivridis, E., Skwarska, A., Slack, R., Slaninová, I., Slavov, N., Smaili, S., Smalley, K., Smith, D., Soenen, S., Soleimanpour, S., Solhaug, A., Somasundaram, K., Son, J., Sonawane, A., Song, C., Song, F., Song, H., Song, J., Song, W., Soo, K., Sood, A., Soong, T., Soontornniyomkij, V., Sorice, M., Sotgia, F., Soto-Pantoja, D., Sotthibundhu, A., Sousa, M., Spaink, H., Span, P., Spang, A., Sparks, J., Speck, P., Spector, S., Spies, C., Springer, W., Clair, D., Stacchiotti, A., Staels, B., Stang, M., Starczynowski, D., Starokadomskyy, P., Steegborn, C., Steele, J., Stefanis, L., Steffan, J., Stellrecht, C., Stenmark, H., Stepkowski, T., Stern, S., Stevens, C., Stockwell, B., Stoka, V., Storchova, Z., Stork, B., Stratoulias, V., Stravopodis, D., Strnad, P., Strohecker, A., Ström, A., Stromhaug, P., Stulik, J., Su, Y., Su, Z., Subauste, C., Subramaniam, S., Sue, C., Suh, S., Sui, X., Sukseree, S., Sulzer, D., Sun, F., Sun, J., Sun, S., Sun, Y., Sundaramoorthy, V., Sung, J., Suzuki, H., Suzuki, K., Suzuki, N., Suzuki, T., Suzuki, Y., Swanson, M., Swanton, C., Swärd, K., Swarup, G., Sweeney, S., Sylvester, P., Szatmari, Z., Szegezdi, E., Szlosarek, P., Taegtmeyer, H., Tafani, M., Taillebourg, E., Tait, S., Takacs-Vellai, K., Takahashi, Y., Takáts, S., Takemura, G., Takigawa, N., Talbot, N., Tamagno, E., Tamburini, J., Tan, C., Tan, L., Tan, M., Tan, Y., Tanaka, K., Tanaka, M., Tang, D., Tang, G., Tanida, I., Tanji, K., Tannous, B., Tapia, J., Tasset-Cuevas, I., Tatar, M., Tavassoly, I., Tavernarakis, N., Taylor, A., Taylor, G., Taylor, J., Taylor, M., Tchetina, E., Tee, A., Teixeira-Clerc, F., Telang, S., Tencomnao, T., Teng, B., Teng, R., Terro, F., Tettamanti, G., Theiss, A., Theron, A., Thomas, K., Thomé, M., Thomes, P., Thorburn, A., Thorner, J., Thum, T., Thumm, M., Thurston, T., Tian, L., Till, A., Ting, J., Titorenko, V., Toker, L., Toldo, S., Tooze, S., Topisirovic, I., Torgersen, M., Torosantucci, L., Torriglia, A., Torrisi, M., Tournier, C., Towns, R., Trajkovic, V., Travassos, L., Triola, G., Tripathi, D., Trisciuoglio, D., Troncoso, R., Trougakos, I., Truttmann, A., Tsai, K., Tschan, M., Tseng, Y., Tsukuba, T., Tsung, A., Tsvetkov, A., Tu, S., Tuan, H., Tucci, M., Tumbarello, D., Turk, B., Turk, V., Turner, R., Tveita, A., Tyagi, S., Ubukata, M., Uchiyama, Y., Udelnow, A., Ueno, T., Umekawa, M., Umemiya-Shirafuji, R., Underwood, B., Ungermann, C., Ureshino, R., Ushioda, R., Uversky, V., Uzcátegui, N., Vaccari, T., Vaccaro, M., Váchová, L., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, E., Vallette, F., Valverde, A., Van den Berghe, G., Van Den Bosch, L., van den Brink, G., van der Goot, F., van der Klei, I., van der Laan, L., van Doorn, W., van Egmond, M., van Golen, K., Van Kaer, L., van Lookeren Campagne, M., Vandenabeele, P., Vandenberghe, W., Vanhorebeek, I., Varela-Nieto, I., Vasconcelos, M., Vasko, R., Vavvas, D., Vega-Naredo, I., Velasco, G., Velentzas, A., Velentzas, P., Vellai, T., Vellenga, E., Vendelbo, M., Venkatachalam, K., Ventura, N., Ventura, S., Veras, P., Verdier, M., Vertessy, B., Viale, A., Vidal, M., Vieira, H., Vierstra, R., Vigneswaran, N., Vij, N., Vila, M., Villar, M., Villar, V., Villarroya, J., Vindis, C., Viola, G., Viscomi, M., Vitale, G., Vogl, D., Voitsekhovskaja, O., von Haefen, C., von Schwarzenberg, K., Voth, D., Vouret-Craviari, V., Vuori, K., Vyas, J., Waeber, C., Walker, C., Walker, M., Walter, J., Wan, L., Wan, X., Wang, B., Wang, C., Wang, D., Wang, F., Wang, G., Wang, H., Wang, J., Wang, M., Wang, P., Wang, R., Wang, S., Wang, T., Wang, X., Wang, Y., Wang, Z., Wappner, P., Ward, C., Ward, D., Warnes, G., Watada, H., Watanabe, Y., Watase, K., Weaver, T., Weekes, C., Wei, J., Weide, T., Weihl, C., Weindl, G., Weis, S., Wen, L., Wen, X., Wen, Y., Westermann, B., Weyand, C., White, A., White, E., Whitton, J., Whitworth, A., Wiels, J., Wild, F., Wildenberg, M., Wileman, T., Wilkinson, D., Wilkinson, S., Willbold, D., Williams, C., Williams, K., Williamson, P., Winklhofer, K., Witkin, S., Wohlgemuth, S., Wollert, T., Wolvetang, E., Wong, E., Wong, G., Wong, R., Wong, V., Woodcock, E., Wright, K., Wu, C., Wu, D., Wu, G., Wu, J., Wu, M., Wu, S., Wu, W., Wu, Y., Wu, Z., Xavier, C., Xavier, R., Xia, G., Xia, T., Xia, W., Xia, Y., Xiao, H., Xiao, J., Xiao, S., Xiao, W., Xie, C., Xie, Z., Xilouri, M., Xiong, Y., Xu, C., Xu, F., Xu, H., Xu, J., Xu, L., Xu, X., Xu, Y., Xu, Z., Xue, Y., Yamada, T., Yamamoto, A., Yamanaka, K., Yamashina, S., Yamashiro, S., Yan, B., Yan, X., Yan, Z., Yanagi, Y., Yang, D., Yang, J., Yang, L., Yang, M., Yang, P., Yang, Q., Yang, W., Yang, X., Yang, Y., Yang, Z., Yao, M., Yao, P., Yao, X., Yao, Z., Yasui, L., Ye, M., Yedvobnick, B., Yeganeh, B., Yeh, E., Yeyati, P., Yi, F., Yi, L., Yin, X., Yip, C., Yoo, Y., Yoon, S., Yoshida, K., Yoshimori, T., Young, K., Yu, H., Yu, J., Yu, L., Yu, W., Yu, X., Yu, Z., Yuan, J., Yuan, Z., Yue, B., Yue, J., Yue, Z., Zacks, D., Zacksenhaus, E., Zaffaroni, N., Zaglia, T., Zakeri, Z., Zecchini, V., Zeng, J., Zeng, M., Zeng, Q., Zervos, A., Zhang, D., Zhang, F., Zhang, G., Zhang, H., Zhang, J., Zhang, L., Zhang, M., Zhang, X., Zhang, Y., Zhao, M., Zhao, W., Zhao, X., Zhao, Y., Zhao, Z., Zheng, D., Zheng, X., Zhivotovsky, B., Zhong, Q., Zhou, G., Zhou, H., Zhou, S., Zhou, X., Zhu, H., Zhu, W., Zhu, X., Zhu, Y., Zhuang, S., Zhuang, X., Ziparo, E., Zois, C., Zoladek, T., Zong, W., Zorzano, A., Zughaier, S., Klionsky, Daniel J, Abdelmohsen, Kotb, Abe, Akihisa, Abedin, Md Joynal, Abeliovich, Hagai, Acevedo Arozena, Abraham, Adachi, Hiroaki, Adams, Christopher M, Adams, Peter D, Adeli, Khosrow, Adhihetty, Peter J, Adler, Sharon G, Agam, Galila, Agarwal, Rajesh, Aghi, Manish K, Agnello, Maria, Agostinis, Patrizia, Aguilar, Patricia V, Aguirre Ghiso, Julio, Airoldi, Edoardo M, Ait Si Ali, Slimane, Akematsu, Takahiko, Akporiaye, Emmanuel T, Al Rubeai, Mohamed, Albaiceta, Guillermo M, Albanese, Chri, Albani, Diego, Albert, Matthew L, Aldudo, Jesu, Algül, Hana, Alirezaei, Mehrdad, Alloza, Iraide, Almasan, Alexandru, Almonte Beceril, Maylin, Alnemri, Emad S, Alonso, Covadonga, Altan Bonnet, Nihal, Altieri, Dario C, Alvarez, Silvia, Alvarez Erviti, Lydia, Alves, Sandro, Amadoro, Giuseppina, Amano, Atsuo, Amantini, Consuelo, Ambrosio, Santiago, Amelio, Ivano, Amer, Amal O, Amessou, Mohamed, Amon, Angelika, An, Zhenyi, Anania, Frank A, Andersen, Stig U, Andley, Usha P, Andreadi, Catherine K, Andrieu Abadie, Nathalie, Anel, Alberto, Ann, David K, Anoopkumar Dukie, Shailendra, Antonioli, Manuela, Aoki, Hiroshi, Apostolova, Nadezda, Aquila, Saveria, Aquilano, Katia, Araki, Koichi, Arama, Eli, Aranda, Agustin, Araya, Jun, Arcaro, Alexandre, Arias, Esperanza, Arimoto, Hirokazu, Ariosa, Aileen R, Armstrong, Jane L, Arnould, Thierry, Arsov, Ivica, Asanuma, Katsuhiko, Askanas, Valerie, Asselin, Eric, Atarashi, Ryuichiro, Atherton, Sally S, Atkin, Julie D, Attardi, Laura D, Auberger, Patrick, Auburger, Georg, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Avantaggiati, Maria Laura, Avrahami, Limor, Awale, Suresh, Azad, Neelam, Bachetti, Tiziana, Backer, Jonathan M, Bae, Dong Hun, Bae, Jae Sung, Bae, Ok Nam, Bae, Soo Han, Baehrecke, Eric H, Baek, Seung Hoon, Baghdiguian, Stephen, Bagniewska Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xue Yuan, Bailly, Yannick, Balaji, Kithiganahalli Narayanaswamy, Balduini, Walter, Ballabio, Andrea, Balzan, Rena, Banerjee, Rajkumar, Bánhegyi, Gábor, Bao, Haijun, Barbeau, Benoit, Barrachina, Maria D, Barreiro, Esther, Bartel, Bonnie, Bartolomé, Alberto, Bassham, Diane C, Bassi, Maria Teresa, Bast, Robert C, Basu, Alakananda, Batista, Maria Teresa, Batoko, Henri, Battino, Maurizio, Bauckman, Kyle, Baumgarner, Bradley L, Bayer, K. Ulrich, Beale, Rupert, Beaulieu, Jean Françoi, Beck, George R, Becker, Christoph, Beckham, J. David, Bédard, Pierre André, Bednarski, Patrick J, Begley, Thomas J, Behl, Christian, Behrends, Christian, Behrens, Georg Mn, Behrns, Kevin E, Bejarano, Eloy, Belaid, Amine, Belleudi, Francesca, Bénard, Giovanni, Berchem, Guy, Bergamaschi, Daniele, Bergami, Matteo, Berkhout, Ben, Berliocchi, Laura, Bernard, Amélie, Bernard, Monique, Bernassola, Francesca, Bertolotti, Anne, Bess, Amanda S, Besteiro, Sébastien, Bettuzzi, Saverio, Bhalla, Savita, Bhattacharyya, Shalmoli, Bhutia, Sujit K, Biagosch, Caroline, Bianchi, Michele Wolfe, Biard Piechaczyk, Martine, Billes, Viktor, Bincoletto, Claudia, Bingol, Bari, Bird, Sara W, Bitoun, Marc, Bjedov, Ivana, Blackstone, Craig, Blanc, Lionel, Blanco, Guillermo A, Blomhoff, Heidi Kiil, Boada Romero, Emilio, Böckler, Stefan, Boes, Marianne, Boesze Battaglia, Kathleen, Boise, Lawrence H, Bolino, Alessandra, Boman, Andrea, Bonaldo, Paolo, Bordi, Matteo, Bosch, Jürgen, Botana, Luis M, Botti, Joelle, Bou, German, Bouché, Marina, Bouchecareilh, Marion, Boucher, Marie Josée, Boulton, Michael E, Bouret, Sebastien G, Boya, Patricia, Boyer Guittaut, Michaël, Bozhkov, Peter V, Brady, Nathan, Braga, Vania Mm, Brancolini, Claudio, Braus, Gerhard H, Bravo San Pedro, José M, Brennan, Lisa A, Bresnick, Emery H, Brest, Patrick, Bridges, Dave, Bringer, Marie Agnè, Brini, Marisa, Brito, Glauber C, Brodin, Bertha, Brookes, Paul S, Brown, Eric J, Brown, Karen, Broxmeyer, Hal E, Bruhat, Alain, Brum, Patricia Chakur, Brumell, John H, BRUNETTI PIERRI, Nicola, Bryson Richardson, Robert J, Buch, Shilpa, Buchan, Alastair M, Budak, Hikmet, Bulavin, Dmitry V, Bultman, Scott J, Bultynck, Geert, Bumbasirevic, Vladimir, Burelle, Yan, Burke, Robert E, Burmeister, Margit, Bütikofer, Peter, Caberlotto, Laura, Cadwell, Ken, Cahova, Monika, Cai, Dongsheng, Cai, Jingjing, Cai, Qian, Calatayud, Sara, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Grant R, Campbell, Matthew, Campello, Silvia, Candau, Robin, Caniggia, Isabella, Cantoni, Lavinia, Cao, Lizhi, Caplan, Allan B, Caraglia, Michele, Cardinali, Claudio, Cardoso, Sandra Morai, Carew, Jennifer S, Carleton, Laura A, Carlin, Cathleen R, Carloni, Silvia, Carlsson, Sven R, Carmona Gutierrez, Didac, Carneiro, Leticia Am, Carnevali, Oliana, Carra, Serena, Carrier, Alice, Carroll, Bernadette, Casas, Caty, Casas, Josefina, Cassinelli, Giuliana, Castets, Perrine, Castro Obregon, Susana, Cavallini, Gabriella, Ceccherini, Isabella, Cecconi, Francesco, Cederbaum, Arthur I, Ceña, Valentín, Cenci, Simone, Cerella, Claudia, Cervia, Davide, Cetrullo, Silvia, Chaachouay, Hassan, Chae, Han Jung, Chagin, Andrei S, Chai, Chee Yin, Chakrabarti, Gopal, Chamilos, Georgio, Chan, Edmond Yw, Chan, Matthew Tv, Chandra, Dhyan, Chandra, Pallavi, Chang, Chih Peng, Chang, Raymond Chuen Chung, Chang, Ta Yuan, Chatham, John C, Chatterjee, Saurabh, Chauhan, Santosh, Che, Yongsheng, Cheetham, Michael E, Cheluvappa, Rajkumar, Chen, Chun Jung, Chen, Gang, Chen, Guang Chao, Chen, Guoqiang, Chen, Hongzhuan, Chen, Jeff W, Chen, Jian Kang, Chen, Min, Chen, Mingzhou, Chen, Peiwen, Chen, Qi, Chen, Quan, Chen, Shang Der, Chen, Si, Chen, Steve S. L, Chen, Wei, Chen, Wei Jung, Chen, Wen Qiang, Chen, Wenli, Chen, Xiangmei, Chen, Yau Hung, Chen, Ye Guang, Chen, Yin, Chen, Yingyu, Chen, Yongshun, Chen, Yu Jen, Chen, Yue Qin, Chen, Yujie, Chen, Zhen, Chen, Zhong, Cheng, Alan, Cheng, Christopher Hk, Cheng, Hua, Cheong, Heesun, Cherry, Sara, Chesney, Jason, Cheung, Chun Hei Antonio, Chevet, Eric, Chi, Hsiang Cheng, Chi, Sung Gil, Chiacchiera, Fulvio, Chiang, Hui Ling, Chiarelli, Roberto, Chiariello, Mario, Chieppa, Marcello, Chin, Lih Shen, Chiong, Mario, Chiu, Gigi Nc, Cho, Dong Hyung, Cho, Ssang Goo, Cho, William C, Cho, Yong Yeon, Cho, Young Seok, Choi, Augustine Mk, Choi, Eui Ju, Choi, Eun Kyoung, Choi, Jayoung, Choi, Mary E, Choi, Seung Il, Chou, Tsui Fen, Chouaib, Salem, Choubey, Divaker, Choubey, Vinay, Chow, Kuan Chih, Chowdhury, Kamal, Chu, Charleen T, Chuang, Tsung Hsien, Chun, Taehoon, Chung, Hyewon, Chung, Taijoon, Chung, Yuen Li, Chwae, Yong Joon, Cianfanelli, Valentina, Ciarcia, Roberto, Ciechomska, Iwona A, Ciriolo, Maria Rosa, Cirone, Mara, Claerhout, Sofie, Clague, Michael J, Clària, Joan, Clarke, Peter Gh, Clarke, Robert, Clementi, Emilio, Cleyrat, Cédric, Cnop, Miriam, Coccia, Eliana M, Cocco, Tiziana, Codogno, Patrice, Coers, Jörn, Cohen, Ezra Ew, Colecchia, David, Coletto, Luisa, Coll, Núria S, Colucci Guyon, Emma, Comincini, Sergio, Condello, Maria, Cook, Katherine L, Coombs, Graham H, Cooper, Cynthia D, Cooper, J. Mark, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corazzari, Marco, Corbalan, Ramon, Corcelle Termeau, Elisabeth, Cordero, Mario D, Corral Ramos, Cristina, Corti, Olga, Cossarizza, Andrea, Costelli, Paola, Costes, Safia, Cotman, Susan L, Coto Montes, Ana, Cottet, Sandra, Couve, Eduardo, Covey, Lori R, Cowart, L. Ashley, Cox, Jeffery S, Coxon, Fraser P, Coyne, Carolyn B, Cragg, Mark S, Craven, Rolf J, Crepaldi, Tiziana, Crespo, Jose L, Criollo, Alfredo, Crippa, Valeria, Cruz, Maria Teresa, Cuervo, Ana Maria, Cuezva, Jose M, Cui, Taixing, Cutillas, Pedro R, Czaja, Mark J, Czyzyk Krzeska, Maria F, Dagda, Ruben K, Dahmen, Uta, Dai, Chunsun, Dai, Wenjie, Dai, Yun, Dalby, Kevin N, Dalla Valle, Luisa, Dalmasso, Guillaume, D'Amelio, Marcello, Damme, Marku, Darfeuille Michaud, Arlette, Dargemont, Catherine, Darley Usmar, Victor M, Dasarathy, Srinivasan, Dasgupta, Biplab, Dash, Srikanta, Dass, Crispin R, Davey, Hazel Marie, Davids, Lester M, Dávila, David, Davis, Roger J, Dawson, Ted M, Dawson, Valina L, Daza, Paula, de Belleroche, Jackie, de Figueiredo, Paul, de Figueiredo, Regina Celia Bressan Queiroz, de la Fuente, José, DE MARTINO, Luisa, De Matteis, Antonella, De Meyer, Guido Ry, De Milito, Angelo, De Santi, Mauro, de Souza, Wanderley, De Tata, Vincenzo, De Zio, Daniela, Debnath, Jayanta, Dechant, Reinhard, Decuypere, Jean Paul, Deegan, Shane, Dehay, Benjamin, Del Bello, Barbara, Del Re, Dominic P, Delage Mourroux, Régi, Delbridge, Lea Md, Deldicque, Louise, Delorme Axford, Elizabeth, Deng, Yizhen, Dengjel, Joern, Denizot, Melanie, Dent, Paul, Der, Channing J, Deretic, Vojo, Derrien, Benoît, Deutsch, Eric, Devarenne, Timothy P, Devenish, Rodney J, Di Bartolomeo, Sabrina, Di Daniele, Nicola, Di Domenico, Fabio, Di Nardo, Alessia, Di Paola, Simone, Di Pietro, Antonio, Di Renzo, Livia, Diantonio, Aaron, Díaz Araya, Guillermo, Díaz Laviada, Ine, Diaz Meco, Maria T, Diaz Nido, Javier, Dickey, Chad A, Dickson, Robert C, Diederich, Marc, Digard, Paul, Dikic, Ivan, Dinesh Kumar, Savithrama P, Ding, Chan, Ding, Wen Xing, Ding, Zufeng, Dini, Luciana, Distler, Jörg Hw, Diwan, Abhinav, Djavaheri Mergny, Mojgan, Dmytruk, Kostyantyn, Dobson, Renwick Cj, Doetsch, Volker, Dokladny, Karol, Dokudovskaya, Svetlana, Donadelli, Massimo, Dong, X. Charlie, Dong, Xiaonan, Dong, Zheng, Donohue, Terrence M, Doran, Kelly S, D'Orazi, Gabriella, Dorn, Gerald W, Dosenko, Victor, Dridi, Sami, Drucker, Liat, Du, Jie, Du, Li Lin, Du, Lihuan, du Toit, André, Dua, Priyamvada, Duan, Lei, Duann, Pu, Dubey, Vikash Kumar, Duchen, Michael R, Duchosal, Michel A, Duez, Helene, Dugail, Isabelle, Dumit, Verónica I, Duncan, Mara C, Dunlop, Elaine A, Dunn, William A, Dupont, Nicola, Dupuis, Luc, Durán, Raúl V, Durcan, Thomas M, Duvezin Caubet, Stéphane, Duvvuri, Umamaheswar, Eapen, Vinay, Ebrahimi Fakhari, Dariu, Echard, Arnaud, Eckhart, Leopold, Edelstein, Charles L, Edinger, Aimee L, Eichinger, Ludwig, Eisenberg, Tobia, Eisenberg Lerner, Avital, Eissa, N. Tony, El Deiry, Wafik S, El Khoury, Victoria, Elazar, Zvulun, Eldar Finkelman, Hagit, Elliott, Chris Jh, Emanuele, Enzo, Emmenegger, Urban, Engedal, Nikolai, Engelbrecht, Anna Mart, Engelender, Simone, Enserink, Jorrit M, Erdmann, Ralf, Erenpreisa, Jekaterina, Eri, Rajaraman, Eriksen, Jason L, Erman, Andreja, Escalante, Ricardo, Eskelinen, Eeva Liisa, Espert, Lucile, Esteban Martínez, Lorena, Evans, Thomas J, Fabri, Mario, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Færgeman, Nils J, Faggioni, Alberto, Fairlie, W. Dougla, Fan, Chunhai, Fan, Daping, Fan, Jie, Fang, Shengyun, Fanto, Manoli, Fanzani, Alessandro, Farkas, Thoma, Faure, Mathia, Favier, Francois B, Fearnhead, Howard, Federici, Massimo, Fei, Erkang, Felizardo, Tania C, Feng, Hua, Feng, Yibin, Feng, Yuchen, Ferguson, Thomas A, Fernández, Álvaro F, Fernandez Barrena, Maite G, Fernandez Checa, Jose C, Fernández López, Arsenio, Fernandez Zapico, Martin E, Feron, Olivier, Ferraro, Elisabetta, Ferreira Halder, Carmen Veríssima, Fesus, Laszlo, Feuer, Ralph, Fiesel, Fabienne C, Filippi Chiela, Eduardo C, Filomeni, Giuseppe, Fimia, Gian Maria, Fingert, John H, Finkbeiner, Steven, Finkel, Toren, Fiorito, Filomena, Fisher, Paul B, Flajolet, Marc, Flamigni, Flavio, Florey, Oliver, Florio, Salvatore, Floto, R. Andre, Folini, Marco, Follo, Carlo, Fon, Edward A, Fornai, Francesco, Fortunato, Franco, Fraldi, Alessandro, Franco, Rodrigo, Francois, Arnaud, François, Aurélie, Frankel, Lisa B, Fraser, Iain Dc, Frey, Norbert, Freyssenet, Damien G, Frezza, Christian, Friedman, Scott L, Frigo, Daniel E, Fu, Dongxu, Fuentes, José M, Fueyo, Juan, Fujitani, Yoshio, Fujiwara, Yuuki, Fujiya, Mikihiro, Fukuda, Mitsunori, Fulda, Simone, Fusco, Carmela, Gabryel, Bozena, Gaestel, Matthia, Gailly, Philippe, Gajewska, Malgorzata, Galadari, Sehamuddin, Galili, Gad, Galindo, Inmaculada, Galindo, Maria F, Galliciotti, Giovanna, Galluzzi, Lorenzo, Galluzzi, Luca, Galy, Vincent, Gammoh, Noor, Gandy, Sam, Ganesan, Anand K, Ganesan, Swamynathan, Ganley, Ian G, Gannagé, Monique, Gao, Fen Biao, Gao, Feng, Gao, Jian Xin, García Nannig, Lorena, García Véscovi, Eleonora, Garcia Macía, Marina, Garcia Ruiz, Carmen, Garg, Abhishek D, Garg, Pramod Kumar, Gargini, Ricardo, Gassen, Nils Christian, Gatica, Damián, Gatti, Evelina, Gavard, Julie, Gavathiotis, Evripidi, Ge, Liang, Ge, Pengfei, Ge, Shengfang, Gean, Po Wu, Gelmetti, Vania, Genazzani, Armando A, Geng, Jiefei, Genschik, Pascal, Gerner, Lisa, Gestwicki, Jason E, Gewirtz, David A, Ghavami, Saeid, Ghigo, Eric, Ghosh, Debabrata, Giammarioli, Anna Maria, Giampieri, Francesca, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibbings, Derrick J, Gibellini, Lara, Gibson, Spencer B, Ginet, Vanessa, Giordano, Antonio, Giorgini, Flaviano, Giovannetti, Elisa, Girardin, Stephen E, Gispert, Suzana, Giuliano, Sandy, Gladson, Candece L, Glavic, Alvaro, Gleave, Martin, Godefroy, Nelly, Gogal, Robert M, Gokulan, Kuppan, Goldman, Gustavo H, Goletti, Delia, Goligorsky, Michael S, Gomes, Aldrin V, Gomes, Ligia C, Gomez, Hernando, Gomez Manzano, Candelaria, Gómez Sánchez, Rubén, Gonçalves, Dawit Ap, Goncu, Ebru, Gong, Qingqiu, Gongora, Céline, Gonzalez, Carlos B, Gonzalez Alegre, Pedro, Gonzalez Cabo, Pilar, González Polo, Rosa Ana, Goping, Ing Swie, Gorbea, Carlo, Gorbunov, Nikolai V, Goring, Daphne R, Gorman, Adrienne M, Gorski, Sharon M, Goruppi, Sandro, Goto Yamada, Shino, Gotor, Cecilia, Gottlieb, Roberta A, Gozes, Illana, Gozuacik, Devrim, Graba, Yacine, Graef, Martin, Granato, Giovanna E, Grant, Gary Dean, Grant, Steven, Gravina, Giovanni Luca, Green, Douglas R, Greenhough, Alexander, Greenwood, Michael T, Grimaldi, Benedetto, Gros, Frédéric, Grose, Charle, Groulx, Jean Francoi, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Guan, Jun Lin, Guan, Kun Liang, Guerra, Barbara, Guillen, Carlo, Gulshan, Kailash, Gunst, Jan, Guo, Chuanyong, Guo, Lei, Guo, Ming, Guo, Wenjie, Guo, Xu Guang, Gust, Andrea A, Gustafsson, Åsa B, Gutierrez, Elaine, Gutierrez, Maximiliano G, Gwak, Ho Shin, Haas, Albert, Haber, James E, Hadano, Shinji, Hagedorn, Monica, Hahn, David R, Halayko, Andrew J, Hamacher Brady, Anne, Hamada, Kozo, Hamai, Ahmed, Hamann, Andrea, Hamasaki, Maho, Hamer, Isabelle, Hamid, Qutayba, Hammond, Ester M, Han, Feng, Han, Weidong, Handa, James T, Hanover, John A, Hansen, Malene, Harada, Masaru, Harhaji Trajkovic, Ljubica, Harper, J. Wade, Harrath, Abdel Halim, Harris, Adrian L, Harris, Jame, Hasler, Udo, Hasselblatt, Peter, Hasui, Kazuhisa, Hawley, Robert G, Hawley, Teresa S, He, Congcong, He, Cynthia Y, He, Fengtian, He, Gu, He, Rong Rong, He, Xian Hui, He, You Wen, He, Yu Ying, Heath, Joan K, Hébert, Marie Josée, Heinzen, Robert A, Helgason, Gudmundur Vignir, Hensel, Michael, Henske, Elizabeth P, Her, Chengtao, Herman, Paul K, Hernández, Agustín, Hernandez, Carlo, Hernández Tiedra, Sonia, Hetz, Claudio, Hiesinger, P. Robin, Higaki, Katsumi, Hilfiker, Sabine, Hill, Bradford G, Hill, Joseph A, Hill, William D, Hino, Keisuke, Hofius, Daniel, Hofman, Paul, Höglinger, Günter U, Höhfeld, Jörg, Holz, Marina K, Hong, Yonggeun, Hood, David A, Hoozemans, Jeroen Jm, Hoppe, Thorsten, Hsu, Chin, Hsu, Chin Yuan, Hsu, Li Chung, Hu, Dong, Hu, Guochang, Hu, Hong Ming, Hu, Hongbo, Hu, Ming Chang, Hu, Yu Chen, Hu, Zhuo Wei, Hua, Fang, Hua, Ya, Huang, Canhua, Huang, Huey Lan, Huang, Kuo How, Huang, Kuo Yang, Huang, Shile, Huang, Shiqian, Huang, Wei Pang, Huang, Yi Ran, Huang, Yong, Huang, Yunfei, Huber, Tobias B, Huebbe, Patricia, Huh, Won Ki, Hulmi, Juha J, Hur, Gang Min, Hurley, James H, Husak, Zvenyslava, Hussain, Sabah Na, Hussain, Salik, Hwang, Jung Jin, Hwang, Seungmin, Hwang, Thomas I, Ichihara, Atsuhiro, Imai, Yuzuru, Imbriano, Carol, Inomata, Megumi, Into, Takeshi, Iovane, Valentina, Iovanna, Juan L, Iozzo, Renato V, Ip, Nancy Y, Irazoqui, Javier E, Iribarren, Pablo, Isaka, Yoshitaka, Isakovic, Aleksandra J, Ischiropoulos, Harry, Isenberg, Jeffrey S, Ishaq, Mohammad, Ishida, Hiroyuki, Ishii, Isao, Ishmael, Jane E, Isidoro, Ciro, Isobe, Ken Ichi, Isono, Erika, Issazadeh Navikas, Shohreh, Itahana, Koji, Itakura, Eisuke, Ivanov, Andrei I, Iyer, Anand Krishnan V, Izquierdo, José M, Izumi, Yotaro, Izzo, Valentina, Jäättelä, Marja, Jaber, Nadia, Jackson, Daniel John, Jackson, William T, Jacob, Tony George, Jacques, Thomas S, Jagannath, Chinnaswamy, Jain, Ashish, Jana, Nihar Ranjan, Jang, Byoung Kuk, Jani, Alkesh, Janji, Bassam, Jannig, Paulo Roberto, Jansson, Patric J, Jean, Steve, Jendrach, Marina, Jeon, Ju Hong, Jessen, Niel, Jeung, Eui Bae, Jia, Kailiang, Jia, Lijun, Jiang, Hong, Jiang, Hongchi, Jiang, Liwen, Jiang, Teng, Jiang, Xiaoyan, Jiang, Xuejun, Jiang, Ying, Jiang, Yongjun, Jiménez, Alberto, Jin, Cheng, Jin, Hongchuan, Jin, Lei, Jin, Meiyan, Jin, Shengkan, Jinwal, Umesh Kumar, Jo, Eun Kyeong, Johansen, Terje, Johnson, Daniel E, Johnson, Gail Vw, Johnson, James D, Jonasch, Eric, Jones, Chri, Joosten, Leo Ab, Jordan, Joaquin, Joseph, Anna Maria, Joseph, Bertrand, Joubert, Annie M, Ju, Dianwen, Ju, Jingfang, Juan, Hsueh Fen, Juenemann, Katrin, Juhász, Gábor, Jung, Hye Seung, Jung, Jae U, Jung, Yong Keun, Jungbluth, Heinz, Justice, Matthew J, Jutten, Barry, Kaakoush, Nadeem O, Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kaeffer, Bertrand, Kågedal, Katarina, Kahana, Alon, Kajimura, Shingo, Kakhlon, Or, Kalia, Manjula, Kalvakolanu, Dhan V, Kamada, Yoshiaki, Kambas, Konstantino, Kaminskyy, Vitaliy O, Kampinga, Harm H, Kandouz, Mustapha, Kang, Chanhee, Kang, Rui, Kang, Tae Cheon, Kanki, Tomotake, Kanneganti, Thirumala Devi, Kanno, Haruo, Kanthasamy, Anumantha G, Kantorow, Marc, Kaparakis Liaskos, Maria, Kapuy, Orsolya, Karantza, Vassiliki, Karim, Md Razaul, Karmakar, Parimal, Kaser, Arthur, Kaushik, Susmita, Kawula, Thoma, Kaynar, A. Murat, Ke, Po Yuan, Ke, Zun Ji, Kehrl, John H, Keller, Kate E, Kemper, Jongsook Kim, Kenworthy, Anne K, Kepp, Oliver, Kern, Andrea, Kesari, Santosh, Kessel, David, Ketteler, Robin, Kettelhut, Isis do Carmo, Khambu, Bilon, Khan, Muzamil Majid, Khandelwal, Vinoth Km, Khare, Sangeeta, Kiang, Juliann G, Kiger, Amy A, Kihara, Akio, Kim, Arianna L, Kim, Cheol Hyeon, Kim, Deok Ryong, Kim, Do Hyung, Kim, Eung Kweon, Kim, Hye Young, Kim, Hyung Ryong, Kim, Jae Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, Jin Hyoung, Kim, Kwang Woon, Kim, Michael D, Kim, Moon Moo, Kim, Peter K, Kim, Seong Who, Kim, Soo Youl, Kim, Yong Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C, Kimura, Tomonori, King, Jason S, Kirkegaard, Karla, Kirkin, Vladimir, Kirshenbaum, Lorrie A, Kishi, Shuji, Kitajima, Yasuo, Kitamoto, Katsuhiko, Kitaoka, Yasushi, Kitazato, Kaio, Kley, Rudolf A, Klimecki, Walter T, Klinkenberg, Michael, Klucken, Jochen, Knævelsrud, Helene, Knecht, Erwin, Knuppertz, Laura, Ko, Jiunn Liang, Kobayashi, Satoru, Koch, Jan C, Koechlin Ramonatxo, Christelle, Koenig, Ulrich, Koh, Young Ho, Köhler, Katja, Kohlwein, Sepp D, Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Dexin, Kong, Hee Jeong, Konstantakou, Eumorphia G, Kopp, Benjamin T, Korcsmaros, Tama, Korhonen, Laura, Korolchuk, Viktor I, Koshkina, Nadya V, Kou, Yanjun, Koukourakis, Michael I, Koumenis, Constantino, Kovács, Attila L, Kovács, Tibor, Kovacs, Werner J, Koya, Daisuke, Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kravic Stevovic, Tamara, Krek, Wilhelm, Kretz Remy, Carole, Krick, Roswitha, Krishnamurthy, Malathi, Kriston Vizi, Jano, Kroemer, Guido, Kruer, Michael C, Kruger, Rejko, Ktistakis, Nicholas T, Kuchitsu, Kazuyuki, Kuhn, Christian, Kumar, Addanki Pratap, Kumar, Anuj, Kumar, Ashok, Kumar, Deepak, Kumar, Dhiraj, Kumar, Rakesh, Kumar, Sharad, Kundu, Mondira, Kung, Hsing Jien, Kuno, Atsushi, Kuo, Sheng Han, Kuret, Jeff, Kurz, Tino, Kwok, Terry, Kwon, Taeg Kyu, Kwon, Yong Tae, Kyrmizi, Irene, La Spada, Albert R, Lafont, Frank, Lahm, Tim, Lakkaraju, Aparna, Lam, Truong, Lamark, Trond, Lancel, Steve, Landowski, Terry H, Lane, Darius J. R, Lane, Jon D, Lanzi, Cinzia, Lapaquette, Pierre, Lapierre, Louis R, Laporte, Jocelyn, Laukkarinen, Johanna, Laurie, Gordon W, Lavandero, Sergio, Lavie, Lena, Lavoie, Matthew J, Law, Betty Yuen Kwan, Law, Helen Ka Wai, Law, Kelsey B, Layfield, Robert, Lazo, Pedro A, Le Cam, Laurent, Le Roch, Karine G, Le Stunff, Hervé, Leardkamolkarn, Vijittra, Lecuit, Marc, Lee, Byung Hoon, Lee, Che Hsin, Lee, Erinna F, Lee, Gyun Min, Lee, He Jin, Lee, Hsinyu, Lee, Jae Keun, Lee, Jongdae, Lee, Ju Hyun, Lee, Jun Hee, Lee, Michael, Lee, Myung Shik, Lee, Patty J, Lee, Sam W, Lee, Seung Jae, Lee, Shiow Ju, Lee, Stella Y, Lee, Sug Hyung, Lee, Sung Sik, Lee, Sung Joon, Lee, Sunhee, Lee, Ying Ray, Lee, Yong J, Lee, Young H, Leeuwenburgh, Christiaan, Lefort, Sylvain, Legouis, Renaud, Lei, Jinzhi, Lei, Qun Ying, Leib, David A, Leibowitz, Gil, Lekli, Istvan, Lemaire, Stéphane D, Lemasters, John J, Lemberg, Marius K, Lemoine, Antoinette, Leng, Shuilong, Lenz, Guido, Lenzi, Paola, Lerman, Lilach O, Lettieri Barbato, Daniele, Leu, Julia I. Ju, Leung, Hing Y, Levine, Beth, Lewis, Patrick A, Lezoualc'H, Frank, Li, Chi, Li, Faqiang, Li, Feng Jun, Li, Jun, Li, Ke, Li, Lian, Li, Min, Li, Qiang, Li, Rui, Li, Sheng, Li, Wei, Li, Xiaotao, Li, Yumin, Lian, Jiqin, Liang, Chengyu, Liang, Qiangrong, Liao, Yulin, Liberal, Joana, Liberski, Pawel P, Lie, Pearl, Lieberman, Andrew P, Lim, Hyunjung Jade, Lim, Kah Leong, Lim, Kyu, Lima, Raquel T, Lin, Chang Shen, Lin, Chiou Feng, Lin, Fang, Lin, Fangming, Lin, Fu Cheng, Lin, Kui, Lin, Kwang Huei, Lin, Pei Hui, Lin, Tianwei, Lin, Wan Wan, Lin, Yee Shin, Lin, Yong, Linden, Rafael, Lindholm, Dan, Lindqvist, Lisa M, Lingor, Paul, Linkermann, Andrea, Liotta, Lance A, Lipinski, Marta M, Lira, Vitor A, Lisanti, Michael P, Liton, Paloma B, Liu, Bo, Liu, Chong, Liu, Chun Feng, Liu, Fei, Liu, Hung Jen, Liu, Jianxun, Liu, Jing Jing, Liu, Jing Lan, Liu, Ke, Liu, Leyuan, Liu, Liang, Liu, Quentin, Liu, Rong Yu, Liu, Shiming, Liu, Shuwen, Liu, Wei, Liu, Xian De, Liu, Xiangguo, Liu, Xiao Hong, Liu, Xinfeng, Liu, Xu, Liu, Xueqin, Liu, Yang, Liu, Yule, Liu, Zexian, Liu, Zhe, Liuzzi, Juan P, Lizard, Gérard, Ljujic, Mila, Lodhi, Irfan J, Logue, Susan E, Lokeshwar, Bal L, Long, Yun Chau, Lonial, Sagar, Loos, Benjamin, López Otín, Carlo, López Vicario, Cristina, Lorente, Mar, Lorenzi, Philip L, Lõrincz, Péter, Los, Marek, Lotze, Michael T, Lovat, Penny E, Lu, Binfeng, Lu, Bo, Lu, Jiahong, Lu, Qing, Lu, She Min, Lu, Shuyan, Lu, Yingying, Luciano, Frédéric, Luckhart, Shirley, Lucocq, John Milton, Ludovico, Paula, Lugea, Aurelia, Lukacs, Nicholas W, Lum, Julian J, Lund, Anders H, Luo, Honglin, Luo, Jia, Luo, Shouqing, Luparello, Claudio, Lyons, Timothy, Ma, Jianjie, Ma, Yi, Ma, Yong, Ma, Zhenyi, Machado, Juliano, Machado Santelli, Glaucia M, Macian, Fernando, Macintosh, Gustavo C, Mackeigan, Jeffrey P, Macleod, Kay F, Macmicking, John D, MacMillan Crow, Lee Ann, Madeo, Frank, Madesh, Muniswamy, Madrigal Matute, Julio, Maeda, Akiko, Maeda, Tatsuya, Maegawa, Gustavo, Maellaro, Emilia, Maes, Hannelore, Magariños, Marta, Maiese, Kenneth, Maiti, Tapas K, Maiuri, Luigi, Maiuri, MARIA CHIARA, Maki, Carl G, Malli, Roland, Malorni, Walter, Maloyan, Alina, Mami Chouaib, Fathia, Man, Na, Mancias, Joseph D, Mandelkow, Eva Maria, Mandell, Michael A, Manfredi, Angelo A, Manié, Serge N, Manzoni, Claudia, Mao, Kai, Mao, Zixu, Mao, Zong Wan, Marambaud, Philippe, Marconi, Anna Maria, Marelja, Zvonimir, Marfe, Gabriella, Margeta, Marta, Margittai, Eva, Mari, Muriel, Mariani, Francesca V, Marin, Concepcio, Marinelli, Sara, Mariño, Guillermo, Markovic, Ivanka, Marquez, Rebecca, Martelli, Alberto M, Martens, Sascha, Martin, Katie R, Martin, Seamus J, Martin, Shaun, Martin Acebes, Miguel A, Martín Sanz, Paloma, Martinand Mari, Camille, Martinet, Wim, Martinez, Jennifer, Martinez Lopez, Nuria, Martinez Outschoorn, Ubaldo, Martínez Velázquez, Moisé, Martinez Vicente, Marta, Martins, Waleska Kerllen, Mashima, Hirosato, Mastrianni, James A, Matarese, Giuseppe, Matarrese, Paola, Mateo, Roberto, Matoba, Satoaki, Matsumoto, Naomichi, Matsushita, Takehiko, Matsuura, Akira, Matsuzawa, Takeshi, Mattson, Mark P, Matus, Soledad, Maugeri, Norma, Mauvezin, Caroline, Mayer, Andrea, Maysinger, Dusica, Mazzolini, Guillermo D, Mcbrayer, Mary Kate, Mccall, Kimberly, Mccormick, Craig, Mcinerney, Gerald M, Mciver, Skye C, Mckenna, Sharon, Mcmahon, John J, Mcneish, Iain A, Mechta Grigoriou, Fatima, Medema, Jan Paul, Medina, Diego L, Megyeri, Klara, Mehrpour, Maryam, Mehta, Jawahar L, Mei, Yide, Meier, Ute Christiane, Meijer, Alfred J, Meléndez, Alicia, Melino, Gerry, Melino, Sonia, de Melo, Edesio Jose Tenorio, Mena, Maria A, Meneghini, Marc D, Menendez, Javier A, Menezes, Regina, Meng, Liesu, Meng, Ling Hua, Meng, Songshu, Menghini, Rossella, Menko, A. Sue, Menna Barreto, Rubem F, Menon, Manoj B, Meraz Ríos, Marco A, Merla, Giuseppe, Merlini, Luciano, Merlot, Angelica M, Meryk, Andrea, Meschini, Stefania, Meyer, Joel N, Mi, Man Tian, Miao, Chao Yu, Micale, Lucia, Michaeli, Simon, Michiels, Carine, Migliaccio, Anna Rita, Mihailidou, Anastasia Susie, Mijaljica, Dalibor, Mikoshiba, Katsuhiko, Milan, Enrico, Miller Fleming, Leonor, Mills, Gordon B, Mills, Ian G, Minakaki, Georgia, Minassian, Berge A, Ming, Xiu Fen, Minibayeva, Farida, Minina, Elena A, Mintern, Justine D, Minucci, Saverio, Miranda Vizuete, Antonio, Mitchell, Claire H, Miyamoto, Shigeki, Miyazawa, Keisuke, Mizushima, Noboru, Mnich, Katarzyna, Mograbi, Baharia, Mohseni, Simin, Moita, Luis Ferreira, Molinari, Marco, Molinari, Maurizio, Møller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Mongillo, Marco, Monick, Martha M, Montagnaro, Serena, Montell, Craig, Moore, Darren J, Moore, Michael N, Mora Rodriguez, Rodrigo, Moreira, Paula I, Morel, Etienne, Morelli, Maria Beatrice, Moreno, Sandra, Morgan, Michael J, Moris, Arnaud, Moriyasu, Yuji, Morrison, Janna L, Morrison, Lynda A, Morselli, Eugenia, Moscat, Jorge, Moseley, Pope L, Mostowy, Serge, Motori, Elisa, Mottet, Deni, Mottram, Jeremy C, Moussa, Charbel E. H, Mpakou, Vassiliki E, Mukhtar, Hasan, Mulcahy Levy, Jean M, Muller, Sylviane, Muñoz Moreno, Raquel, Muñoz Pinedo, Cristina, Münz, Christian, Murphy, Maureen E, Murray, James T, Murthy, Aditya, Mysorekar, Indira U, Nabi, Ivan R, Nabissi, Massimo, Nader, Gustavo A, Nagahara, Yukitoshi, Nagai, Yoshitaka, Nagata, Kazuhiro, Nagelkerke, Anika, Nagy, Péter, Naidu, Samisubbu R, Nair, Sreejayan, Nakano, Hiroyasu, Nakatogawa, Hitoshi, Nanjundan, Meera, Napolitano, Gennaro, Naqvi, Naweed I, Nardacci, Roberta, Narendra, Derek P, Narita, Masashi, Nascimbeni, Anna Chiara, Natarajan, Ramesh, Navegantes, Luiz C, Nawrocki, Steffan T, Nazarko, Taras Y, Nazarko, Volodymyr Y, Neill, Thoma, Neri, Luca M, Netea, Mihai G, Netea Maier, Romana T, Neves, Bruno M, Ney, Paul A, Nezis, Ioannis P, Nguyen, Hang Tt, Nguyen, Huu Phuc, Nicot, Anne Sophie, Nilsen, Hilde, Nilsson, Per, Nishimura, Mikio, Nishino, Ichizo, Niso Santano, Mireia, Niu, Hua, Nixon, Ralph A, Njar, Vincent Co, Noda, Takeshi, Noegel, Angelika A, Nolte, Elsie Magdalena, Norberg, Erik, Norga, Koenraad K, Noureini, Sakineh Kazemi, Notomi, Shoji, Notterpek, Lucia, Nowikovsky, Karin, Nukina, Nobuyuki, Nürnberger, Thorsten, O'Donnell, Valerie B, O'Donovan, Tracey, O'Dwyer, Peter J, Oehme, Ina, Oeste, Clara L, Ogawa, Michinaga, Ogretmen, Besim, Ogura, Yuji, Oh, Young J, Ohmuraya, Masaki, Ohshima, Takayuki, Ojha, Rani, Okamoto, Koji, Okazaki, Toshiro, Oliver, F. Javier, Ollinger, Karin, Olsson, Stefan, Orban, Daniel P, Ordonez, Paulina, Orhon, Idil, Orosz, Laszlo, O'Rourke, Eyleen J, Orozco, Helena, Ortega, Angel L, Ortona, Elena, Osellame, Laura D, Oshima, Junko, Oshima, Shigeru, Osiewacz, Heinz D, Otomo, Takanobu, Otsu, Kinya, Ou, Jing Hsiung Jame, Outeiro, Tiago F, Ouyang, Dong Yun, Ouyang, Hongjiao, Overholtzer, Michael, Ozbun, Michelle A, Ozdinler, P. Hande, Ozpolat, Bulent, Pacelli, Consiglia, Paganetti, Paolo, Page, Guylène, Pages, Gille, Pagnini, Ugo, Pajak, Beata, Pak, Stephen C, Pakos Zebrucka, Karolina, Pakpour, Nazzy, Palková, Zdena, Palladino, Francesca, Pallauf, Kathrin, Pallet, Nicola, Palmieri, Marta, Paludan, Søren R, Palumbo, Camilla, Palumbo, Silvia, Pampliega, Olatz, Pan, Hongming, Pan, Wei, Panaretakis, Theochari, Pandey, Aseem, Pantazopoulou, Areti, Papackova, Zuzana, Papademetrio, Daniela L, Papassideri, Issidora, Papini, Alessio, Parajuli, Nirmala, Pardo, Julian, Parekh, Vrajesh V, Parenti, Giancarlo, Park, Jong In, Park, Junsoo, Park, Ohkmae K, Parker, Roy, Parlato, Rosanna, Parys, Jan B, Parzych, Katherine R, Pasquet, Jean Max, Pasquier, Benoit, Pasumarthi, Kishore B, Patschan, Daniel, Patterson, Cam, Pattingre, Sophie, Pattison, Scott, Pause, Arnim, Pavenstädt, Hermann, Pavone, Flaminia, Pedrozo, Zully, Peña, Fernando J, Peñalva, Miguel A, Pende, Mario, Peng, Jianxin, Penna, Fabio, Penninger, Josef M, Pensalfini, Anna, Pepe, Salvatore, Pereira, Gustavo J, Pereira, Paulo C, Pérez de la Cruz, Verónica, Pérez Pérez, María Esther, Pérez Rodríguez, Diego, Pérez Sala, Dolore, Perier, Celine, Perl, Andra, Perlmutter, David H, Perrotta, Ida, Pervaiz, Shazib, Pesonen, Maija, Pessin, Jeffrey E, Peters, Godefridus J, Petersen, Morten, Petrache, Irina, Petrof, Basil J, Petrovski, Goran, Phang, James M, Piacentini, Mauro, Pierdominici, Marina, Pierre, Philippe, Pierrefite Carle, Valérie, Pietrocola, Federico, Pimentel Muiños, Felipe X, Pinar, Mario, Pineda, Benjamin, Pinkas Kramarski, Ronit, Pinti, Marcello, Pinton, Paolo, Piperdi, Bilal, Piret, James M, Platanias, Leonidas C, Platta, Harald W, Plowey, Edward D, Pöggeler, Stefanie, Poirot, Marc, Polčic, Peter, Poletti, Angelo, Poon, Audrey H, Popelka, Hana, Popova, Blagovesta, Poprawa, Izabela, Poulose, Shibu M, Poulton, Joanna, Powers, Scott K, Powers, Ted, Pozuelo Rubio, Mercede, Prak, Krisna, Prange, Reinhild, Prescott, Mark, Priault, Muriel, Prince, Sharon, Proia, Richard L, Proikas Cezanne, Tassula, Prokisch, Holger, Promponas, Vasilis J, Przyklenk, Karin, Puertollano, Rosa, Pugazhenthi, Subbiah, Puglielli, Luigi, Pujol, Aurora, Puyal, Julien, Pyeon, Dohun, Qi, Xin, Qian, Wen Bin, Qin, Zheng Hong, Qiu, Yu, Qu, Ziwei, Quadrilatero, Joe, Quinn, Frederick, Raben, Nina, Rabinowich, Hannah, Radogna, Flavia, Ragusa, Michael J, Rahmani, Mohamed, Raina, Komal, Ramanadham, Sasanka, Ramesh, Rajagopal, Rami, Abdelhaq, Randall Demllo, Sarron, Randow, Felix, Rao, Hai, Rao, V. Ashutosh, Rasmussen, Blake B, Rasse, Tobias M, Ratovitski, Edward A, Rautou, Pierre Emmanuel, Ray, Swapan K, Razani, Babak, Reed, Bruce H, Reggiori, Fulvio, Rehm, Marku, Reichert, Andreas S, Rein, Theo, Reiner, David J, Reits, Eric, Ren, Jun, Ren, Xingcong, Renna, Maurizio, Reusch, Jane Eb, Revuelta, Jose L, Reyes, Leticia, Rezaie, Alireza R, Richards, Robert I, Richardson, Des R, Richetta, Clémence, Riehle, Michael A, Rihn, Bertrand H, Rikihisa, Yasuko, Riley, Brigit E, Rimbach, Gerald, Rippo, Maria Rita, Ritis, Konstantino, Rizzi, Federica, Rizzo, Elizete, Roach, Peter J, Robbins, Jeffrey, Roberge, Michel, Roca, Gabriela, Roccheri, Maria Carmela, Rocha, Sonia, Rodrigues, Cecilia Mp, Rodríguez, Clara I, de Cordoba, Santiago Rodriguez, Rodriguez Muela, Natalia, Roelofs, Jeroen, Rogov, Vladimir V, Rohn, Troy T, Rohrer, Bärbel, Romanelli, Davide, Romani, Luigina, Romano, Patricia Silvia, Roncero, M. Isabel G, Rosa, Jose Lui, Rosello, Alicia, Rosen, Kirill V, Rosenstiel, Philip, Rost Roszkowska, Magdalena, Roth, Kevin A, Roué, Gael, Rouis, Mustapha, Rouschop, Kasper M, Ruan, Daniel T, Ruano, Diego, Rubinsztein, David C, Rucker, Edmund B, Rudich, Assaf, Rudolf, Emil, Rudolf, Ruediger, Ruegg, Markus A, Ruiz Roldan, Carmen, Ruparelia, Avnika Ashok, Rusmini, Paola, Russ, David W, Russo, Gian Luigi, Russo, Giuseppe, Russo, Rossella, Rusten, Tor Erik, Ryabovol, Victoria, Ryan, Kevin M, Ryter, Stefan W, Sabatini, David M, Sacher, Michael, Sachse, Carsten, Sack, Michael N, Sadoshima, Junichi, Saftig, Paul, Sagi Eisenberg, Ronit, Sahni, Sumit, Saikumar, Pothana, Saito, Tsunenori, Saitoh, Tatsuya, Sakakura, Koichi, Sakoh Nakatogawa, Machiko, Sakuraba, Yasuhito, Salazar Roa, María, Salomoni, Paolo, Saluja, Ashok K, Salvaterra, Paul M, Salvioli, Rosa, Samali, Afshin, Sanchez, Anthony Mj, Sánchez Alcázar, José A, Sanchez Prieto, Ricardo, Sandri, Marco, Sanjuan, Miguel A, Santaguida, Stefano, Santambrogio, Laura, Santoni, Giorgio, Dos Santos, Claudia Nune, Saran, Shweta, Sardiello, Marco, Sargent, Graeme, Sarkar, Pallabi, Sarkar, Sovan, Sarrias, Maria Rosa, Sarwal, Minnie M, Sasakawa, Chihiro, Sasaki, Motoko, Sass, Miklo, Sato, Ken, Sato, Miyuki, Satriano, Joseph, Savaraj, Niramol, Saveljeva, Svetlana, Schaefer, Liliana, Schaible, Ulrich E, Scharl, Michael, Schatzl, Hermann M, Schekman, Randy, Scheper, Wiep, Schiavi, Alfonso, Schipper, Hyman M, Schmeisser, Hana, Schmidt, Jen, Schmitz, Ingo, Schneider, Bianca E, Schneider, E. Marion, Schneider, Jaime L, Schon, Eric A, Schönenberger, Miriam J, Schönthal, Axel H, Schorderet, Daniel F, Schröder, Bernd, Schuck, Sebastian, Schulze, Ryan J, Schwarten, Melanie, Schwarz, Thomas L, Sciarretta, Sebastiano, Scotto, Kathleen, Scovassi, A. Ivana, Screaton, Robert A, Screen, Mark, Seca, Hugo, Sedej, Simon, Segatori, Laura, Segev, Nava, Seglen, Per O, Seguí Simarro, Jose M, Segura Aguilar, Juan, Seki, Ekihiro, Sell, Christian, Seiliez, Iban, Semenkovich, Clay F, Semenza, Gregg L, Sen, Utpal, Serra, Andreas L, Serrano Puebla, Ana, Sesaki, Hiromi, Setoguchi, Takao, Settembre, Carmine, Shacka, John J, Shajahan Haq, Ayesha N, Shapiro, Irving M, Sharma, Shweta, She, Hua, Shen, C. K. Jame, Shen, Chiung Chyi, Shen, Han Ming, Shen, Sanbing, Shen, Weili, Sheng, Rui, Sheng, Xianyong, Sheng, Zu Hang, Shepherd, Trevor G, Shi, Junyan, Shi, Qiang, Shi, Qinghua, Shi, Yuguang, Shibutani, Shusaku, Shibuya, Kenichi, Shidoji, Yoshihiro, Shieh, Jeng Jer, Shih, Chwen Ming, Shimada, Yohta, Shimizu, Shigeomi, Shin, Dong Wook, Shinohara, Mari L, Shintani, Michiko, Shintani, Takahiro, Shioi, Tetsuo, Shirabe, Ken, Shiri Sverdlov, Ronit, Shirihai, Orian, Shore, Gordon C, Shu, Chih Wen, Shukla, Deepak, Sibirny, Andriy A, Sica, Valentina, Sigurdson, Christina J, Sigurdsson, Einar M, Sijwali, Puran Singh, Sikorska, Beata, Silveira, Wilian A, Silvente Poirot, Sandrine, Silverman, Gary A, Simak, Jan, Simmet, Thoma, Simon, Anna Katharina, Simon, Hans Uwe, Simone, Cristiano, Simons, Matia, Simonsen, Anne, Singh, Rajat, Singh, Shivendra V, Singh, Shrawan K, Sinha, Debasish, Sinha, Sangita, Sinicrope, Frank A, Sirko, Agnieszka, Sirohi, Kapil, Sishi, Balindiwe Jn, Sittler, Annie, Siu, Parco M, Sivridis, Efthimio, Skwarska, Anna, Slack, Ruth, Slaninová, Iva, Slavov, Nikolai, Smaili, Soraya S, Smalley, Keiran Sm, Smith, Duncan R, Soenen, Stefaan J, Soleimanpour, Scott A, Solhaug, Anita, Somasundaram, Kumaravel, Son, Jin H, Sonawane, Avinash, Song, Chunjuan, Song, Fuyong, Song, Hyun Kyu, Song, Ju Xian, Song, Wei, Soo, Kai Y, Sood, Anil K, Soong, Tuck Wah, Soontornniyomkij, Virawudh, Sorice, Maurizio, Sotgia, Federica, Soto Pantoja, David R, Sotthibundhu, Areechun, Sousa, Maria João, Spaink, Herman P, Span, Paul N, Spang, Anne, Sparks, Janet D, Speck, Peter G, Spector, Stephen A, Spies, Claudia D, Springer, Wolfdieter, Clair, Daret St, Stacchiotti, Alessandra, Staels, Bart, Stang, Michael T, Starczynowski, Daniel T, Starokadomskyy, Petro, Steegborn, Clemen, Steele, John W, Stefanis, Leonida, Steffan, Joan, Stellrecht, Christine M, Stenmark, Harald, Stepkowski, Tomasz M, Stern, Stęphan T, Stevens, Craig, Stockwell, Brent R, Stoka, Veronika, Storchova, Zuzana, Stork, Björn, Stratoulias, Vassili, Stravopodis, Dimitrios J, Strnad, Pavel, Strohecker, Anne Marie, Ström, Anna Lena, Stromhaug, Per, Stulik, Jiri, Su, Yu Xiong, Su, Zhaoliang, Subauste, Carlos S, Subramaniam, Srinivasa, Sue, Carolyn M, Suh, Sang Won, Sui, Xinbing, Sukseree, Supawadee, Sulzer, David, Sun, Fang Lin, Sun, Jiaren, Sun, Jun, Sun, Shi Yong, Sun, Yang, Sun, Yi, Sun, Yingjie, Sundaramoorthy, Vinod, Sung, Joseph, Suzuki, Hidekazu, Suzuki, Kuninori, Suzuki, Naoki, Suzuki, Tadashi, Suzuki, Yuichiro J, Swanson, Michele S, Swanton, Charle, Swärd, Karl, Swarup, Ghanshyam, Sweeney, Sean T, Sylvester, Paul W, Szatmari, Zsuzsanna, Szegezdi, Eva, Szlosarek, Peter W, Taegtmeyer, Heinrich, Tafani, Marco, Taillebourg, Emmanuel, Tait, Stephen Wg, Takacs Vellai, Krisztina, Takahashi, Yoshinori, Takáts, Szabolc, Takemura, Genzou, Takigawa, Nagio, Talbot, Nicholas J, Tamagno, Elena, Tamburini, Jerome, Tan, Cai Ping, Tan, Lan, Tan, Mei Lan, Tan, Ming, Tan, Yee Joo, Tanaka, Keiji, Tanaka, Masaki, Tang, Daolin, Tang, Dingzhong, Tang, Guomei, Tanida, Isei, Tanji, Kunikazu, Tannous, Bakhos A, Tapia, Jose A, Tasset Cuevas, Inmaculada, Tatar, Marc, Tavassoly, Iman, Tavernarakis, Nektario, Taylor, Allen, Taylor, Graham S, Taylor, Gregory A, Taylor, J. Paul, Taylor, Mark J, Tchetina, Elena V, Tee, Andrew R, Teixeira Clerc, Fatima, Telang, Sucheta, Tencomnao, Tewin, Teng, Ba Bie, Teng, Ru Jeng, Terro, Faraj, Tettamanti, Gianluca, Theiss, Arianne L, Theron, Anne E, Thomas, Kelly Jean, Thomé, Marcos P, Thomes, Paul G, Thorburn, Andrew, Thorner, Jeremy, Thum, Thoma, Thumm, Michael, Thurston, Teresa Lm, Tian, Ling, Till, Andrea, Ting, Jenny Pan Yun, Titorenko, Vladimir I, Toker, Lilach, Toldo, Stefano, Tooze, Sharon A, Topisirovic, Ivan, Torgersen, Maria Lyngaa, Torosantucci, Liliana, Torriglia, Alicia, Torrisi, Maria Rosaria, Tournier, Cathy, Towns, Roberto, Trajkovic, Vladimir, Travassos, Leonardo H, Triola, Gemma, Tripathi, Durga Nand, Trisciuoglio, Daniela, Troncoso, Rodrigo, Trougakos, Ioannis P, Truttmann, Anita C, Tsai, Kuen Jer, Tschan, Mario P, Tseng, Yi Hsin, Tsukuba, Takayuki, Tsung, Allan, Tsvetkov, Andrey S, Tu, Shuiping, Tuan, Hsing Yu, Tucci, Marco, Tumbarello, David A, Turk, Bori, Turk, Vito, Turner, Robin Fb, Tveita, Anders A, Tyagi, Suresh C, Ubukata, Makoto, Uchiyama, Yasuo, Udelnow, Andrej, Ueno, Takashi, Umekawa, Midori, Umemiya Shirafuji, Rika, Underwood, Benjamin R, Ungermann, Christian, Ureshino, Rodrigo P, Ushioda, Ryo, Uversky, Vladimir N, Uzcátegui, Néstor L, Vaccari, Thoma, Vaccaro, Maria I, Váchová, Libuše, Vakifahmetoglu Norberg, Helin, Valdor, Rut, Valente, Enza Maria, Vallette, Francoi, Valverde, Angela M, Van den Berghe, Greet, Van Den Bosch, Ludo, van den Brink, Gijs R, van der Goot, F. Gisou, van der Klei, Ida J, van der Laan, Luc Jw, van Doorn, Wouter G, van Egmond, Marjolein, van Golen, Kenneth L, Van Kaer, Luc, van Lookeren Campagne, Menno, Vandenabeele, Peter, Vandenberghe, Wim, Vanhorebeek, Ilse, Varela Nieto, Isabel, Vasconcelos, M. Helena, Vasko, Radovan, Vavvas, Demetrios G, Vega Naredo, Ignacio, Velasco, Guillermo, Velentzas, Athanassios D, Velentzas, Panagiotis D, Vellai, Tibor, Vellenga, Edo, Vendelbo, Mikkel Holm, Venkatachalam, Kartik, Ventura, Natascia, Ventura, Salvador, Veras, Patrícia St, Verdier, Mireille, Vertessy, Beata G, Viale, Andrea, Vidal, Michel, Vieira, Helena L. A, Vierstra, Richard D, Vigneswaran, Nadarajah, Vij, Neeraj, Vila, Miquel, Villar, Margarita, Villar, Victor H, Villarroya, Joan, Vindis, Cécile, Viola, Giampietro, Viscomi, Maria Teresa, Vitale, Giovanni, Vogl, Dan T, Voitsekhovskaja, Olga V, von Haefen, Clarissa, von Schwarzenberg, Karin, Voth, Daniel E, Vouret Craviari, Valérie, Vuori, Kristina, Vyas, Jatin M, Waeber, Christian, Walker, Cheryl Lyn, Walker, Mark J, Walter, Jochen, Wan, Lei, Wan, Xiangbo, Wang, Bo, Wang, Caihong, Wang, Chao Yung, Wang, Chengshu, Wang, Chenran, Wang, Chuangui, Wang, Dong, Wang, Fen, Wang, Fuxin, Wang, Guanghui, Wang, Hai Jie, Wang, Haichao, Wang, Hong Gang, Wang, Hongmin, Wang, Horng Dar, Wang, Jing, Wang, Junjun, Wang, Mei, Wang, Mei Qing, Wang, Pei Yu, Wang, Peng, Wang, Richard C, Wang, Shuo, Wang, Ting Fang, Wang, Xian, Wang, Xiao Jia, Wang, Xiao Wei, Wang, Xin, Wang, Xuejun, Wang, Yan, Wang, Yanming, Wang, Ying, Wang, Ying Jan, Wang, Yipeng, Wang, Yu, Wang, Yu Tian, Wang, Yuqing, Wang, Zhi Nong, Wappner, Pablo, Ward, Carl, Ward, Diane McVey, Warnes, Gary, Watada, Hirotaka, Watanabe, Yoshihisa, Watase, Kei, Weaver, Timothy E, Weekes, Colin D, Wei, Jiwu, Weide, Thoma, Weihl, Conrad C, Weindl, Günther, Weis, Simone Nardin, Wen, Longping, Wen, Xin, Wen, Yunfei, Westermann, Benedikt, Weyand, Cornelia M, White, Anthony R, White, Eileen, Whitton, J. Lindsay, Whitworth, Alexander J, Wiels, Joëlle, Wild, Franziska, Wildenberg, Manon E, Wileman, Tom, Wilkinson, Deepti Sriniva, Wilkinson, Simon, Willbold, Dieter, Williams, Chri, Williams, Katherine, Williamson, Peter R, Winklhofer, Konstanze F, Witkin, Steven S, Wohlgemuth, Stephanie E, Wollert, Thoma, Wolvetang, Ernst J, Wong, Esther, Wong, G. William, Wong, Richard W, Wong, Vincent Kam Wai, Woodcock, Elizabeth A, Wright, Karen L, Wu, Chunlai, Wu, Defeng, Wu, Gen Sheng, Wu, Jian, Wu, Junfang, Wu, Mian, Wu, Min, Wu, Shengzhou, Wu, William Kk, Wu, Yaohua, Wu, Zhenlong, Xavier, Cristina Pr, Xavier, Ramnik J, Xia, Gui Xian, Xia, Tian, Xia, Weiliang, Xia, Yong, Xiao, Hengyi, Xiao, Jian, Xiao, Shi, Xiao, Wuhan, Xie, Chuan Ming, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xiong, Yuyan, Xu, Chuanshan, Xu, Congfeng, Xu, Feng, Xu, Haoxing, Xu, Hongwei, Xu, Jian, Xu, Jianzhen, Xu, Jinxian, Xu, Liang, Xu, Xiaolei, Xu, Yangqing, Xu, Ye, Xu, Zhi Xiang, Xu, Ziheng, Xue, Yu, Yamada, Takahiro, Yamamoto, Ai, Yamanaka, Koji, Yamashina, Shunhei, Yamashiro, Shigeko, Yan, Bing, Yan, Bo, Yan, Xianghua, Yan, Zhen, Yanagi, Yasuo, Yang, Dun Sheng, Yang, Jin Ming, Yang, Liu, Yang, Minghua, Yang, Pei Ming, Yang, Peixin, Yang, Qian, Yang, Wannian, Yang, Wei Yuan, Yang, Xuesong, Yang, Yi, Yang, Ying, Yang, Zhifen, Yang, Zhihong, Yao, Meng Chao, Yao, Pamela J, Yao, Xiaofeng, Yao, Zhenyu, Yao, Zhiyuan, Yasui, Linda S, Ye, Mingxiang, Yedvobnick, Barry, Yeganeh, Behzad, Yeh, Elizabeth S, Yeyati, Patricia L, Yi, Fan, Yi, Long, Yin, Xiao Ming, Yip, Calvin K, Yoo, Yeong Min, Yoo, Young Hyun, Yoon, Seung Yong, Yoshida, Ken Ichi, Yoshimori, Tamotsu, Young, Ken H, Yu, Huixin, Yu, Jane J, Yu, Jin Tai, Yu, Jun, Yu, Li, Yu, W. Haung, Yu, Xiao Fang, Yu, Zhengping, Yuan, Junying, Yuan, Zhi Min, Yue, Beatrice Yjt, Yue, Jianbo, Yue, Zhenyu, Zacks, David N, Zacksenhaus, Eldad, Zaffaroni, Nadia, Zaglia, Tania, Zakeri, Zahra, Zecchini, Vincent, Zeng, Jinsheng, Zeng, Min, Zeng, Qi, Zervos, Antonis S, Zhang, Donna D, Zhang, Fan, Zhang, Guo, Zhang, Guo Chang, Zhang, Hao, Zhang, Hong, Zhang, Hongbing, Zhang, Jian, Zhang, Jiangwei, Zhang, Jianhua, Zhang, Jing Pu, Zhang, Li, Zhang, Lin, Zhang, Long, Zhang, Ming Yong, Zhang, Xiangnan, Zhang, Xu Dong, Zhang, Yan, Zhang, Yang, Zhang, Yanjin, Zhang, Yingmei, Zhang, Yunjiao, Zhao, Mei, Zhao, Wei Li, Zhao, Xiaonan, Zhao, Yan G, Zhao, Ying, Zhao, Yongchao, Zhao, Yu Xia, Zhao, Zhendong, Zhao, Zhizhuang J, Zheng, Dexian, Zheng, Xi Long, Zheng, Xiaoxiang, Zhivotovsky, Bori, Zhong, Qing, Zhou, Guang Zhou, Zhou, Guofei, Zhou, Huiping, Zhou, Shu Feng, Zhou, Xu Jie, Zhu, Hongxin, Zhu, Hua, Zhu, Wei Guo, Zhu, Wenhua, Zhu, Xiao Feng, Zhu, Yuhua, Zhuang, Shi Mei, Zhuang, Xiaohong, Ziparo, Elio, Zois, Christos E, Zoladek, Teresa, Zong, Wei Xing, Zorzano, Antonio, Zughaier, Susu M., MEDINA SANABRIA, Diego Luis, RS: GROW - R2 - Basic and Translational Cancer Biology, RS: NUTRIM - R2 - Gut-liver homeostasis, Molecular Genetics, Beeldvorming, Genetica & Celbiologie, Medical oncology laboratory, CCA - Target Discovery & Preclinial Therapy Development, Pathology, Amsterdam Neuroscience - Cellular & Molecular Mechanisms, CCA - Clinical Therapy Development, Human genetics, Surgery, Molecular cell biology and Immunology, Klionsky, Dj, Abdelmohsen, K, Abe, A, Abedin, Mj, Abeliovich, H, Acevedo Arozena, A, Adachi, H, Adams, Cm, Adams, Pd, Adeli, K, Adhihetty, Pj, Adler, Sg, Agam, G, Agarwal, R, Aghi, Mk, Agnello, M, Agostinis, P, Aguilar, Pv, Aguirre Ghiso, J, Airoldi, Em, Ait Si Ali, S, Akematsu, T, Akporiaye, Et, Al Rubeai, M, Albaiceta, Gm, Albanese, C, Albani, D, Albert, Ml, Aldudo, J, Algül, H, Alirezaei, M, Alloza, I, Almasan, A, Almonte Beceril, M, Alnemri, E, Alonso, C, Altan Bonnet, N, Altieri, Dc, Alvarez, S, Alvarez Erviti, L, Alves, S, Amadoro, G, Amano, A, Amantini, C, Ambrosio, S, Amelio, I, Amer, Ao, Amessou, M, Amon, A, An, Z, Anania, Fa, Andersen, Su, Andley, Up, Andreadi, Ck, Andrieu Abadie, N, Anel, A, Ann, Dk, Anoopkumar Dukie, S, Antonioli, M, Aoki, H, Apostolova, N, Aquila, S, Aquilano, K, Araki, K, Arama, E, Aranda, A, Araya, J, Arcaro, A, Arias, E, Arimoto, H, Ariosa, Ar, Armstrong, Jl, Arnould, T, Arsov, I, Asanuma, K, Askanas, V, Asselin, E, Atarashi, R, Atherton, S, Atkin, Jd, Attardi, Ld, Auberger, P, Auburger, G, Aurelian, L, Autelli, R, Avagliano, L, Avantaggiati, Ml, Avrahami, L, Awale, S, Azad, N, Bachetti, T, Backer, Jm, Bae, Dh, Bae, J, Bae, On, Bae, Sh, Baehrecke, Eh, Baek, Sh, Baghdiguian, S, Bagniewska Zadworna, A, Bai, H, Bai, J, Bai, Xy, Bailly, Y, Balaji, Kn, Balduini, W, Ballabio, A, Balzan, R, Banerjee, R, Bánhegyi, G, Bao, H, Barbeau, B, Barrachina, Md, Barreiro, E, Bartel, B, Bartolomé, A, Bassham, Dc, Bassi, Mt, Bast RC, Jr, Basu, A, Batista, Mt, Batoko, H, Battino, M, Bauckman, K, Baumgarner, Bl, Bayer, Ku, Beale, R, Beaulieu, Jf, Beck GR, Jr, Becker, C, Beckham, Jd, Bédard, Pa, Bednarski, Pj, Begley, Tj, Behl, C, Behrends, C, Behrens, Gm, Behrns, Ke, Bejarano, E, Belaid, A, Belleudi, F, Bénard, G, Berchem, G, Bergamaschi, D, Bergami, M, Berkhout, B, Berliocchi, L, Bernard, A, Bernard, M, Bernassola, F, Bertolotti, A, Bess, A, Besteiro, S, Bettuzzi, S, Bhalla, S, Bhattacharyya, S, Bhutia, Sk, Biagosch, C, Bianchi, Mw, Biard Piechaczyk, M, Billes, V, Bincoletto, C, Bingol, B, Bird, Sw, Bitoun, M, Bjedov, I, Blackstone, C, Blanc, L, Blanco, Ga, Blomhoff, Hk, Boada Romero, E, Böckler, S, Boes, M, Boesze Battaglia, K, Boise, Lh, Bolino, A, Boman, A, Bonaldo, P, Bordi, M, Bosch, J, Botana, Lm, Botti, J, Bou, G, Bouché, M, Bouchecareilh, M, Boucher, Mj, Boulton, Me, Bouret, Sg, Boya, P, Boyer Guittaut, M, Bozhkov, Pv, Brady, N, Braga, Vm, Brancolini, C, Braus, Gh, Bravo San Pedro, Jm, Brennan, La, Bresnick, Eh, Brest, P, Bridges, D, Bringer, Ma, Brini, M, Brito, Gc, Brodin, B, Brookes, P, Brown, Ej, Brown, K, Broxmeyer, He, Bruhat, A, Brum, Pc, Brumell, Jh, Brunetti Pierri, N, Bryson Richardson, Rj, Buch, S, Buchan, Am, Budak, H, Bulavin, Dv, Bultman, Sj, Bultynck, G, Bumbasirevic, V, Burelle, Y, Burke, Re, Burmeister, M, Bütikofer, P, Caberlotto, L, Cadwell, K, Cahova, M, Cai, D, Cai, J, Cai, Q, Calatayud, S, Camougrand, N, Campanella, M, Campbell, Gr, Campbell, M, Campello, S, Candau, R, Caniggia, I, Cantoni, L, Cao, L, Caplan, Ab, Caraglia, M, Cardinali, C, Cardoso, Sm, Carew, J, Carleton, La, Carlin, Cr, Carloni, S, Carlsson, Sr, Carmona Gutierrez, D, Carneiro, La, Carnevali, O, Carra, S, Carrier, A, Carroll, B, Casas, C, Casas, J, Cassinelli, G, Castets, P, Castro Obregon, S, Cavallini, G, Ceccherini, I, Cecconi, F, Cederbaum, Ai, Ceña, V, Cenci, S, Cerella, C, Cervia, D, Cetrullo, S, Chaachouay, H, Chae, Hj, Chagin, A, Chai, Cy, Chakrabarti, G, Chamilos, G, Chan, Ey, Chan, Mt, Chandra, D, Chandra, P, Chang, Cp, Chang, Rc, Chang, Ty, Chatham, Jc, Chatterjee, S, Chauhan, S, Che, Y, Cheetham, Me, Cheluvappa, R, Chen, Cj, Chen, G, Chen, Gc, Chen, H, Chen, Jw, Chen, Jk, Chen, M, Chen, P, Chen, Q, Chen, Sd, Chen, S, Chen, W, Chen, Wj, Chen, Wq, Chen, X, Chen, Yh, Chen, Yg, Chen, Y, Chen, Yj, Chen, Yq, Chen, Z, Cheng, A, Cheng, Ch, Cheng, H, Cheong, H, Cherry, S, Chesney, J, Cheung, Ch, Chevet, E, Chi, Hc, Chi, Sg, Chiacchiera, F, Chiang, Hl, Chiarelli, R, Chiariello, M, Chieppa, M, Chin, L, Chiong, M, Chiu, Gn, Cho, Dh, Cho, Sg, Cho, Wc, Cho, Yy, Cho, Y, Choi, Am, Choi, Ej, Choi, Ek, Choi, J, Choi, Me, Choi, Si, Chou, Tf, Chouaib, S, Choubey, D, Choubey, V, Chow, Kc, Chowdhury, K, Chu, Ct, Chuang, Th, Chun, T, Chung, H, Chung, T, Chung, Yl, Chwae, Yj, Cianfanelli, V, Ciarcia, R, Ciechomska, Ia, Ciriolo, Mr, Cirone, M, Claerhout, S, Clague, Mj, Clària, J, Clarke, Pg, Clarke, R, Clementi, E, Cleyrat, C, Cnop, M, Coccia, Em, Cocco, T, Codogno, P, Coers, J, Cohen, Ee, Colecchia, D, Coletto, L, Coll, N, Colucci Guyon, E, Comincini, S, Condello, M, Cook, Kl, Coombs, Gh, Cooper, Cd, Cooper, Jm, Coppens, I, Corasaniti, Mt, Corazzari, M, Corbalan, R, Corcelle Termeau, E, Cordero, Md, Corral Ramos, C, Corti, O, Cossarizza, A, Costelli, P, Costes, S, Cotman, Sl, Coto Montes, A, Cottet, S, Couve, E, Covey, Lr, Cowart, La, Cox, J, Coxon, Fp, Coyne, Cb, Cragg, M, Craven, Rj, Crepaldi, T, Crespo, Jl, Criollo, A, Crippa, V, Cruz, Mt, Cuervo, Am, Cuezva, Jm, Cui, T, Cutillas, Pr, Czaja, Mj, Czyzyk Krzeska, Mf, Dagda, Rk, Dahmen, U, Dai, C, Dai, W, Dai, Y, Dalby, Kn, Dalla Valle, L, Dalmasso, G, D'Amelio, M, Damme, M, Darfeuille Michaud, A, Dargemont, C, Darley Usmar, Vm, Dasarathy, S, Dasgupta, B, Dash, S, Dass, Cr, Davey, Hm, Davids, Lm, Dávila, D, Davis, Rj, Dawson, Tm, Dawson, Vl, Daza, P, de Belleroche, J, de Figueiredo, P, de Figueiredo, Rc, de la Fuente, J, De Martino, L, De Matteis, A, De Meyer, Gr, De Milito, A, De Santi, M, de Souza, W, De Tata, V, De Zio, D, Debnath, J, Dechant, R, Decuypere, Jp, Deegan, S, Dehay, B, Del Bello, B, Del Re, Dp, Delage Mourroux, R, Delbridge, Lm, Deldicque, L, Delorme Axford, E, Deng, Y, Dengjel, J, Denizot, M, Dent, P, Der, Cj, Deretic, V, Derrien, B, Deutsch, E, Devarenne, Tp, Devenish, Rj, Di Bartolomeo, S, Di Daniele, N, Di Domenico, F, Di Nardo, A, Di Paola, S, Di Pietro, A, Di Renzo, L, Diantonio, A, Díaz Araya, G, Díaz Laviada, I, Diaz Meco, Mt, Diaz Nido, J, Dickey, Ca, Dickson, Rc, Diederich, M, Digard, P, Dikic, I, Dinesh Kumar, Sp, Ding, C, Ding, Wx, Ding, Z, Distler, Jh, Diwan, A, Djavaheri Mergny, M, Dmytruk, K, Dobson, Rc, Doetsch, V, Dokladny, K, Dokudovskaya, S, Donadelli, M, Dong, Xc, Dong, X, Dong, Z, Donohue TM, Jr, Doran, K, D'Orazi, G, Dorn GW, 2nd, Dosenko, V, Dridi, S, Drucker, L, Du, J, Du, Ll, Du, L, du Toit, A, Dua, P, Duan, L, Duann, P, Dubey, Vk, Duchen, Mr, Duchosal, Ma, Duez, H, Dugail, I, Dumit, Vi, Duncan, Mc, Dunlop, Ea, Dunn WA, Jr, Dupont, N, Dupuis, L, Durán, Rv, Durcan, Tm, Duvezin Caubet, S, Duvvuri, U, Eapen, V, Ebrahimi Fakhari, D, Echard, A, Eckhart, L, Edelstein, Cl, Edinger, Al, Eichinger, L, Eisenberg, T, Eisenberg Lerner, A, Eissa, Nt, El Deiry, W, El Khoury, V, Elazar, Z, Eldar Finkelman, H, Elliott, Cj, Emanuele, E, Emmenegger, U, Engedal, N, Engelbrecht, Am, Engelender, S, Enserink, Jm, Erdmann, R, Erenpreisa, J, Eri, R, Eriksen, Jl, Erman, A, Escalante, R, Eskelinen, El, Espert, L, Esteban Martínez, L, Evans, Tj, Fabri, M, Fabrias, G, Fabrizi, C, Facchiano, A, Færgeman, Nj, Faggioni, A, Fairlie, Wd, Fan, C, Fan, D, Fan, J, Fang, S, Fanto, M, Fanzani, A, Farkas, T, Faure, M, Favier, Fb, Fearnhead, H, Federici, M, Fei, E, Felizardo, Tc, Feng, H, Feng, Y, Ferguson, Ta, Fernández, Áf, Fernandez Barrena, Mg, Fernandez Checa, Jc, Fernández López, A, Fernandez Zapico, Me, Feron, O, Ferraro, E, Ferreira Halder, Cv, Fesus, L, Feuer, R, Fiesel, Fc, Filippi Chiela, Ec, Filomeni, G, Fingert, Jh, Finkbeiner, S, Finkel, T, Fiorito, F, Fisher, Pb, Flajolet, M, Flamigni, F, Florey, O, Florio, S, Floto, Ra, Folini, M, Follo, C, Fon, Ea, Fornai, F, Fortunato, F, Fraldi, A, Franco, R, Francois, A, François, A, Frankel, Lb, Fraser, Id, Frey, N, Freyssenet, Dg, Frezza, C, Friedman, Sl, Frigo, De, Fu, D, Fuentes, Jm, Fueyo, J, Fujitani, Y, Fujiwara, Y, Fujiya, M, Fukuda, M, Fulda, S, Fusco, C, Gabryel, B, Gaestel, M, Gailly, P, Gajewska, M, Galadari, S, Galili, G, Galindo, I, Galindo, Mf, Galliciotti, G, Galluzzi, L, Galy, V, Gammoh, N, Gandy, S, Ganesan, Ak, Ganesan, S, Ganley, Ig, Gannagé, M, Gao, Fb, Gao, F, Gao, Jx, García Nannig, L, García Véscovi, E, Garcia Macía, M, Garcia Ruiz, C, Garg, Ad, Garg, Pk, Gargini, R, Gassen, Nc, Gatica, D, Gatti, E, Gavard, J, Gavathiotis, E, Ge, L, Ge, P, Ge, S, Gean, Pw, Gelmetti, V, Genazzani, Aa, Geng, J, Genschik, P, Gerner, L, Gestwicki, Je, Gewirtz, Da, Ghavami, S, Ghigo, E, Ghosh, D, Giammarioli, Am, Giampieri, F, Giampietri, C, Giatromanolaki, A, Gibbings, Dj, Gibellini, L, Gibson, Sb, Ginet, V, Giordano, A, Giorgini, F, Giovannetti, E, Girardin, Se, Gispert, S, Giuliano, S, Gladson, Cl, Glavic, A, Gleave, M, Godefroy, N, Gogal RM, Jr, Gokulan, K, Goldman, Gh, Goletti, D, Goligorsky, M, Gomes, Av, Gomes, Lc, Gomez, H, Gomez Manzano, C, Gómez Sánchez, R, Gonçalves, Da, Goncu, E, Gong, Q, Gongora, C, Gonzalez, Cb, Gonzalez Alegre, P, Gonzalez Cabo, P, González Polo, Ra, Goping, I, Gorbea, C, Gorbunov, Nv, Goring, Dr, Gorman, Am, Gorski, Sm, Goruppi, S, Goto Yamada, S, Gotor, C, Gottlieb, Ra, Gozes, I, Gozuacik, D, Graba, Y, Graef, M, Granato, Ge, Grant, Gd, Grant, S, Gravina, Gl, Green, Dr, Greenhough, A, Greenwood, Mt, Grimaldi, B, Gros, F, Grose, C, Groulx, Jf, Gruber, F, Grumati, P, Grune, T, Guan, Jl, Guan, Kl, Guerra, B, Guillen, C, Gulshan, K, Gunst, J, Guo, C, Guo, L, Guo, M, Guo, W, Guo, Xg, Gust, Aa, Gustafsson, Åb, Gutierrez, E, Gutierrez, Mg, Gwak, H, Haas, A, Haber, Je, Hadano, S, Hagedorn, M, Hahn, Dr, Halayko, Aj, Hamacher Brady, A, Hamada, K, Hamai, A, Hamann, A, Hamasaki, M, Hamer, I, Hamid, Q, Hammond, Em, Han, F, Han, W, Handa, Jt, Hanover, Ja, Hansen, M, Harada, M, Harhaji Trajkovic, L, Harper, Jw, Harrath, Ah, Harris, Al, Harris, J, Hasler, U, Hasselblatt, P, Hasui, K, Hawley, Rg, Hawley, T, He, C, He, Cy, He, F, He, G, He, Rr, He, Xh, He, Yw, He, Yy, Heath, Jk, Hébert, Mj, Heinzen, Ra, Helgason, Gv, Hensel, M, Henske, Ep, Her, C, Herman, Pk, Hernández, A, Hernandez, C, Hernández Tiedra, S, Hetz, C, Hiesinger, Pr, Higaki, K, Hilfiker, S, Hill, Bg, Hill, Ja, Hill, Wd, Hino, K, Hofius, D, Hofman, P, Höglinger, Gu, Höhfeld, J, Holz, Mk, Hong, Y, Hood, Da, Hoozemans, Jj, Hoppe, T, Hsu, C, Hsu, Cy, Hsu, Lc, Hu, D, Hu, G, Hu, Hm, Hu, H, Hu, Mc, Hu, Yc, Hu, Zw, Hua, F, Hua, Y, Huang, C, Huang, Hl, Huang, Kh, Huang, Ky, Huang, S, Huang, Wp, Huang, Yr, Huang, Y, Huber, Tb, Huebbe, P, Huh, Wk, Hulmi, Jj, Hur, Gm, Hurley, Jh, Husak, Z, Hussain, Sn, Hussain, S, Hwang, Jj, Hwang, S, Hwang, Ti, Ichihara, A, Imai, Y, Imbriano, C, Inomata, M, Into, T, Iovane, V, Iovanna, Jl, Iozzo, Rv, Ip, Ny, Irazoqui, Je, Iribarren, P, Isaka, Y, Isakovic, Aj, Ischiropoulos, H, Isenberg, J, Ishaq, M, Ishida, H, Ishii, I, Ishmael, Je, Isidoro, C, Isobe, Ki, Isono, E, Issazadeh Navikas, S, Itahana, K, Itakura, E, Ivanov, Ai, Iyer, Ak, Izquierdo, Jm, Izumi, Y, Izzo, V, Jäättelä, M, Jaber, N, Jackson, Dj, Jackson, Wt, Jacob, Tg, Jacques, T, Jagannath, C, Jain, A, Jana, Nr, Jang, Bk, Jani, A, Janji, B, Jannig, Pr, Jansson, Pj, Jean, S, Jendrach, M, Jeon, Jh, Jessen, N, Jeung, Eb, Jia, K, Jia, L, Jiang, H, Jiang, L, Jiang, T, Jiang, X, Jiang, Y, Jiménez, A, Jin, C, Jin, H, Jin, L, Jin, M, Jin, S, Jinwal, Uk, Jo, Ek, Johansen, T, Johnson, De, Johnson, Gv, Johnson, Jd, Jonasch, E, Jones, C, Joosten, La, Jordan, J, Joseph, Am, Joseph, B, Joubert, Am, Ju, D, Ju, J, Juan, Hf, Juenemann, K, Juhász, G, Jung, H, Jung, Ju, Jung, Yk, Jungbluth, H, Justice, Mj, Jutten, B, Kaakoush, No, Kaarniranta, K, Kaasik, A, Kabuta, T, Kaeffer, B, Kågedal, K, Kahana, A, Kajimura, S, Kakhlon, O, Kalia, M, Kalvakolanu, Dv, Kamada, Y, Kambas, K, Kaminskyy, Vo, Kampinga, Hh, Kandouz, M, Kang, C, Kang, R, Kang, Tc, Kanki, T, Kanneganti, Td, Kanno, H, Kanthasamy, Ag, Kantorow, M, Kaparakis Liaskos, M, Kapuy, O, Karantza, V, Karim, Mr, Karmakar, P, Kaser, A, Kaushik, S, Kawula, T, Kaynar, Am, Ke, Py, Ke, Zj, Kehrl, Jh, Keller, Ke, Kemper, Jk, Kenworthy, Ak, Kepp, O, Kern, A, Kesari, S, Kessel, D, Ketteler, R, Kettelhut, Id, Khambu, B, Khan, Mm, Khandelwal, Vk, Khare, S, Kiang, Jg, Kiger, Aa, Kihara, A, Kim, Al, Kim, Ch, Kim, Dr, Kim, Dh, Kim, Ek, Kim, Hy, Kim, Hr, Kim, J, Kim, Jh, Kim, Jc, Kim, Kw, Kim, Md, Kim, Mm, Kim, Pk, Kim, Sw, Kim, Sy, Kim, Y, Kimchi, A, Kimmelman, Ac, Kimura, T, King, J, Kirkegaard, K, Kirkin, V, Kirshenbaum, La, Kishi, S, Kitajima, Y, Kitamoto, K, Kitaoka, Y, Kitazato, K, Kley, Ra, Klimecki, Wt, Klinkenberg, M, Klucken, J, Knævelsrud, H, Knecht, E, Knuppertz, L, Ko, Jl, Kobayashi, S, Koch, Jc, Koechlin Ramonatxo, C, Koenig, U, Koh, Yh, Köhler, K, Kohlwein, Sd, Koike, M, Komatsu, M, Kominami, E, Kong, D, Kong, Hj, Konstantakou, Eg, Kopp, Bt, Korcsmaros, T, Korhonen, L, Korolchuk, Vi, Koshkina, Nv, Kou, Y, Koukourakis, Mi, Koumenis, C, Kovács, Al, Kovács, T, Kovacs, Wj, Koya, D, Kraft, C, Krainc, D, Kramer, H, Kravic Stevovic, T, Krek, W, Kretz Remy, C, Krick, R, Krishnamurthy, M, Kriston Vizi, J, Kroemer, G, Kruer, Mc, Kruger, R, Ktistakis, Nt, Kuchitsu, K, Kuhn, C, Kumar, Ap, Kumar, A, Kumar, D, Kumar, R, Kumar, S, Kundu, M, Kung, Hj, Kuno, A, Kuo, Sh, Kuret, J, Kurz, T, Kwok, T, Kwon, Tk, Kwon, Yt, Kyrmizi, I, La Spada, Ar, Lafont, F, Lahm, T, Lakkaraju, A, Lam, T, Lamark, T, Lancel, S, Landowski, Th, Lane, Dj, Lane, Jd, Lanzi, C, Lapaquette, P, Lapierre, Lr, Laporte, J, Laukkarinen, J, Laurie, Gw, Lavandero, S, Lavie, L, Lavoie, Mj, Law, By, Law, Hk, Law, Kb, Layfield, R, Lazo, Pa, Le Cam, L, Le Roch, Kg, Le Stunff, H, Leardkamolkarn, V, Lecuit, M, Lee, Bh, Lee, Ch, Lee, Ef, Lee, Gm, Lee, Hj, Lee, H, Lee, Jk, Lee, J, Lee, Jh, Lee, M, Lee, Pj, Lee, Sw, Lee, Sj, Lee, Sy, Lee, Sh, Lee, S, Lee, Yr, Lee, Yj, Lee, Yh, Leeuwenburgh, C, Lefort, S, Legouis, R, Lei, J, Lei, Qy, Leib, Da, Leibowitz, G, Lekli, I, Lemaire, Sd, Lemasters, Jj, Lemberg, Mk, Lemoine, A, Leng, S, Lenz, G, Lenzi, P, Lerman, Lo, Lettieri Barbato, D, Leu, Ji, Leung, Hy, Levine, B, Lewis, Pa, Lezoualc'H, F, Li, C, Li, F, Li, Fj, Li, J, Li, K, Li, L, Li, M, Li, Q, Li, R, Li, S, Li, W, Li, X, Li, Y, Lian, J, Liang, C, Liang, Q, Liao, Y, Liberal, J, Liberski, Pp, Lie, P, Lieberman, Ap, Lim, Hj, Lim, Kl, Lim, K, Lima, Rt, Lin, C, Lin, Cf, Lin, F, Lin, Fc, Lin, K, Lin, Kh, Lin, Ph, Lin, T, Lin, Ww, Lin, Y, Linden, R, Lindholm, D, Lindqvist, Lm, Lingor, P, Linkermann, A, Liotta, La, Lipinski, Mm, Lira, Va, Lisanti, Mp, Liton, Pb, Liu, B, Liu, C, Liu, Cf, Liu, F, Liu, Hj, Liu, J, Liu, Jj, Liu, Jl, Liu, K, Liu, L, Liu, Q, Liu, Ry, Liu, S, Liu, W, Liu, Xd, Liu, X, Liu, Xh, Liu, Y, Liu, Z, Liuzzi, Jp, Lizard, G, Ljujic, M, Lodhi, Ij, Logue, Se, Lokeshwar, Bl, Long, Yc, Lonial, S, Loos, B, López Otín, C, López Vicario, C, Lorente, M, Lorenzi, Pl, Lõrincz, P, Los, M, Lotze, Mt, Lovat, Pe, Lu, B, Lu, J, Lu, Q, Lu, Sm, Lu, S, Lu, Y, Luciano, F, Luckhart, S, Lucocq, Jm, Ludovico, P, Lugea, A, Lukacs, Nw, Lum, Jj, Lund, Ah, Luo, H, Luo, J, Luo, S, Luparello, C, Lyons, T, Ma, J, Ma, Y, Ma, Z, Machado, J, Machado Santelli, Gm, Macian, F, Macintosh, Gc, Mackeigan, Jp, Macleod, Kf, Macmicking, Jd, MacMillan Crow, La, Madeo, F, Madesh, M, Madrigal Matute, J, Maeda, A, Maeda, T, Maegawa, G, Maellaro, E, Maes, H, Magariños, M, Maiese, K, Maiti, Tk, Maiuri, L, Maiuri, Mc, Maki, Cg, Malli, R, Malorni, W, Maloyan, A, Mami Chouaib, F, Man, N, Mancias, Jd, Mandelkow, Em, Mandell, Ma, Manfredi, Aa, Manié, Sn, Manzoni, C, Mao, K, Mao, Z, Mao, Zw, Marambaud, P, Marconi, Am, Marelja, Z, Marfe, G, Margeta, M, Margittai, E, Mari, M, Mariani, Fv, Marin, C, Marinelli, S, Mariño, G, Markovic, I, Marquez, R, Martelli, Am, Martens, S, Martin, Kr, Martin, Sj, Martin, S, Martin Acebes, Ma, Martín Sanz, P, Martinand Mari, C, Martinet, W, Martinez, J, Martinez Lopez, N, Martinez Outschoorn, U, Martínez Velázquez, M, Martinez Vicente, M, Martins, Wk, Mashima, H, Mastrianni, Ja, Matarese, G, Matarrese, P, Mateo, R, Matoba, S, Matsumoto, N, Matsushita, T, Matsuura, A, Matsuzawa, T, Mattson, Mp, Matus, S, Maugeri, N, Mauvezin, C, Mayer, A, Maysinger, D, Mazzolini, Gd, Mcbrayer, Mk, Mccall, K, Mccormick, C, Mcinerney, Gm, Mciver, Sc, Mckenna, S, Mcmahon, Jj, Mcneish, Ia, Mechta Grigoriou, F, Medema, Jp, Medina, Dl, Megyeri, K, Mehrpour, M, Mehta, Jl, Mei, Y, Meier, Uc, Meijer, Aj, Meléndez, A, Melino, G, Melino, S, de Melo, Ej, Mena, Ma, Meneghini, Md, Menendez, Ja, Menezes, R, Meng, L, Meng, Lh, Meng, S, Menghini, R, Menko, A, Menna Barreto, Rf, Menon, Mb, Meraz Ríos, Ma, Merla, G, Merlini, L, Merlot, Am, Meryk, A, Meschini, S, Meyer, Jn, Mi, Mt, Miao, Cy, Micale, L, Michaeli, S, Michiels, C, Migliaccio, Ar, Mihailidou, A, Mijaljica, D, Mikoshiba, K, Milan, E, Miller Fleming, L, Mills, Gb, Mills, Ig, Minakaki, G, Minassian, Ba, Ming, Xf, Minibayeva, F, Minina, Ea, Mintern, Jd, Minucci, S, Miranda Vizuete, A, Mitchell, Ch, Miyamoto, S, Miyazawa, K, Mizushima, N, Mnich, K, Mograbi, B, Mohseni, S, Moita, Lf, Molinari, M, Møller, Ab, Mollereau, B, Mollinedo, F, Mongillo, M, Monick, Mm, Montagnaro, S, Montell, C, Moore, Dj, Moore, Mn, Mora Rodriguez, R, Moreira, Pi, Morel, E, Morelli, Mb, Moreno, S, Morgan, Mj, Moris, A, Moriyasu, Y, Morrison, Jl, Morrison, La, Morselli, E, Moscat, J, Moseley, Pl, Mostowy, S, Motori, E, Mottet, D, Mottram, Jc, Moussa, Ce, Mpakou, Ve, Mukhtar, H, Mulcahy Levy, Jm, Muller, S, Muñoz Moreno, R, Muñoz Pinedo, C, Münz, C, Murphy, Me, Murray, Jt, Murthy, A, Mysorekar, Iu, Nabi, Ir, Nabissi, M, Nader, Ga, Nagahara, Y, Nagai, Y, Nagata, K, Nagelkerke, A, Nagy, P, Naidu, Sr, Nair, S, Nakano, H, Nakatogawa, H, Nanjundan, M, Napolitano, G, Naqvi, Ni, Nardacci, R, Narendra, Dp, Narita, M, Nascimbeni, Ac, Natarajan, R, Navegantes, Lc, Nawrocki, St, Nazarko, Ty, Nazarko, Vy, Neill, T, Neri, Lm, Netea, Mg, Netea Maier, Rt, Neves, Bm, Ney, Pa, Nezis, Ip, Nguyen, Ht, Nguyen, Hp, Nicot, A, Nilsen, H, Nilsson, P, Nishimura, M, Nishino, I, Niso Santano, M, Niu, H, Nixon, Ra, Njar, Vc, Noda, T, Noegel, Aa, Nolte, Em, Norberg, E, Norga, Kk, Noureini, Sk, Notomi, S, Notterpek, L, Nowikovsky, K, Nukina, N, Nürnberger, T, O'Donnell, Vb, O'Donovan, T, O'Dwyer, Pj, Oehme, I, Oeste, Cl, Ogawa, M, Ogretmen, B, Ogura, Y, Oh, Yj, Ohmuraya, M, Ohshima, T, Ojha, R, Okamoto, K, Okazaki, T, Oliver, Fj, Ollinger, K, Olsson, S, Orban, Dp, Ordonez, P, Orhon, I, Orosz, L, O'Rourke, Ej, Orozco, H, Ortega, Al, Ortona, E, Osellame, Ld, Oshima, J, Oshima, S, Osiewacz, Hd, Otomo, T, Otsu, K, Ou, Jj, Outeiro, Tf, Ouyang, Dy, Ouyang, H, Overholtzer, M, Ozbun, Ma, Ozdinler, Ph, Ozpolat, B, Pacelli, C, Paganetti, P, Page, G, Pages, G, Pagnini, U, Pajak, B, Pak, Sc, Pakos Zebrucka, K, Pakpour, N, Palková, Z, Palladino, F, Pallauf, K, Pallet, N, Palmieri, M, Paludan, Sr, Palumbo, C, Palumbo, S, Pampliega, O, Pan, H, Pan, W, Panaretakis, T, Pandey, A, Pantazopoulou, A, Papackova, Z, Papademetrio, Dl, Papassideri, I, Papini, A, Parajuli, N, Pardo, J, Parekh, Vv, Parenti, G, Park, Ji, Park, J, Park, Ok, Parker, R, Parlato, R, Parys, Jb, Parzych, Kr, Pasquet, Jm, Pasquier, B, Pasumarthi, Kb, Patschan, D, Patterson, C, Pattingre, S, Pattison, S, Pause, A, Pavenstädt, H, Pavone, F, Pedrozo, Z, Peña, Fj, Peñalva, Ma, Pende, M, Peng, J, Penna, F, Penninger, Jm, Pensalfini, A, Pepe, S, Pereira, Gj, Pereira, Pc, Pérez de la Cruz, V, Pérez Pérez, Me, Pérez Rodríguez, D, Pérez Sala, D, Perier, C, Perl, A, Perlmutter, Dh, Perrotta, I, Pervaiz, S, Pesonen, M, Pessin, Je, Peters, Gj, Petersen, M, Petrache, I, Petrof, Bj, Petrovski, G, Phang, Jm, Piacentini, M, Pierdominici, M, Pierre, P, Pierrefite Carle, V, Pietrocola, F, Pimentel Muiños, Fx, Pinar, M, Pineda, B, Pinkas Kramarski, R, Pinti, M, Pinton, P, Piperdi, B, Piret, Jm, Platanias, Lc, Platta, Hw, Plowey, Ed, Pöggeler, S, Poirot, M, Polčic, P, Poletti, A, Poon, Ah, Popelka, H, Popova, B, Poprawa, I, Poulose, Sm, Poulton, J, Powers, Sk, Powers, T, Pozuelo Rubio, M, Prak, K, Prange, R, Prescott, M, Priault, M, Prince, S, Proia, Rl, Proikas Cezanne, T, Prokisch, H, Promponas, Vj, Przyklenk, K, Puertollano, R, Pugazhenthi, S, Puglielli, L, Pujol, A, Puyal, J, Pyeon, D, Qi, X, Qian, Wb, Qin, Zh, Qiu, Y, Qu, Z, Quadrilatero, J, Quinn, F, Raben, N, Rabinowich, H, Radogna, F, Ragusa, Mj, Rahmani, M, Raina, K, Ramanadham, S, Ramesh, R, Rami, A, Randall Demllo, S, Randow, F, Rao, H, Rao, Va, Rasmussen, Bb, Rasse, Tm, Ratovitski, Ea, Rautou, Pe, Ray, Sk, Razani, B, Reed, Bh, Reggiori, F, Rehm, M, Reichert, A, Rein, T, Reiner, Dj, Reits, E, Ren, J, Ren, X, Renna, M, Reusch, Je, Revuelta, Jl, Reyes, L, Rezaie, Ar, Richards, Ri, Richardson, Dr, Richetta, C, Riehle, Ma, Rihn, Bh, Rikihisa, Y, Riley, Be, Rimbach, G, Rippo, Mr, Ritis, K, Rizzi, F, Rizzo, E, Roach, Pj, Robbins, J, Roberge, M, Roca, G, Roccheri, Mc, Rocha, S, Rodrigues, Cm, Rodríguez, Ci, de Cordoba, Sr, Rodriguez Muela, N, Roelofs, J, Rogov, Vv, Rohn, Tt, Rohrer, B, Romanelli, D, Romani, L, Romano, P, Roncero, Mi, Rosa, Jl, Rosello, A, Rosen, Kv, Rosenstiel, P, Rost Roszkowska, M, Roth, Ka, Roué, G, Rouis, M, Rouschop, Km, Ruan, Dt, Ruano, D, Rubinsztein, Dc, Rucker EB, 3rd, Rudich, A, Rudolf, E, Rudolf, R, Ruegg, Ma, Ruiz Roldan, C, Ruparelia, Aa, Rusmini, P, Russ, Dw, Russo, Gl, Russo, G, Russo, R, Rusten, Te, Ryabovol, V, Ryan, Km, Ryter, Sw, Sabatini, Dm, Sacher, M, Sachse, C, Sack, Mn, Sadoshima, J, Saftig, P, Sagi Eisenberg, R, Sahni, S, Saikumar, P, Saito, T, Saitoh, T, Sakakura, K, Sakoh Nakatogawa, M, Sakuraba, Y, Salazar Roa, M, Salomoni, P, Saluja, Ak, Salvaterra, Pm, Salvioli, R, Samali, A, Sanchez, Am, Sánchez Alcázar, Ja, Sanchez Prieto, R, Sandri, M, Sanjuan, Ma, Santaguida, S, Santambrogio, L, Santoni, G, Dos Santos, Cn, Saran, S, Sardiello, M, Sargent, G, Sarkar, P, Sarkar, S, Sarrias, Mr, Sarwal, Mm, Sasakawa, C, Sasaki, M, Sass, M, Sato, K, Sato, M, Satriano, J, Savaraj, N, Saveljeva, S, Schaefer, L, Schaible, Ue, Scharl, M, Schatzl, Hm, Schekman, R, Scheper, W, Schiavi, A, Schipper, Hm, Schmeisser, H, Schmidt, J, Schmitz, I, Schneider, Be, Schneider, Em, Schneider, Jl, Schon, Ea, Schönenberger, Mj, Schönthal, Ah, Schorderet, Df, Schröder, B, Schuck, S, Schulze, Rj, Schwarten, M, Schwarz, Tl, Sciarretta, S, Scotto, K, Scovassi, Ai, Screaton, Ra, Screen, M, Seca, H, Sedej, S, Segatori, L, Segev, N, Seglen, Po, Seguí Simarro, Jm, Segura Aguilar, J, Seki, E, Sell, C, Selliez, I, Semenkovich, Cf, Semenza, Gl, Sen, U, Serra, Al, Serrano Puebla, A, Sesaki, H, Setoguchi, T, Settembre, C, Shacka, Jj, Shajahan Haq, An, Shapiro, Im, Sharma, S, She, H, Shen, Cj, Shen, Cc, Shen, Hm, Shen, S, Shen, W, Sheng, R, Sheng, X, Sheng, Zh, Shepherd, Tg, Shi, J, Shi, Q, Shi, Y, Shibutani, S, Shibuya, K, Shidoji, Y, Shieh, Jj, Shih, Cm, Shimada, Y, Shimizu, S, Shin, Dw, Shinohara, Ml, Shintani, M, Shintani, T, Shioi, T, Shirabe, K, Shiri Sverdlov, R, Shirihai, O, Shore, Gc, Shu, Cw, Shukla, D, Sibirny, Aa, Sica, V, Sigurdson, Cj, Sigurdsson, Em, Sijwali, P, Sikorska, B, Silveira, Wa, Silvente Poirot, S, Silverman, Ga, Simak, J, Simmet, T, Simon, Ak, Simon, Hu, Simone, C, Simons, M, Simonsen, A, Singh, R, Singh, Sv, Singh, Sk, Sinha, D, Sinha, S, Sinicrope, Fa, Sirko, A, Sirohi, K, Sishi, Bj, Sittler, A, Siu, Pm, Sivridis, E, Skwarska, A, Slack, R, Slaninová, I, Slavov, N, Smaili, S, Smalley, K, Smith, Dr, Soenen, Sj, Soleimanpour, Sa, Solhaug, A, Somasundaram, K, Son, Jh, Sonawane, A, Song, C, Song, F, Song, Hk, Song, Jx, Song, W, Soo, Ky, Sood, Ak, Soong, Tw, Soontornniyomkij, V, Sorice, M, Sotgia, F, Soto Pantoja, Dr, Sotthibundhu, A, Sousa, Mj, Spaink, Hp, Span, Pn, Spang, A, Sparks, Jd, Speck, Pg, Spector, Sa, Spies, Cd, Springer, W, Clair, D, Stacchiotti, A, Staels, B, Stang, Mt, Starczynowski, Dt, Starokadomskyy, P, Steegborn, C, Steele, Jw, Stefanis, L, Steffan, J, Stellrecht, Cm, Stenmark, H, Stepkowski, Tm, Stern, St, Stevens, C, Stockwell, Br, Stoka, V, Storchova, Z, Stork, B, Stratoulias, V, Stravopodis, Dj, Strnad, P, Strohecker, Am, Ström, Al, Stromhaug, P, Stulik, J, Su, Yx, Su, Z, Subauste, C, Subramaniam, S, Sue, Cm, Suh, Sw, Sui, X, Sukseree, S, Sulzer, D, Sun, Fl, Sun, J, Sun, Sy, Sun, Y, Sundaramoorthy, V, Sung, J, Suzuki, H, Suzuki, K, Suzuki, N, Suzuki, T, Suzuki, Yj, Swanson, M, Swanton, C, Swärd, K, Swarup, G, Sweeney, St, Sylvester, Pw, Szatmari, Z, Szegezdi, E, Szlosarek, Pw, Taegtmeyer, H, Tafani, M, Taillebourg, E, Tait, Sw, Takacs Vellai, K, Takahashi, Y, Takáts, S, Takemura, G, Takigawa, N, Talbot, Nj, Tamagno, E, Tamburini, J, Tan, Cp, Tan, L, Tan, Ml, Tan, M, Tan, Yj, Tanaka, K, Tanaka, M, Tang, D, Tang, G, Tanida, I, Tanji, K, Tannous, Ba, Tapia, Ja, Tasset Cuevas, I, Tatar, M, Tavassoly, I, Tavernarakis, N, Taylor, A, Taylor, G, Taylor, Ga, Taylor, Jp, Taylor, Mj, Tchetina, Ev, Tee, Ar, Teixeira Clerc, F, Telang, S, Tencomnao, T, Teng, Bb, Teng, Rj, Terro, F, Tettamanti, G, Theiss, Al, Theron, Ae, Thomas, Kj, Thomé, Mp, Thomes, Pg, Thorburn, A, Thorner, J, Thum, T, Thumm, M, Thurston, Tl, Tian, L, Till, A, Ting, Jp, Titorenko, Vi, Toker, L, Toldo, S, Tooze, Sa, Topisirovic, I, Torgersen, Ml, Torosantucci, L, Torriglia, A, Torrisi, Mr, Tournier, C, Towns, R, Trajkovic, V, Travassos, Lh, Triola, G, Tripathi, Dn, Trisciuoglio, D, Troncoso, R, Trougakos, Ip, Truttmann, Ac, Tsai, Kj, Tschan, Mp, Tseng, Yh, Tsukuba, T, Tsung, A, Tsvetkov, A, Tu, S, Tuan, Hy, Tucci, M, Tumbarello, Da, Turk, B, Turk, V, Turner, Rf, Tveita, Aa, Tyagi, Sc, Ubukata, M, Uchiyama, Y, Udelnow, A, Ueno, T, Umekawa, M, Umemiya Shirafuji, R, Underwood, Br, Ungermann, C, Ureshino, Rp, Ushioda, R, Uversky, Vn, Uzcátegui, Nl, Vaccari, T, Vaccaro, Mi, Váchová, L, Vakifahmetoglu Norberg, H, Valdor, R, Valente, Em, Vallette, F, Valverde, Am, Van den Berghe, G, Van Den Bosch, L, van den Brink, Gr, van der Goot, Fg, van der Klei, Ij, van der Laan, Lj, van Doorn, Wg, van Egmond, M, van Golen, Kl, Van Kaer, L, van Lookeren Campagne, M, Vandenabeele, P, Vandenberghe, W, Vanhorebeek, I, Varela Nieto, I, Vasconcelos, Mh, Vasko, R, Vavvas, Dg, Vega Naredo, I, Velasco, G, Velentzas, Ad, Velentzas, Pd, Vellai, T, Vellenga, E, Vendelbo, Mh, Venkatachalam, K, Ventura, N, Ventura, S, Veras, P, Verdier, M, Vertessy, Bg, Viale, A, Vidal, M, Vieira, H, Vierstra, Rd, Vigneswaran, N, Vij, N, Vila, M, Villar, M, Villar, Vh, Villarroya, J, Vindis, C, Viola, G, Viscomi, Mt, Vitale, G, Vogl, Dt, Voitsekhovskaja, Ov, von Haefen, C, von Schwarzenberg, K, Voth, De, Vouret Craviari, V, Vuori, K, Vyas, Jm, Waeber, C, Walker, Cl, Walker, Mj, Walter, J, Wan, L, Wan, X, Wang, B, Wang, C, Wang, Cy, Wang, D, Wang, F, Wang, G, Wang, Hj, Wang, H, Wang, Hg, Wang, Hd, Wang, J, Wang, M, Wang, Mq, Wang, Py, Wang, P, Wang, Rc, Wang, S, Wang, Tf, Wang, X, Wang, Xj, Wang, Xw, Wang, Y, Wang, Yj, Wang, Yt, Wang, Zn, Wappner, P, Ward, C, Ward, Dm, Warnes, G, Watada, H, Watanabe, Y, Watase, K, Weaver, Te, Weekes, Cd, Wei, J, Weide, T, Weihl, Cc, Weindl, G, Weis, Sn, Wen, L, Wen, X, Wen, Y, Westermann, B, Weyand, Cm, White, Ar, White, E, Whitton, Jl, Whitworth, Aj, Wiels, J, Wild, F, Wildenberg, Me, Wileman, T, Wilkinson, D, Wilkinson, S, Willbold, D, Williams, C, Williams, K, Williamson, Pr, Winklhofer, Kf, Witkin, S, Wohlgemuth, Se, Wollert, T, Wolvetang, Ej, Wong, E, Wong, Gw, Wong, Rw, Wong, Vk, Woodcock, Ea, Wright, Kl, Wu, C, Wu, D, Wu, G, Wu, J, Wu, M, Wu, S, Wu, Wk, Wu, Y, Wu, Z, Xavier, Cp, Xavier, Rj, Xia, Gx, Xia, T, Xia, W, Xia, Y, Xiao, H, Xiao, J, Xiao, S, Xiao, W, Xie, Cm, Xie, Z, Xilouri, M, Xiong, Y, Xu, C, Xu, F, Xu, H, Xu, J, Xu, L, Xu, X, Xu, Y, Xu, Zx, Xu, Z, Xue, Y, Yamada, T, Yamamoto, A, Yamanaka, K, Yamashina, S, Yamashiro, S, Yan, B, Yan, X, Yan, Z, Yanagi, Y, Yang, D, Yang, Jm, Yang, L, Yang, M, Yang, Pm, Yang, P, Yang, Q, Yang, W, Yang, Wy, Yang, X, Yang, Y, Yang, Z, Yao, Mc, Yao, Pj, Yao, X, Yao, Z, Yasui, L, Ye, M, Yedvobnick, B, Yeganeh, B, Yeh, E, Yeyati, Pl, Yi, F, Yi, L, Yin, Xm, Yip, Ck, Yoo, Ym, Yoo, Yh, Yoon, Sy, Yoshida, Ki, Yoshimori, T, Young, Kh, Yu, H, Yu, Jj, Yu, Jt, Yu, J, Yu, L, Yu, Wh, Yu, Xf, Yu, Z, Yuan, J, Yuan, Zm, Yue, By, Yue, J, Yue, Z, Zacks, Dn, Zacksenhaus, E, Zaffaroni, N, Zaglia, T, Zakeri, Z, Zecchini, V, Zeng, J, Zeng, M, Zeng, Q, Zervos, A, Zhang, Dd, Zhang, F, Zhang, G, Zhang, Gc, Zhang, H, Zhang, J, Zhang, Jp, Zhang, L, Zhang, My, Zhang, X, Zhang, Xd, Zhang, Y, Zhao, M, Zhao, Wl, Zhao, X, Zhao, Yg, Zhao, Y, Zhao, Yx, Zhao, Z, Zhao, Zj, Zheng, D, Zheng, Xl, Zheng, X, Zhivotovsky, B, Zhong, Q, Zhou, Gz, Zhou, G, Zhou, H, Zhou, Sf, Zhou, Xj, Zhu, H, Zhu, Wg, Zhu, W, Zhu, Xf, Zhu, Y, Zhuang, Sm, Zhuang, X, Ziparo, E, Zois, Ce, Zoladek, T, Zong, Wx, Zorzano, A, Zughaier, Sm, AII - Amsterdam institute for Infection and Immunity, Medical Microbiology and Infection Prevention, Other departments, CCA -Cancer Center Amsterdam, Center of Experimental and Molecular Medicine, Radiotherapy, AGEM - Amsterdam Gastroenterology Endocrinology Metabolism, Medical Biochemistry, ANS - Cellular & Molecular Mechanisms, Cell Biology and Histology, Gastroenterology and Hepatology, Tytgat Institute for Liver and Intestinal Research, Daniel J Klionsky, Kotb Abdelmohsen, Akihisa Abe, Md Joynal Abedin, Hagai Abeliovich, Abraham Acevedo Arozena, Hiroaki Adachi, Christopher M Adam, Peter D Adam, Khosrow Adeli, Peter J Adhihetty, Sharon G Adler, Galila Agam, Rajesh Agarwal, Manish K Aghi, Maria Agnello, Patrizia Agostini, Patricia V Aguilar, Julio Aguirre-Ghiso, Edoardo M Airoldi, Slimane Ait-Si-Ali, Takahiko Akematsu, Emmanuel T Akporiaye, Mohamed Al-Rubeai, Guillermo M Albaiceta, Chris Albanese, Diego Albani, Matthew L Albert, Jesus Aldudo, Hana Algül, Mehrdad Alirezaei, Iraide Alloza, Alexandru Almasan, Maylin Almonte-Beceril, Emad S Alnemri, Covadonga Alonso, Nihal Altan-Bonnet, Dario C Altieri, Silvia Alvarez, Lydia Alvarez- Erviti, Sandro Alve, Giuseppina Amadoro, Atsuo Amano, Consuelo Amantini, Santiago Ambrosio, Ivano Amelio, Amal O Amer, Mohamed Amessou, Angelika Amon, Zhenyi An, Frank A Anania, Stig U Andersen, Usha P Andley, Catherine K Andreadi, Nathalie Andrieu- Abadie, Alberto Anel, David K Ann, Shailendra Anoopkumar-Dukie, Manuela Antonioli, Hiroshi Aoki, Nadezda Apostolova, Saveria Aquila, Katia Aquilano, Koichi Araki, Eli Arama, Agustin Aranda, Jun Araya, Alexandre Arcaro, Esperanza Aria, Hirokazu Arimoto, Aileen R Ariosa, Jane L Armstrong, Thierry Arnould, Ivica Arsov, Katsuhiko Asanuma, Valerie Askana, Eric Asselin, Ryuichiro Atarashi, Sally S Atherton, Julie D Atkin, Laura D Attardi, Patrick Auberger, Georg Auburger, Laure Aurelian, Riccardo Autelli, Laura Avagliano, Maria Laura Avantaggiati, Limor Avrahami, Suresh Awale, Neelam Azad, Tiziana Bachetti, Jonathan M Backer, Dong- Hun Bae, Jae-sung Bae, Ok-Nam Bae, Soo Han Bae, Eric H Baehrecke, Seung-Hoon Baek, Stephen Baghdiguian, Agnieszka Bagniewska-Zadworna, Hua Bai, Jie Bai, Xue-Yuan Bai, Yannick Bailly, Kithiganahalli Narayanaswamy Balaji, Walter Balduini, Andrea Ballabio, Rena Balzan, Rajkumar Banerjee, Gábor Bánhegyi, Haijun Bao, Benoit Barbeau, Maria D Barrachina, Esther Barreiro, Bonnie Bartel, Alberto Bartolomé, Diane C Bassham, Maria Teresa Bassi, Robert C Bast Jr, Alakananda Basu, Maria Teresa Batista, Henri Batoko, Maurizio Battino, Kyle Bauckman, Bradley L Baumgarner, K Ulrich Bayer, Rupert Beale, Jean-François Beaulieu, George R. Beck Jr, Christoph Becker, J David Beckham, Pierre-André Bédard, Patrick J Bednarski, Thomas J Begley, Christian Behl, Christian Behrend, Georg MN Behren, Kevin E Behrn, Eloy Bejarano, Amine Belaid, Francesca Belleudi, Giovanni Bénard, Guy Berchem, Daniele Bergamaschi, Matteo Bergami, Ben Berkhout, Laura Berliocchi, Amélie Bernard, Monique Bernard, Francesca Bernassola, Anne Bertolotti, Amanda S Be, Sébastien Besteiro, Saverio Bettuzzi, Savita Bhalla, Shalmoli Bhattacharyya, Sujit K Bhutia, Caroline Biagosch, Michele Wolfe Bianchi, Martine Biard-Piechaczyk, Viktor Bille, Claudia Bincoletto, Baris Bingol, Sara W Bird, Marc Bitoun, Ivana Bjedov, Craig Blackstone, Lionel Blanc, Guillermo A Blanco, Heidi Kiil Blomhoff, Emilio Boada-Romero, Stefan Böckler, Marianne Boe, Kathleen Boesze-Battaglia, Lawrence H Boise, Alessandra Bolino, Andrea Boman, Paolo Bonaldo, Matteo Bordi, Jürgen Bosch, Luis M Botana, Joelle Botti, German Bou, Marina Bouché, Marion Bouchecareilh, Marie- Josée Boucher, Michael E Boulton, Sebastien G Bouret, Patricia Boya, Michaël Boyer-Guittaut, Peter V Bozhkov, Nathan Brady, Vania MM Braga, Claudio Brancolini, Gerhard H Brau, José M Bravo-San Pedro, Lisa A Brennan, Emery H Bresnick, Patrick Brest, Dave Bridge, MarieAgnès Bringer, Marisa Brini, Glauber C Brito, Bertha Brodin, Paul S Brooke, Eric J Brown, Karen Brown, Hal E Broxmeyer, Alain Bruhat, Patricia Chakur Brum, John H Brumell, Nicola Brunetti-Pierri, Robert J Bryson-Richardson, Shilpa Buch, Alastair M Buchan, Hikmet Budak, Dmitry V Bulavin, Scott J Bultman, Geert Bultynck, Vladimir Bumbasirevic, Yan Burelle, Robert E Burke, Margit Burmeister, Peter Bütikofer, Laura Caberlotto, Ken Cadwell, Monika Cahova, Dongsheng Cai, Jingjing Cai, Qian Cai, Sara Calatayud, Nadine Camougrand, Michelangelo Campanella, Grant R Campbell, Matthew Campbell, Silvia Campello, Robin Candau, Isabella Caniggia, Lavinia Cantoni, Lizhi Cao, Allan B Caplan, Michele Caraglia, Claudio Cardinali, Sandra Morais Cardoso, Jennifer S Carew, Laura A Carleton, Cathleen R Carlin, Silvia Carloni, Sven R Carlsson, Didac Carmona-Gutierrez, Leticia AM Carneiro, Oliana Carnevali, Serena Carra, Alice Carrier, Bernadette Carroll, Caty Casa, Josefina Casa, Giuliana Cassinelli, Perrine Castet, Susana Castro-Obregon, Gabriella Cavallini, Isabella Ceccherini, Francesco Cecconi, Arthur I Cederbaum, Valentín Ceña, Simone Cenci, Claudia Cerella, Davide Cervia, Silvia Cetrullo, Hassan Chaachouay, Han-Jung Chae, Andrei S Chagin, Chee-Yin Chai, Gopal Chakrabarti, Georgios Chamilo, Edmond YW Chan, Matthew TV Chan, Dhyan Chandra, Pallavi Chandra, Chih-Peng Chang, Raymond Chuen-Chung Chang, Ta Yuan Chang, John C Chatham, Saurabh Chatterjee, Santosh Chauhan, Yongsheng Che, Michael E Cheetham, Rajkumar Cheluvappa, Chun-Jung Chen, Gang Chen, Guang-Chao Chen, Guoqiang Chen, Hongzhuan Chen, Jeff W Chen, Jian-Kang Chen, Min Chen, Mingzhou Chen, Peiwen Chen, Qi Chen, Quan Chen, Shang- Der Chen, Si Chen, Steve S-L Chen, Wei Chen, Wei-Jung Chen, Wen Qiang Chen, Wenli Chen, Xiangmei Chen, Yau-Hung Chen, Ye-Guang Chen, Yin Chen, Yingyu Chen, Yongshun Chen, Yu- Jen Chen, Yue-Qin Chen, Yujie Chen, Zhen Chen, Zhong Chen, Alan Cheng, Christopher HK Cheng, Hua Cheng, Heesun Cheong, Sara Cherry, Jason Chesney, Chun Hei Antonio Cheung, Eric Chevet, Hsiang Cheng Chi, Sung-Gil Chi, Fulvio Chiacchiera, Hui-Ling Chiang, Roberto Chiarelli, Mario Chiariello, Marcello Chieppa, Lih-Shen Chin, Mario Chiong, Gigi NC Chiu, Dong-Hyung Cho, Ssang-Goo Cho, William C Cho, Yong-Yeon Cho, Young-Seok Cho, Augustine MK Choi, Eui-Ju Choi, Eun-Kyoung Choi, Jayoung Choi, Mary E Choi, Seung-Il Choi, Tsui-Fen Chou, Salem Chouaib, Divaker Choubey, Vinay Choubey, Kuan-Chih Chow, Kamal Chowdhury, Charleen T Chu, Tsung-Hsien Chuang, Taehoon Chun, Hyewon Chung, Taijoon Chung, Yuen-Li Chung, Yong-Joon Chwae, Valentina Cianfanelli, Roberto Ciarcia, Iwona A Ciechomska, Maria Rosa Ciriolo, Mara Cirone, Sofie Claerhout, Michael J Clague, Joan Clària, Peter GH Clarke, Robert Clarke, Emilio Clementi, Cédric Cleyrat, Miriam Cnop, Eliana M Coccia, Tiziana Cocco, Patrice Codogno, Jörn Coer, Ezra EW Cohen, David Colecchia, Luisa Coletto, Núria S Coll, Emma Colucci-Guyon, Sergio Comincini, Maria Condello, Katherine L Cook, Graham H Coomb, Cynthia D Cooper, J Mark Cooper, Isabelle Coppen, Maria Tiziana Corasaniti, Marco Corazzari, Ramon Corbalan, Elisabeth Corcelle-Termeau, Mario D Cordero, Cristina Corral-Ramo, Olga Corti, Andrea Cossarizza, Paola Costelli, Safia Coste, Susan L Cotman, Ana Coto-Monte, Sandra Cottet, Eduardo Couve, Lori R Covey, L Ashley Cowart, Jeffery S Cox, Fraser P Coxon, Carolyn B Coyne, Mark S Cragg, Rolf J Craven, Tiziana Crepaldi, Jose L Crespo, Alfredo Criollo, Valeria Crippa, Maria Teresa Cruz, Ana Maria Cuervo, Jose M Cuezva, Taixing Cui, Pedro R Cutilla, Mark J Czaja, Maria F Czyzyk-Krzeska, Ruben K Dagda, Uta Dahmen, Chunsun Dai, Wenjie Dai, Yun Dai, Kevin N Dalby, Luisa Dalla Valle, Guillaume Dalmasso, Marcello D'Amelio, Markus Damme, Arlette Darfeuille-Michaud, Catherine Dargemont, Victor M Darley-Usmar, Srinivasan Dasarathy, Biplab Dasgupta, Srikanta Dash, Crispin R Da, Hazel Marie Davey, Lester M David, David Dávila, Roger J Davi, Ted M Dawson, Valina L Dawson, Paula Daza, Jackie de Belleroche, Paul de Figueiredo, Regina Celia Bressan Queiroz de Figueiredo, José de la Fuente, Luisa De Martino, Antonella De Mattei, Guido RY De Meyer, Angelo De Milito, Mauro De Santi, Wanderley de Souza, Vincenzo De Tata, Daniela De Zio, Jayanta Debnath, Reinhard Dechant, Jean-Paul Decuypere, Shane Deegan, Benjamin Dehay, Barbara Del Bello, Dominic P Del Re, Régis Delage-Mourroux, Lea MD Delbridge, Louise Deldicque, Elizabeth Delorme-Axford, Yizhen Deng, Joern Dengjel, Melanie Denizot, Paul Dent, Channing J Der, Vojo Deretic, Benoît Derrien, Eric Deutsch, Timothy P Devarenne, Rodney J Devenish, Sabrina Di Bartolomeo, Nicola Di Daniele, Fabio Di Domenico, Alessia Di Nardo, Simone Di Paola, Antonio Di Pietro, Livia Di Renzo, Aaron DiAntonio, Guillermo Díaz-Araya, Ines Díaz-Laviada, Maria T Diaz-Meco, Javier Diaz-Nido, Chad A Dickey, Robert C Dickson, Marc Diederich, Paul Digard, Ivan Dikic, Savithrama P Dinesh-Kumar, Chan Ding, Wen-Xing Ding, Zufeng Ding, Luciana Dini, Jörg HW Distler, Abhinav Diwan, Mojgan Djavaheri-Mergny, Kostyantyn Dmytruk, Renwick CJ Dobson, Volker Doetsch, Karol Dokladny, Svetlana Dokudovskaya, Massimo Donadelli, X Charlie Dong, Xiaonan Dong, Zheng Dong, Terrence M Donohue Jr, Kelly S Doran, Gabriella D'Orazi, Gerald W Dorn II, Victor Dosenko, Sami Dridi, Liat Drucker, Jie Du, Li-Lin Du, Lihuan Du, André du Toit, Priyamvada Dua, Lei Duan, Pu Duann, Vikash Kumar Dubey, Michael R Duchen, Michel A Duchosal, Helene Duez, Isabelle Dugail, Verónica I Dumit, Mara C Duncan, Elaine A Dunlop, William A Dunn Jr, Nicolas Dupont, Luc Dupui, Raúl V Durán, Thomas M Durcan, Stéphane Duvezin-Caubet, Umamaheswar Duvvuri, Vinay Eapen, Darius Ebrahimi-Fakhari, Arnaud Echard, Leopold Eckhart, Charles L Edelstein, Aimee L Edinger, Ludwig Eichinger, Tobias Eisenberg, Avital Eisenberg-Lerner, N Tony Eissa, Wafik S El-Deiry, Victoria El-Khoury, Zvulun Elazar, Hagit Eldar-Finkelman, Chris JH Elliott, Enzo Emanuele, Urban Emmenegger, Nikolai Engedal, Anna-Mart Engelbrecht, Simone Engelender, Jorrit M Enserink, Ralf Erdmann, Jekaterina Erenpreisa, Rajaraman Eri, Jason L Eriksen, Andreja Erman, Ricardo Escalante, Eeva- Liisa Eskelinen, Lucile Espert, Lorena Esteban-Martínez, Thomas J Evan, Mario Fabri, Gemma Fabria, Cinzia Fabrizi, Antonio Facchiano, Nils J Færgeman, Alberto Faggioni, W Douglas Fairlie, Chunhai Fan, Daping Fan, Jie Fan, Shengyun Fang, Manolis Fanto, Alessandro Fanzani, Thomas Farka, Mathias Faure, Francois B Favier, Howard Fearnhead, Massimo Federici, Erkang Fei, Tania C Felizardo, Hua Feng, Yibin Feng, Yuchen Feng, Thomas A Ferguson, Álvaro F Fernández, Maite G Fernandez-Barrena, Jose C Fernandez-Checa, Arsenio Fernández-López, Martin E Fernandez-Zapico, Olivier Feron, Elisabetta Ferraro, Carmen Veríssima Ferreira-Halder, Laszlo Fesu, Ralph Feuer, Fabienne C Fiesel, Eduardo C Filippi-Chiela, Giuseppe Filomeni, Gian Maria Fimia, John H Fingert, Steven Finkbeiner, Toren Finkel, Filomena Fiorito, Paul B Fisher, Marc Flajolet, Flavio Flamigni, Oliver Florey, Salvatore Florio, R Andres Floto, Marco Folini, Carlo Follo, Edward A Fon, Francesco Fornai, Franco Fortunato, Alessandro Fraldi, Rodrigo Franco, Arnaud Francoi, Aurélie Françoi, Lisa B Frankel, Iain DC Fraser, Norbert Frey, Damien G Freyssenet, Christian Frezza, Scott L Friedman, Daniel E Frigo, Dongxu Fu, José M Fuente, Juan Fueyo, Yoshio Fujitani, Yuuki Fujiwara, Mikihiro Fujiya, Mitsunori Fukuda, Simone Fulda, Carmela Fusco, Bozena Gabryel, Matthias Gaestel, Philippe Gailly, Malgorzata Gajewska, Sehamuddin Galadari, Gad Galili, Inmaculada Galindo, Maria F Galindo, Giovanna Galliciotti, Lorenzo Galluzzi, Luca Galluzzi, Vincent Galy, Noor Gammoh, Sam Gandy, Anand K Ganesan, Swamynathan Ganesan, Ian G Ganley, Monique Gannagé, Fen-Biao Gao, Feng Gao, Jian-Xin Gao, Lorena García Nannig, Eleonora García Véscovi, Marina Garcia-Macía, Carmen Garcia- Ruiz, Abhishek D Garg, Pramod Kumar Garg, Ricardo Gargini, Nils Christian Gassen, Damián Gatica, Evelina Gatti, Julie Gavard, Evripidis Gavathioti, Liang Ge, Pengfei Ge, Shengfang Ge, Po-Wu Gean, Vania Gelmetti, Armando A Genazzani, Jiefei Geng, Pascal Genschik, Lisa Gerner, Jason E Gestwicki, David A Gewirtz, Saeid Ghavami, Eric Ghigo, Debabrata Ghosh, Anna Maria Giammarioli, Francesca Giampieri, Claudia Giampietri, Alexandra Giatromanolaki, Derrick J Gibbing, Lara Gibellini, Spencer B Gibson, Vanessa Ginet, Antonio Giordano, Flaviano Giorgini, Elisa Giovannetti, Stephen E Girardin, Suzana Gispert, Sandy Giuliano, Candece L Gladson, Alvaro Glavic, Martin Gleave, Nelly Godefroy, Robert M Gogal Jr, Kuppan Gokulan, Gustavo H Goldman, Delia Goletti, Michael S Goligorsky, Aldrin V Gome, Ligia C Gome, Hernando Gomez, Candelaria Gomez-Manzano, Rubén Gómez-Sánchez, Dawit AP Gonçalve, Ebru Goncu, Qingqiu Gong, Céline Gongora, Carlos B Gonzalez, Pedro Gonzalez-Alegre, Pilar Gonzalez-Cabo, Rosa Ana González-Polo, Ing Swie Goping, Carlos Gorbea, Nikolai V Gorbunov, Daphne R Goring, Adrienne M Gorman, Sharon M Gorski, Sandro Goruppi, Shino Goto- Yamada, Cecilia Gotor, Roberta A Gottlieb, Illana Goze, Devrim Gozuacik, Yacine Graba, Martin Graef, Giovanna E Granato, Gary Dean Grant, Steven Grant, Giovanni Luca Gravina, Douglas R Green, Alexander Greenhough, Michael T Greenwood, Benedetto Grimaldi, Frédéric Gro, Charles Grose, Jean-Francois Groulx, Florian Gruber, Paolo Grumati, Tilman Grune, Jun-Lin Guan, Kun-Liang Guan, Barbara Guerra, Carlos Guillen, Kailash Gulshan, Jan Gunst, Chuanyong Guo, Lei Guo, Ming Guo, Wenjie Guo, Xu-Guang Guo, Andrea A Gust, Åsa B Gustafsson, Elaine Gutierrez, Maximiliano G Gutierrez, Ho-Shin Gwak, Albert Haa, James E Haber, Shinji Hadano, Monica Hagedorn, David R Hahn, Andrew J Halayko, Anne Hamacher-Brady, Kozo Hamada, Ahmed Hamai, Andrea Hamann, Maho Hamasaki, Isabelle Hamer, Qutayba Hamid, Ester M Hammond, Feng Han, Weidong Han, James T Handa, John A Hanover, Malene Hansen, Masaru Harada, Ljubica Harhaji-Trajkovic, J Wade Harper, Abdel Halim Harrath, Adrian L Harri, James Harri, Udo Hasler, Peter Hasselblatt, Kazuhisa Hasui, Robert G Hawley, Teresa S Hawley, Congcong He, Cynthia Y He, Fengtian He, Gu He, Rong-Rong He, Xian-Hui He, You-Wen He, Yu- Ying He, Joan K Heath, Marie-Josée Hébert, Robert A Heinzen, Gudmundur Vignir Helgason, Michael Hensel, Elizabeth P Henske, Chengtao Her, Paul K Herman, Agustín Hernández, Carlos Hernandez, Sonia Hernández-Tiedra, Claudio Hetz, P Robin Hiesinger, Katsumi Higaki, Sabine Hilfiker, Bradford G Hill, Joseph A Hill, William D Hill, Keisuke Hino, Daniel Hofiu, Paul Hofman, Günter U Höglinger, Jörg Höhfeld, Marina K Holz, Yonggeun Hong, David A Hood, Jeroen JM Hoozeman, Thorsten Hoppe, Chin Hsu, Chin-Yuan Hsu, Li-Chung Hsu, Dong Hu, Guochang Hu, Hong-Ming Hu, Hongbo Hu, Ming Chang Hu, Yu-Chen Hu, Zhuo-Wei Hu, Fang Hua, Ya Hua, Canhua Huang, Huey-Lan Huang, Kuo-How Huang, Kuo-Yang Huang, Shile Huang, Shiqian Huang, Wei-Pang Huang, Yi-Ran Huang, Yong Huang, Yunfei Huang, Tobias B Huber, Patricia Huebbe, Won-Ki Huh, Juha J Hulmi, Gang Min Hur, James H Hurley, Zvenyslava Husak, Sabah NA Hussain, Salik Hussain, Jung Jin Hwang, Seungmin Hwang, Thomas IS Hwang, Atsuhiro Ichihara, Yuzuru Imai, Carol Imbriano, Megumi Inomata, Takeshi Into, Valentina Iovane, Juan L Iovanna, Renato V Iozzo, Nancy Y Ip, Javier E Irazoqui, Pablo Iribarren, Yoshitaka Isaka, Aleksandra J Isakovic, Harry Ischiropoulo, Jeffrey S Isenberg, Mohammad Ishaq, Hiroyuki Ishida, Isao Ishii, Jane E Ishmael, Ciro Isidoro, Ken-ichi Isobe, Erika Isono, Shohreh Issazadeh- Navika, Koji Itahana, Eisuke Itakura, Andrei I Ivanov, Anand Krishnan V Iyer, José M Izquierdo, Yotaro Izumi, Valentina Izzo, Marja Jäättelä, Nadia Jaber, Daniel John Jackson, William T Jackson, Tony George Jacob, Thomas S Jacque, Chinnaswamy Jagannath, Ashish Jain, Nihar Ranjan Jana, Byoung Kuk Jang, Alkesh Jani, Bassam Janji, Paulo Roberto Jannig, Patric J Jansson, Steve Jean, Marina Jendrach, Ju-Hong Jeon, Niels Jessen, Eui-Bae Jeung, Kailiang Jia, Lijun Jia, Hong Jiang, Hongchi Jiang, Liwen Jiang, Teng Jiang, Xiaoyan Jiang, Xuejun Jiang, Ying Jiang, Yongjun Jiang, Alberto Jiménez, Cheng Jin, Hongchuan Jin, Lei Jin, Meiyan Jin, Shengkan Jin, Umesh Kumar Jinwal, Eun-Kyeong Jo, Terje Johansen, Daniel E Johnson, Gail VW Johnson, James D Johnson, Eric Jonasch, Chris Jone, Leo AB Joosten, Joaquin Jordan, Anna-Maria Joseph, Bertrand Joseph, Annie M Joubert, Dianwen Ju, Jingfang Ju, Hsueh-Fen Juan, Katrin Juenemann, Gábor Juhász, Hye Seung Jung, Jae U Jung, Yong-Keun Jung, Heinz Jungbluth, Matthew J Justice, Barry Jutten, Nadeem O Kaakoush, Kai Kaarniranta, Allen Kaasik, Tomohiro Kabuta, Bertrand Kaeffer, Katarina Kågedal, Alon Kahana, Shingo Kajimura, Or Kakhlon, Manjula Kalia, Dhan V Kalvakolanu, Yoshiaki Kamada, Konstantinos Kamba, Vitaliy O Kaminskyy, Harm H Kampinga, Mustapha Kandouz, Chanhee Kang, Rui Kang, Tae-Cheon Kang, Tomotake Kanki, Thirumala- Devi Kanneganti, Haruo Kanno, Anumantha G Kanthasamy, Marc Kantorow, Maria Kaparakis- Liasko, Orsolya Kapuy, Vassiliki Karantza, Md Razaul Karim, Parimal Karmakar, Arthur Kaser, Susmita Kaushik, Thomas Kawula, A Murat Kaynar, Po-Yuan Ke, Zun-Ji Ke, John H Kehrl, Kate E Keller, Jongsook Kim Kemper, Anne K Kenworthy, Oliver Kepp, Andreas Kern, Santosh Kesari, David Kessel, Robin Ketteler, Isis do Carmo Kettelhut, Bilon Khambu, Muzamil Majid Khan, Vinoth KM Khandelwal, Sangeeta Khare, Juliann G Kiang, Amy A Kiger, Akio Kihara, Arianna L Kim, Cheol Hyeon Kim, Deok Ryong Kim, Do-Hyung Kim, Eung Kweon Kim, Hye Young Kim, Hyung-Ryong Kim, Jae-Sung Kim, Jeong Hun Kim, Jin Cheon Kim, Jin Hyoung Kim, Kwang Woon Kim, Michael D Kim, Moon-Moo Kim, Peter K Kim, Seong Who Kim, Soo-Youl Kim, Yong-Sun Kim, Yonghyun Kim, Adi Kimchi, Alec C Kimmelman, Tomonori Kimura, Jason S King, Karla Kirkegaard, Vladimir Kirkin, Lorrie A Kirshenbaum, Shuji Kishi, Yasuo Kitajima, Katsuhiko Kitamoto, Yasushi Kitaoka, Kaio Kitazato, Rudolf A Kley, Walter T Klimecki, Michael Klinkenberg, Jochen Klucken, Helene Knævelsrud, Erwin Knecht, Laura Knuppertz, Jiunn-Liang Ko, Satoru Kobayashi, Jan C Koch, Christelle Koechlin-Ramonatxo, Ulrich Koenig, Young Ho Koh, Katja Köhler, Sepp D Kohlwein, Masato Koike, Masaaki Komatsu, Eiki Kominami, Dexin Kong, Hee Jeong Kong, Eumorphia G Konstantakou, Benjamin T Kopp, Tamas Korcsmaro, Laura Korhonen, Viktor I Korolchuk, Nadya V Koshkina, Yanjun Kou, Michael I Koukouraki, Constantinos Koumeni, Attila L Kovác, Tibor Kovác, Werner J Kovac, Daisuke Koya, Claudine Kraft, Dimitri Krainc, Helmut Kramer, Tamara Kravic-Stevovic, Wilhelm Krek, Carole Kretz-Remy, Roswitha Krick, Malathi Krishnamurthy, Janos Kriston-Vizi, Guido Kroemer, Michael C Kruer, Rejko Kruger, Nicholas T Ktistaki, Kazuyuki Kuchitsu, Christian Kuhn, Addanki Pratap Kumar, Anuj Kumar, Ashok Kumar, Deepak Kumar, Dhiraj Kumar, Rakesh Kumar, Sharad Kumar, Mondira Kundu, Hsing-Jien Kung, Atsushi Kuno, Sheng-Han Kuo, Jeff Kuret, Tino Kurz, Terry Kwok, Taeg Kyu Kwon, Yong Tae Kwon, Irene Kyrmizi, Albert R La Spada, Frank Lafont, Tim Lahm, Aparna Lakkaraju, Truong Lam, Trond Lamark, Steve Lancel, Terry H Landowski, Darius JR Lane, Jon D Lane, Cinzia Lanzi, Pierre Lapaquette, Louis R Lapierre, Jocelyn Laporte, Johanna Laukkarinen, Gordon W Laurie, Sergio Lavandero, Lena Lavie, Matthew J LaVoie, Betty Yuen Kwan Law, Helen Ka-wai Law, Kelsey B Law, Robert Layfield, Pedro A Lazo, Laurent Le Cam, Karine G Le Roch, Hervé Le Stunff, Vijittra Leardkamolkarn, Marc Lecuit, Byung-Hoon Lee, Che- Hsin Lee, Erinna F Lee, Gyun Min Lee, He-Jin Lee, Hsinyu Lee, Jae Keun Lee, Jongdae Lee, Juhyun Lee, Jun Hee Lee, Michael Lee, Myung-Shik Lee, Patty J Lee, Sam W Lee, Seung-Jae Lee, Shiow-Ju Lee, Stella Y Lee, Sug Hyung Lee, Sung Sik Lee, Sung-Joon Lee, Sunhee Lee, Ying- Ray Lee, Yong J Lee, Young H Lee, Christiaan Leeuwenburgh, Sylvain Lefort, Renaud Legoui, Jinzhi Lei, Qun-Ying Lei, David A Leib, Gil Leibowitz, Istvan Lekli, Stéphane D Lemaire, John J Lemaster, Marius K Lemberg, Antoinette Lemoine, Shuilong Leng, Guido Lenz, Paola Lenzi, Lilach O Lerman, Daniele Lettieri Barbato, Julia I-Ju Leu, Hing Y Leung, Beth Levine, Patrick A Lewi, Frank Lezoualc'h, Chi Li, Faqiang Li, Feng-Jun Li, Jun Li, Ke Li, Lian Li, Min Li, Qiang Li, Rui Li, Sheng Li, Wei Li, Xiaotao Li, Yumin Li, Jiqin Lian, Chengyu Liang, Qiangrong Liang, Yulin Liao, Joana Liberal, Pawel P Liberski, Pearl Lie, Andrew P Lieberman, Hyunjung Jade Lim, Kah-Leong Lim, Kyu Lim, Raquel T Lima, Chang-Shen Lin, Chiou-Feng Lin, Fang Lin, Fangming Lin, Fu-Cheng Lin, Kui Lin, Kwang-Huei Lin, Pei-Hui Lin, Tianwei Lin, Wan-Wan Lin, Yee-Shin Lin, Yong Lin, Rafael Linden, Dan Lindholm, Lisa M Lindqvist, Paul Lingor, Andreas Linkermann, Lance A Liotta, Marta M Lipinski, Vitor A Lira, Michael P Lisanti, Paloma B Liton, Bo Liu, Chong Liu, Chun-Feng Liu, Fei Liu, Hung-Jen Liu, Jianxun Liu, Jing-Jing Liu, Jing-Lan Liu, Ke Liu, Leyuan Liu, Liang Liu, Quentin Liu, Rong-Yu Liu, Shiming Liu, Shuwen Liu, Wei Liu, Xian-De Liu, Xiangguo Liu, Xiao-Hong Liu, Xinfeng Liu, Xu Liu, Xueqin Liu, Yang Liu, Yule Liu, Zexian Liu, Zhe Liu, Juan P Liuzzi, Gérard Lizard, Mila Ljujic, Irfan J Lodhi, Susan E Logue, Bal L Lokeshwar, Yun Chau Long, Sagar Lonial, Benjamin Loo, Carlos López-Otín, Cristina López-Vicario, Mar Lorente, Philip L Lorenzi, Péter Lõrincz, Marek Lo, Michael T Lotze, Penny E Lovat, Binfeng Lu, Bo Lu, Jiahong Lu, Qing Lu, She-Min Lu, Shuyan Lu, Yingying Lu, Frédéric Luciano, Shirley Luckhart, John Milton Lucocq, Paula Ludovico, Aurelia Lugea, Nicholas W Lukac, Julian J Lum, Anders H Lund, Honglin Luo, Jia Luo, Shouqing Luo, Claudio Luparello, Timothy Lyon, Jianjie Ma, Yi Ma, Yong Ma, Zhenyi Ma, Juliano Machado, Glaucia M Machado-Santelli, Fernando Macian, Gustavo C MacIntosh, Jeffrey P MacKeigan, Kay F Macleod, John D MacMicking, Lee Ann MacMillan-Crow, Frank Madeo, Muniswamy Madesh, Julio Madrigal-Matute, Akiko Maeda, Tatsuya Maeda, Gustavo Maegawa, Emilia Maellaro, Hannelore Mae, Marta Magariño, Kenneth Maiese, Tapas K Maiti, Luigi Maiuri, Maria Chiara Maiuri, Carl G Maki, Roland Malli, Walter Malorni, Alina Maloyan, Fathia Mami-Chouaib, Na Man, Joseph D Mancia, Eva-Maria Mandelkow, Michael A Mandell, Angelo A Manfredi, Serge N Manié, Claudia Manzoni, Kai Mao, Zixu Mao, Zong-Wan Mao, Philippe Marambaud, Anna Maria Marconi, Zvonimir Marelja, Gabriella Marfe, Marta Margeta, Eva Margittai, Muriel Mari, Francesca V Mariani, Concepcio Marin, Sara Marinelli, Guillermo Mariño, Ivanka Markovic, Rebecca Marquez, Alberto M Martelli, Sascha Marten, Katie R Martin, Seamus J Martin, Shaun Martin, Miguel A Martin- Acebe, Paloma Martín-Sanz, Camille Martinand-Mari, Wim Martinet, Jennifer Martinez, Nuria Martinez-Lopez, Ubaldo Martinez-Outschoorn, Moisés Martínez-Velázquez, Marta Martinez- Vicente, Waleska Kerllen Martin, Hirosato Mashima, James A Mastrianni, Giuseppe Matarese, Paola Matarrese, Roberto Mateo, Satoaki Matoba, Naomichi Matsumoto, Takehiko Matsushita, Akira Matsuura, Takeshi Matsuzawa, Mark P Mattson, Soledad Matu, Norma Maugeri, Caroline Mauvezin, Andreas Mayer, Dusica Maysinger, Guillermo D Mazzolini, Mary Kate McBrayer, Kimberly McCall, Craig McCormick, Gerald M McInerney, Skye C McIver, Sharon McKenna, John J McMahon, Iain A McNeish, Fatima Mechta-Grigoriou, Jan Paul Medema, Diego L Medina, Klara Megyeri, Maryam Mehrpour, Jawahar L Mehta, Yide Mei, Ute-Christiane Meier, Alfred J Meijer, Alicia Meléndez, Gerry Melino, Sonia Melino, Edesio Jose Tenorio de Melo, Maria A Mena, Marc D Meneghini, Javier A Menendez, Regina Meneze, Liesu Meng, Ling-hua Meng, Songshu Meng, Rossella Menghini, A Sue Menko, Rubem FS Menna-Barreto, Manoj B Menon, Marco A Meraz-Río, Giuseppe Merla, Luciano Merlini, Angelica M Merlot, Andreas Meryk, Stefania Meschini, Joel N Meyer, Man-tian Mi, Chao-Yu Miao, Lucia Micale, Simon Michaeli, Carine Michiel, Anna Rita Migliaccio, Anastasia Susie Mihailidou, Dalibor Mijaljica, Katsuhiko Mikoshiba, Enrico Milan, Leonor Miller-Fleming, Gordon B Mill, Ian G Mill, Georgia Minakaki, Berge A Minassian, Xiu-Fen Ming, Farida Minibayeva, Elena A Minina, Justine D Mintern, Saverio Minucci, Antonio Miranda-Vizuete, Claire H Mitchell, Shigeki Miyamoto, Keisuke Miyazawa, Noboru Mizushima, Katarzyna Mnich, Baharia Mograbi, Simin Mohseni, Luis Ferreira Moita, Marco Molinari, Maurizio Molinari, Andreas Buch Møller, Bertrand Mollereau, Faustino Mollinedo, Marco Mongillo, Martha M Monick, Serena Montagnaro, Craig Montell, Darren J Moore, Michael N Moore, Rodrigo Mora-Rodriguez, Paula I Moreira, Etienne Morel, Maria Beatrice Morelli, Sandra Moreno, Michael J Morgan, Arnaud Mori, Yuji Moriyasu, Janna L Morrison, Lynda A Morrison, Eugenia Morselli, Jorge Moscat, Pope L Moseley, Serge Mostowy, Elisa Motori, Denis Mottet, Jeremy C Mottram, Charbel E-H Moussa, Vassiliki E Mpakou, Hasan Mukhtar, Jean M Mulcahy Levy, Sylviane Muller, Raquel Muñoz-Moreno, Cristina Muñoz-Pinedo, Christian Münz, Maureen E Murphy, James T Murray, Aditya Murthy, Indira U Mysorekar, Ivan R Nabi, Massimo Nabissi, Gustavo A Nader, Yukitoshi Nagahara, Yoshitaka Nagai, Kazuhiro Nagata, Anika Nagelkerke, Péter Nagy, Samisubbu R Naidu, Sreejayan Nair, Hiroyasu Nakano, Hitoshi Nakatogawa, Meera Nanjundan, Gennaro Napolitano, Naweed I Naqvi, Roberta Nardacci, Derek P Narendra, Masashi Narita, Anna Chiara Nascimbeni, Ramesh Natarajan, Luiz C Navegante, Steffan T Nawrocki, Taras Y Nazarko, Volodymyr Y Nazarko, Thomas Neill, Luca M Neri, Mihai G Netea, Romana T Netea-Maier, Bruno M Neve, Paul A Ney, Ioannis P Nezi, Hang TT Nguyen, Huu Phuc Nguyen, Anne-Sophie Nicot, Hilde Nilsen, Per Nilsson, Mikio Nishimura, Ichizo Nishino, Mireia Niso-Santano, Hua Niu, Ralph A Nixon, Vincent CO Njar, Takeshi Noda, Angelika A Noegel, Elsie Magdalena Nolte, Erik Norberg, Koenraad K Norga, Sakineh Kazemi Noureini, Shoji Notomi, Lucia Notterpek, Karin Nowikovsky, Nobuyuki Nukina, Thorsten Nürnberger, Valerie B O'Donnell, Tracey O'Donovan, Peter J O'Dwyer, Ina Oehme, Clara L Oeste, Michinaga Ogawa, Besim Ogretmen, Yuji Ogura, Young J Oh, Masaki Ohmuraya, Takayuki Ohshima, Rani Ojha, Koji Okamoto, Toshiro Okazaki, F Javier Oliver, Karin Ollinger, Stefan Olsson, Daniel P Orban, Paulina Ordonez, Idil Orhon, Laszlo Orosz, Eyleen J O'Rourke, Helena Orozco, Angel L Ortega, Elena Ortona, Laura D Osellame, Junko Oshima, Shigeru Oshima, Heinz D Osiewacz, Takanobu Otomo, Kinya Otsu, Jing-hsiung James Ou, Tiago F Outeiro, Dong-yun Ouyang, Hongjiao Ouyang, Michael Overholtzer, Michelle A Ozbun, P Hande Ozdinler, Bulent Ozpolat, Consiglia Pacelli, Paolo Paganetti, Guylène Page, Gilles Page, Ugo Pagnini, Beata Pajak, Stephen C Pak, Karolina Pakos-Zebrucka, Nazzy Pakpour, Zdena Palková, Francesca Palladino, Kathrin Pallauf, Nicolas Pallet, Marta Palmieri, Søren R Paludan, Camilla Palumbo, Silvia Palumbo, Olatz Pampliega, Hongming Pan, Wei Pan, Theocharis Panaretaki, Aseem Pandey, Areti Pantazopoulou, Zuzana Papackova, Daniela L Papademetrio, Issidora Papassideri, Alessio Papini, Nirmala Parajuli, Julian Pardo, Vrajesh V Parekh, Giancarlo Parenti, Jong-In Park, Junsoo Park, Ohkmae K Park, Roy Parker, Rosanna Parlato, Jan B Pary, Katherine R Parzych, Jean-Max Pasquet, Benoit Pasquier, Kishore BS Pasumarthi, Daniel Patschan, Cam Patterson, Sophie Pattingre, Scott Pattison, Arnim Pause, Hermann Pavenstädt, Flaminia Pavone, Zully Pedrozo, Fernando J Peña, Miguel A Peñalva, Mario Pende, Jianxin Peng, Fabio Penna, Josef M Penninger, Anna Pensalfini, Salvatore Pepe, Gustavo JS Pereira, Paulo C Pereira, Verónica Pérez-de la Cruz, María Esther Pérez-Pérez, Diego Pérez-Rodríguez, Dolores Pérez-Sala, Celine Perier, Andras Perl, David H Perlmutter, Ida Perrotta, Shazib Pervaiz, Maija Pesonen, Jeffrey E Pessin, Godefridus J Peter, Morten Petersen, Irina Petrache, Basil J Petrof, Goran Petrovski, James M Phang, Mauro Piacentini, Marina Pierdominici, Philippe Pierre, Valérie Pierrefite-Carle, Federico Pietrocola, Felipe X Pimentel-Muiño, Mario Pinar, Benjamin Pineda, Ronit Pinkas-Kramarski, Marcello Pinti, Paolo Pinton, Bilal Piperdi, James M Piret, Leonidas C Platania, Harald W Platta, Edward D Plowey, Stefanie Pöggeler, Marc Poirot, Peter Polčic, Angelo Poletti, Audrey H Poon, Hana Popelka, Blagovesta Popova, Izabela Poprawa, Shibu M Poulose, Joanna Poulton, Scott K Power, Ted Power, Mercedes Pozuelo- Rubio, Krisna Prak, Reinhild Prange, Mark Prescott, Muriel Priault, Sharon Prince, Richard L Proia, Tassula Proikas-Cezanne, Holger Prokisch, Vasilis J Prompona, Karin Przyklenk, Rosa Puertollano, Subbiah Pugazhenthi, Luigi Puglielli, Aurora Pujol, Julien Puyal, Dohun Pyeon, Xin Qi, Wen-bin Qian, Zheng-Hong Qin, Yu Qiu, Ziwei Qu, Joe Quadrilatero, Frederick Quinn, Nina Raben, Hannah Rabinowich, Flavia Radogna, Michael J Ragusa, Mohamed Rahmani, Komal Raina, Sasanka Ramanadham, Rajagopal Ramesh, Abdelhaq Rami, Sarron Randall- Demllo, Felix Randow, Hai Rao, V Ashutosh Rao, Blake B Rasmussen, Tobias M Rasse, Edward A Ratovitski, Pierre-Emmanuel Rautou, Swapan K Ray, Babak Razani, Bruce H Reed, Fulvio Reggiori, Markus Rehm, Andreas S Reichert, Theo Rein, David J Reiner, Eric Reit, Jun Ren, Xingcong Ren, Maurizio Renna, Jane EB Reusch, Jose L Revuelta, Leticia Reye, Alireza R Rezaie, Robert I Richard, Des R Richardson, Clémence Richetta, Michael A Riehle, Bertrand H Rihn, Yasuko Rikihisa, Brigit E Riley, Gerald Rimbach, Maria Rita Rippo, Konstantinos Riti, Federica Rizzi, Elizete Rizzo, Peter J Roach, Jeffrey Robbin, Michel Roberge, Gabriela Roca, Maria Carmela Roccheri, Sonia Rocha, Cecilia MP Rodrigue, Clara I Rodríguez, Santiago Rodriguez de Cordoba, Natalia Rodriguez-Muela, Jeroen Roelof, Vladimir V Rogov, Troy T Rohn, Bärbel Rohrer, Davide Romanelli, Luigina Romani, Patricia Silvia Romano, M Isabel G Roncero, Jose Luis Rosa, Alicia Rosello, Kirill V Rosen, Philip Rosenstiel, Magdalena Rost-Roszkowska, Kevin A Roth, Gael Roué, Mustapha Roui, Kasper M Rouschop, Daniel T Ruan, Diego Ruano, David C Rubinsztein, Edmund B Rucker III, Assaf Rudich, Emil Rudolf, Ruediger Rudolf, Markus A Ruegg, Carmen Ruiz-Roldan, Avnika Ashok Ruparelia, Paola Rusmini, David W Ru, Gian Luigi Russo, Giuseppe Russo, Rossella Russo, Tor Erik Rusten, Victoria Ryabovol, Kevin M Ryan, Stefan W Ryter, David M Sabatini, Michael Sacher, Carsten Sachse, Michael N Sack, Junichi Sadoshima, Paul Saftig, Ronit Sagi-Eisenberg, Sumit Sahni, Pothana Saikumar, Tsunenori Saito, Tatsuya Saitoh, Koichi Sakakura, Machiko Sakoh-Nakatogawa, Yasuhito Sakuraba, María Salazar-Roa, Paolo Salomoni, Ashok K Saluja, Paul M Salvaterra, Rosa Salvioli, Afshin Samali, Anthony MJ Sanchez, José A Sánchez-Alcázar, Ricardo Sanchez-Prieto, Marco Sandri, Miguel A Sanjuan, Stefano Santaguida, Laura Santambrogio, Giorgio Santoni, Claudia Nunes dos Santo, Shweta Saran, Marco Sardiello, Graeme Sargent, Pallabi Sarkar, Sovan Sarkar, Maria Rosa Sarria, Minnie M Sarwal, Chihiro Sasakawa, Motoko Sasaki, Miklos Sa, Ken Sato, Miyuki Sato, Joseph Satriano, Niramol Savaraj, Svetlana Saveljeva, Liliana Schaefer, Ulrich E Schaible, Michael Scharl, Hermann M Schatzl, Randy Schekman, Wiep Scheper, Alfonso Schiavi, Hyman M Schipper, Hana Schmeisser, Jens Schmidt, Ingo Schmitz, Bianca E Schneider, E Marion Schneider, Jaime L Schneider, Eric A Schon, Miriam J Schönenberger, Axel H Schönthal, Daniel F Schorderet, Bernd Schröder, Sebastian Schuck, Ryan J Schulze, Melanie Schwarten, Thomas L Schwarz, Sebastiano Sciarretta, Kathleen Scotto, A Ivana Scovassi, Robert A Screaton, Mark Screen, Hugo Seca, Simon Sedej, Laura Segatori, Nava Segev, Per O Seglen, Jose M Seguí- Simarro, Juan Segura-Aguilar, Ekihiro Seki, Iban Seiliez, Christian Sell, Clay F Semenkovich, Gregg L Semenza, Utpal Sen, Andreas L Serra, Ana Serrano-Puebla, Hiromi Sesaki, Takao Setoguchi, Carmine Settembre, John J Shacka, Ayesha N Shajahan-Haq, Irving M Shapiro, Shweta Sharma, Hua She, C-K James Shen, Chiung-Chyi Shen, Han-Ming Shen, Sanbing Shen, Weili Shen, Rui Sheng, Xianyong Sheng, Zu-Hang Sheng, Trevor G Shepherd, Junyan Shi, Qiang Shi, Qinghua Shi, Yuguang Shi, Shusaku Shibutani, Kenichi Shibuya, Yoshihiro Shidoji, Jeng- Jer Shieh, Chwen-Ming Shih, Yohta Shimada, Shigeomi Shimizu, Dong Wook Shin, Mari L Shinohara, Michiko Shintani, Takahiro Shintani, Tetsuo Shioi, Ken Shirabe, Ronit Shiri-Sverdlov, Orian Shirihai, Gordon C Shore, Chih-Wen Shu, Deepak Shukla, Andriy A Sibirny, Valentina Sica, Christina J Sigurdson, Einar M Sigurdsson, Puran Singh Sijwali, Beata Sikorska, Wilian A Silveira, Sandrine Silvente-Poirot, Gary A Silverman, Jan Simak, Thomas Simmet, Anna Katharina Simon, Hans-Uwe Simon, Cristiano Simone, Matias Simon, Anne Simonsen, Rajat Singh, Shivendra V Singh, Shrawan K Singh, Debasish Sinha, Sangita Sinha, Frank A Sinicrope, Agnieszka Sirko, Kapil Sirohi, Balindiwe JN Sishi, Annie Sittler, Parco M Siu, Efthimios Sivridi, Anna Skwarska, Ruth Slack, Iva Slaninová, Nikolai Slavov, Soraya S Smaili, Keiran SM Smalley, Duncan R Smith, Stefaan J Soenen, Scott A Soleimanpour, Anita Solhaug, Kumaravel Somasundaram, Jin H Son, Avinash Sonawane, Chunjuan Song, Fuyong Song, Hyun Kyu Song, Ju-Xian Song, Wei Song, Kai Y Soo, Anil K Sood, Tuck Wah Soong, Virawudh Soontornniyomkij, Maurizio Sorice, Federica Sotgia, David R Soto-Pantoja, Areechun Sotthibundhu, Maria João Sousa, Herman P Spaink, Paul N Span, Anne Spang, Janet D Spark, Peter G Speck, Stephen A Spector, Claudia D Spie, Wolfdieter Springer, Daret St Clair, Alessandra Stacchiotti, Bart Stael, Michael T Stang, Daniel T Starczynowski, Petro Starokadomskyy, Clemens Steegborn, John W Steele, Leonidas Stefani, Joan Steffan, Christine M Stellrecht, Harald Stenmark, Tomasz M Stepkowski, Stęphan T Stern, Craig Steven, Brent R Stockwell, Veronika Stoka, Zuzana Storchova, Björn Stork, Vassilis Stratoulia, Dimitrios J Stravopodi, Pavel Strnad, Anne Marie Strohecker, Anna- Lena Ström, Per Stromhaug, Jiri Stulik, Yu-Xiong Su, Zhaoliang Su, Carlos S Subauste, Srinivasa Subramaniam, Carolyn M Sue, Sang Won Suh, Xinbing Sui, Supawadee Sukseree, David Sulzer, Fang-Lin Sun, Jiaren Sun, Jun Sun, Shi-Yong Sun, Yang Sun, Yi Sun, Yingjie Sun, Vinod Sundaramoorthy, Joseph Sung, Hidekazu Suzuki, Kuninori Suzuki, Naoki Suzuki, Tadashi Suzuki, Yuichiro J Suzuki, Michele S Swanson, Charles Swanton, Karl Swärd, Ghanshyam Swarup, Sean T Sweeney, Paul W Sylvester, Zsuzsanna Szatmari, Eva Szegezdi, Peter W Szlosarek, Heinrich Taegtmeyer, Marco Tafani, Emmanuel Taillebourg, Stephen WG Tait, Krisztina Takacs-Vellai, Yoshinori Takahashi, Szabolcs Takát, Genzou Takemura, Nagio Takigawa, Nicholas J Talbot, Elena Tamagno, Jerome Tamburini, Cai-Ping Tan, Lan Tan, Mei Lan Tan, Ming Tan, Yee-Joo Tan, Keiji Tanaka, Masaki Tanaka, Daolin Tang, Dingzhong Tang, Guomei Tang, Isei Tanida, Kunikazu Tanji, Bakhos A Tannou, Jose A Tapia, Inmaculada Tasset-Cueva, Marc Tatar, Iman Tavassoly, Nektarios Tavernaraki, Allen Taylor, Graham S Taylor, Gregory A Taylor, J Paul Taylor, Mark J Taylor, Elena V Tchetina, Andrew R Tee, Fatima Teixeira-Clerc, Sucheta Telang, Tewin Tencomnao, Ba-Bie Teng, Ru-Jeng Teng, Faraj Terro, Gianluca Tettamanti, Arianne L Thei, Anne E Theron, Kelly Jean Thoma, Marcos P Thomé, Paul G Thome, Andrew Thorburn, Jeremy Thorner, Thomas Thum, Michael Thumm, Teresa LM Thurston, Ling Tian, Andreas Till, Jenny Pan-yun Ting, Vladimir I Titorenko, Lilach Toker, Stefano Toldo, Sharon A Tooze, Ivan Topisirovic, Maria Lyngaas Torgersen, Liliana Torosantucci, Alicia Torriglia, Maria Rosaria Torrisi, Cathy Tournier, Roberto Town, Vladimir Trajkovic, Leonardo H Travasso, Gemma Triola, Durga Nand Tripathi, Daniela Trisciuoglio, Rodrigo Troncoso, Ioannis P Trougako, Anita C Truttmann, Kuen-Jer Tsai, Mario P Tschan, Yi-Hsin Tseng, Takayuki Tsukuba, Allan Tsung, Andrey S Tsvetkov, Shuiping Tu, Hsing-Yu Tuan, Marco Tucci, David A Tumbarello, Boris Turk, Vito Turk, Robin FB Turner, Anders A Tveita, Suresh C Tyagi, Makoto Ubukata, Yasuo Uchiyama, Andrej Udelnow, Takashi Ueno, Midori Umekawa, Rika Umemiya-Shirafuji, Benjamin R Underwood, Christian Ungermann, Rodrigo P. Ureshino, Ryo Ushioda, Vladimir N Uversky, Néstor L Uzcátegui, Thomas Vaccari, Maria I Vaccaro, Libuše Váchová, Helin Vakifahmetoglu-Norberg, Rut Valdor, Enza Maria Valente, Francois Vallette, Angela M Valverde, Greet Van den Berghe, Ludo Van Den Bosch, Gijs R van den Brink, F Gisou van der Goot, Ida J van der Klei, Luc JW van der Laan, Wouter G van Doorn, Marjolein van Egmond, Kenneth L van Golen, Luc Van Kaer, Menno van Lookeren Campagne, Peter Vandenabeele, Wim Vandenberghe, Ilse Vanhorebeek, Isabel Varela-Nieto, M Helena Vasconcelo, Radovan Vasko, Demetrios G Vavva, Ignacio Vega- Naredo, Guillermo Velasco, Athanassios D Velentza, Panagiotis D Velentza, Tibor Vellai, Edo Vellenga, Mikkel Holm Vendelbo, Kartik Venkatachalam, Natascia Ventura, Salvador Ventura, Patrícia ST Vera, Mireille Verdier, Beata G Vertessy, Andrea Viale, Michel Vidal, Helena LA Vieira, Richard D Vierstra, Nadarajah Vigneswaran, Neeraj Vij, Miquel Vila, Margarita Villar, Victor H Villar, Joan Villarroya, Cécile Vindi, Giampietro Viola, Maria Teresa Viscomi, Giovanni Vitale, Dan T Vogl, Olga V Voitsekhovskaja, Clarissa von Haefen, Karin von Schwarzenberg, Daniel E Voth, Valérie Vouret-Craviari, Kristina Vuori, Jatin M Vya, Christian Waeber, Cheryl Lyn Walker, Mark J Walker, Jochen Walter, Lei Wan, Xiangbo Wan, Bo Wang, Caihong Wang, Chao-Yung Wang, Chengshu Wang, Chenran Wang, Chuangui Wang, Dong Wang, Fen Wang, Fuxin Wang, Guanghui Wang, Hai-jie Wang, Haichao Wang, Hong-Gang Wang, Hongmin Wang, Horng-Dar Wang, Jing Wang, Junjun Wang, Mei Wang, Mei-Qing Wang, Pei-Yu Wang, Peng Wang, Richard C Wang, Shuo Wang, Ting-Fang Wang, Xian Wang, Xiao-jia Wang, Xiao-Wei Wang, Xin Wang, Xuejun Wang, Yan Wang, Yanming Wang, Ying Wang, Ying-Jan Wang, Yipeng Wang, Yu Wang, Yu Tian Wang, Yuqing Wang, Zhi-Nong Wang, Pablo Wappner, Carl Ward, Diane McVey Ward, Gary Warne, Hirotaka Watada, Yoshihisa Watanabe, Kei Watase, Timothy E Full Terms & Conditions of access and use can be found at http://www.tandfonline.com/action/journalInformation?journalCode=kaup20 Download by: [Alma Mater Studiorum - Università di Bologna] Date: 23 September 2016, At: 06:43 Weaver, Colin D Weeke, Jiwu Wei, Thomas Weide, Conrad C Weihl, Günther Weindl, Simone Nardin Wei, Longping Wen, Xin Wen, Yunfei Wen, Benedikt Westermann, Cornelia M Weyand, Anthony R White, Eileen White, J Lindsay Whitton, Alexander J Whitworth, Joëlle Wiel, Franziska Wild, Manon E Wildenberg, Tom Wileman, Deepti Srinivas Wilkinson, Simon Wilkinson, Dieter Willbold, Chris William, Katherine William, Peter R Williamson, Konstanze F Winklhofer, Steven S Witkin, Stephanie E Wohlgemuth, Thomas Wollert, Ernst J Wolvetang, Esther Wong, G William Wong, Richard W Wong, Vincent Kam Wai Wong, Elizabeth A Woodcock, Karen L Wright, Chunlai Wu, Defeng Wu, Gen Sheng Wu, Jian Wu, Junfang Wu, Mian Wu, Min Wu, Shengzhou Wu, William KK Wu, Yaohua Wu, Zhenlong Wu, Cristina PR Xavier, Ramnik J Xavier, Gui-Xian Xia, Tian Xia, Weiliang Xia, Yong Xia, Hengyi Xiao, Jian Xiao, Shi Xiao, Wuhan Xiao, Chuan-Ming Xie, Zhiping Xie, Zhonglin Xie, Maria Xilouri, Yuyan Xiong, Chuanshan Xu, Congfeng Xu, Feng Xu, Haoxing Xu, Hongwei Xu, Jian Xu, Jianzhen Xu, Jinxian Xu, Liang Xu, Xiaolei Xu, Yangqing Xu, Ye Xu, Zhi-Xiang Xu, Ziheng Xu, Yu Xue, Takahiro Yamada, Ai Yamamoto, Koji Yamanaka, Shunhei Yamashina, Shigeko Yamashiro, Bing Yan, Bo Yan, Xianghua Yan, Zhen Yan, Yasuo Yanagi, Dun-Sheng Yang, Jin-Ming Yang, Liu Yang, Minghua Yang, Pei-Ming Yang, Peixin Yang, Qian Yang, Wannian Yang, Wei Yuan Yang, Xuesong Yang, Yi Yang, Ying Yang, Zhifen Yang, Zhihong Yang, Meng-Chao Yao, Pamela J Yao, Xiaofeng Yao, Zhenyu Yao, Zhiyuan Yao, Linda S Yasui, Mingxiang Ye, Barry Yedvobnick, Behzad Yeganeh, Elizabeth S Yeh, Patricia L Yeyati, Fan Yi, Long Yi, Xiao-Ming Yin, Calvin K Yip, Yeong-Min Yoo, Young Hyun Yoo, Seung-Yong Yoon, Ken-Ichi Yoshida, Tamotsu Yoshimori, Ken H Young, Huixin Yu, Jane J Yu, Jin-Tai Yu, Jun Yu, Li Yu, W Haung Yu, Xiao-Fang Yu, Zhengping Yu, Junying Yuan, Zhi-Min Yuan, Beatrice YJT Yue, Jianbo Yue, Zhenyu Yue, David N Zack, Eldad Zacksenhau, Nadia Zaffaroni, Tania Zaglia, Zahra Zakeri, Vincent Zecchini, Jinsheng Zeng, Min Zeng, Qi Zeng, Antonis S Zervo, Donna D Zhang, Fan Zhang, Guo Zhang, Guo-Chang Zhang, Hao Zhang, Hong Zhang, Hongbing Zhang, Jian Zhang, Jiangwei Zhang, Jianhua Zhang, Jing-pu Zhang, Li Zhang, Lin Zhang, Long Zhang, Ming-Yong Zhang, Xiangnan Zhang, Xu Dong Zhang, Yan Zhang, Yang Zhang, Yanjin Zhang, Yingmei Zhang, Yunjiao Zhang, Mei Zhao, Wei-Li Zhao, Xiaonan Zhao, Yan G Zhao, Ying Zhao, Yongchao Zhao, Yu-xia Zhao, Zhendong Zhao, Zhizhuang J Zhao, Dexian Zheng, Xi-Long Zheng, Xiaoxiang Zheng, Boris Zhivotovsky, Qing Zhong, Guang-Zhou Zhou, Guofei Zhou, Huiping Zhou, Shu-Feng Zhou, Xu-jie Zhou, Hongxin Zhu, Hua Zhu, Wei- Guo Zhu, Wenhua Zhu, Xiao-Feng Zhu, Yuhua Zhu, Shi-Mei Zhuang, Xiaohong Zhuang, Elio Ziparo, Christos E Zoi, Teresa Zoladek, Wei-Xing Zong, and Antonio Zorzano & Susu M Zughaier
Subjects: [SDV]Life Sciences [q-bio], autophagosome, Review Article, ddc:616.07, stress, stre, LC3, MESH: Animals, Settore MED/49 - Scienze Tecniche Dietetiche Applicate, Settore BIO/06 - Anatomia Comparata E Citologia, chaperone-mediated autophagy, ComputingMilieux_MISCELLANEOUS, Settore BIO/11, Pharmacology. Therapy, Settore BIO/13, standards [Biological Assay], autolysosome, MESH: Autophagy*/physiology, lysosome, methods [Biological Assay], Biological Assay, Settore BIO/17 - ISTOLOGIA, Erratum, Human, Biochemistry & Molecular Biology, Settore BIO/06, physiology [Autophagy], Chaperonemediated autophagy, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, NO, autophagy, guidelines, molecular biology, ultrastructure, flux, macroautophagy, phagophore, vacuole, MESH: Biological Assay/methods, MESH: Computer Simulation, ddc:570, Autolysosome, Autophagosome, Chaperonemediated autophagy, Flux, LC3, Lysosome, Macroautophagy, Phagophore, Stress, Vacuole, Autophagy, Animals, Humans, Computer Simulation, Settore BIO/10, ddc:612, Biology, MESH: Humans, Animal, 0601 Biochemistry And Cell Biology, MESH: Biological Assay/standards, Human medicine
Abstract: Seuls les 100 premiers auteurs dont les auteurs INRA ont été entrés dans la notice. La liste complète des auteurs et de leurs affiliations est accessible sur la publication.; International audience; In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes.For example, a key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process versus those that measure flux through the autophagy pathway (i.e., the complete process including the amount and rate of cargo sequestered and degraded). In particular, a block in macroautophagy that results in autophagosome accumulation must be differentiated from stimuli that increase autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. It is worth emphasizing here that lysosomal digestion is a stage of autophagy and evaluating its competence is a crucial part of the evaluation of autophagic flux, or complete autophagy.Here, we present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes. These guidelines are not meant to be a formulaic set of rules, because the appropriate assays depend in part on the question being asked and the system being used. In addition, we emphasize that no individual assay is guaranteed to be the most appropriate one in every situation, and we strongly recommend the use of multiple assays to monitor autophagy. Along these lines, because of the potential for pleiotropic effects due to blocking autophagy through genetic manipulation, it is imperative to target by gene knockout or RNA interference more than one autophagy-related protein. In addition, some individual Atg proteins, or groups of proteins, are involved in other cellular pathways implying that not all Atg proteins can be used as a specific marker for an autophagic process. In these guidelines, we consider these various methods of assessing autophagy and what information can, or cannot, be obtained from them. Finally, by discussing the merits and limits of particular assays, we hope to encourage technical innovation in the field.
Published: 2016

27. Phytosphingosine degradation pathway includes fatty acid α-oxidation reactions in the endoplasmic reticulum

Author: Akio Kihara, Naoya Seki, and Takuya Kitamura
Subjects: 0301 basic medicine, Stereochemistry, Aldehyde dehydrogenase, CHO Cells, Endoplasmic Reticulum, Palmitic acid, 03 medical and health sciences, chemistry.chemical_compound, Cricetulus, Sphingosine, Alpha oxidation, Animals, Humans, chemistry.chemical_classification, Multidisciplinary, biology, Endoplasmic reticulum, Fatty acid, Metabolism, Peroxisome, Lyase, Aldehyde Oxidoreductases, HEK293 Cells, 030104 developmental biology, PNAS Plus, chemistry, Biochemistry, Proteolysis, biology.protein, Oxidation-Reduction, Metabolic Networks and Pathways, HeLa Cells
Abstract: Although normal fatty acids (FAs) are degraded via β-oxidation, unusual FAs such as 2-hydroxy (2-OH) FAs and 3-methyl-branched FAs are degraded via α-oxidation. Phytosphingosine (PHS) is one of the long-chain bases (the sphingolipid components) and exists in specific tissues, including the epidermis and small intestine in mammals. In the degradation pathway, PHS is converted to 2-OH palmitic acid and then to pentadecanoic acid (C15:0-COOH) via FA α-oxidation. However, the detailed reactions and genes involved in the α-oxidation reactions of the PHS degradation pathway have yet to be determined. In the present study, we reveal the entire PHS degradation pathway: PHS is converted to C15:0-COOH via six reactions [phosphorylation, cleavage, oxidation, CoA addition, cleavage (C1 removal), and oxidation], in which the last three reactions correspond to the α-oxidation. The aldehyde dehydrogenase ALDH3A2 catalyzes both the first and second oxidation reactions (fatty aldehydes to FAs). In Aldh3a2-deficient cells, the unmetabolized fatty aldehydes are reduced to fatty alcohols and are incorporated into ether-linked glycerolipids. We also identify HACL2 (2-hydroxyacyl-CoA lyase 2) [previous name, ILVBL; ilvB (bacterial acetolactate synthase)-like] as the major 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the FA α-oxidation of the PHS degradation pathway. HACL2 is localized in the endoplasmic reticulum. Thus, in addition to the already-known FA α-oxidation in the peroxisomes, we have revealed the existence of FA α-oxidation in the endoplasmic reticulum in mammals.
Published: 2017

28. Sphingosine 1-phosphate is a key metabolite linking sphingolipids to glycerophospholipids

Author: Akio Kihara
Subjects: Sphingolipids, Sphingosine, Lipid metabolism, Glycerophospholipids, Cell Biology, Lipid signaling, Biology, Sphingolipid, Cell biology, chemistry.chemical_compound, Metabolic pathway, chemistry, Biochemistry, Extracellular, Animals, Humans, lipids (amino acids, peptides, and proteins), Sphingosine-1-phosphate, Lysophospholipids, Molecular Biology, Metabolic Networks and Pathways, Intracellular
Abstract: The sphingolipid metabolite sphingosine 1-phosphate (S1P) is a well-known lipid mediator. As a lipid mediator, S1P must be present in extracellular space and bind to its cell surface receptors (S1P1–5). However, most S1P, synthesized intracellularly, is metabolized without being released into extracellular space, in other words, without functioning as a lipid mediator in the vast majority of cells except those supplying plasma and lymph S1P such as blood cells and endothelial cells. Instead, intracellular S1P plays an important role as an intermediate of the sole sphingolipid-to-glycerophospholipid metabolic pathway. The degradation of S1P by S1P lyase is the first irreversible reaction (committed step) of this pathway. This metabolic pathway is conserved in eukaryotes from yeast to human, indicating its much older origin than the function of S1P as a lipid mediator, which is found to be present only in vertebrates and chordates. The sphingolipid-to-glycerophospholipid metabolism takes place ubiquitously in mammalian tissues, and its defect causes an aberration of several tissue functions as well as abnormal lipid metabolism. Although this metabolic pathway has been known for over four decades, only recently the precise reactions and enzymes involved in this pathway have been revealed. This review will focus on the recent advances in our understanding of the sphingolipid metabolic pathway via S1P and its physiological and pathological roles. This article is part of a Special Issue entitled New Frontiers in Sphingolipid Biology.
Published: 2014

29. Lorenzo's oil inhibits ELOVL1 and lowers the level of sphingomyelin with a saturated very long-chain fatty acid

Author: Akio Kihara, Takeshi Wakashima, Yusuke Ohno, and Takayuki Sassa
Subjects: Erucic Acids, Fatty Acid Elongases, Very long chain fatty acid, Immunoblotting, Palmitic Acid, QD415-436, Lorenzo's oil, Biology, Biochemistry, Gene Expression Regulation, Enzymologic, Palmitic acid, chemistry.chemical_compound, Endocrinology, Acetyltransferases, medicine, Humans, peroxisome, Triolein, X-linked adrenoleukodystrophy, Research Articles, chemistry.chemical_classification, sphingolipids, Dose-Response Relationship, Drug, Reverse Transcriptase Polymerase Chain Reaction, elongation of very long-chain fatty acid 1, Fatty Acids, ABCD1, Fatty acid, Cell Biology, medicine.disease, Sphingomyelins, Oleic acid, Drug Combinations, Kinetics, erucic acid, HEK293 Cells, chemistry, oleic acid, Erucic acid, Adrenoleukodystrophy, Stearic Acids, HeLa Cells
Abstract: X-linked adrenoleukodystrophy (X-ALD) is a peroxisomal disorder caused by impaired degradation of very long-chain fatty acids (VLCFAs) due to mutations in the ABCD1 gene responsible for VLCFA transport into peroxisomes. Lorenzo's oil, a 4: 1 mixture of glyceryl trioleate and glyceryl trierucate, has been used to reduce the saturated VLCFA level in the plasma of X-ALD patients; however, the mechanism by which this occurs remains elusive. We report the biochemical characterization of Lorenzo's oil activity toward elongation of very long-chain fatty acid (ELOVL) 1, the primary enzyme responsible for the synthesis of saturated and monounsaturated VLCFAs. Oleic and erucic acids inhibited ELOVL1, and, moreover, their 4:1 mixture (the FA composition of Lorenzo's oil) exhibited the most potent inhibitory activity. The kinetics analysis revealed that this was a mixed (not a competitive) inhibition. At the cellular level, treatment with the 4:1 mixture reduced the level of SM with a saturated VLCFA accompanied by an increased level of SM with a monounsaturated VLCFA, probably due to the incorporation of erucic acid into the FA elongation cycle.(jlr) These results suggest that inhibition of ELOVL1 may be an underlying mechanism by which Lorenzo's oil exerts its action.
Published: 2014

30. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway

Author: Aya Ohkuni, Akio Kihara, and Yusuke Ohno
Subjects: Biophysics, Palmitic Acids, Saccharomyces cerevisiae, Endoplasmic Reticulum, Biochemistry, Sphingolipid, chemistry.chemical_compound, Sphingosine, Coenzyme A Ligases, Humans, Sphingosine-1-phosphate, Molecular Biology, Glyceraldehyde 3-phosphate dehydrogenase, biology, Endoplasmic reticulum, Acyl-CoA synthetase, Cell Biology, Lipid, Yeast, Glycerophospholipid, Cell biology, Triacsin C, Metabolic pathway, chemistry, Sphingosine 1-phosphate, biology.protein, lipids (amino acids, peptides, and proteins), Lysophospholipids, Metabolic Networks and Pathways, HeLa Cells
Abstract: Sphingosine 1-phosphate (SIP) plays important roles both as a bioactive lipid molecule and an intermediate of the sphingolipid-to-glycerophospholipid metabolic pathway. To identify human acyl-CoA synthetases (ACSs) involved in SIP metabolism, we cloned all 26 human ACS genes and examined their abilities to restore deficient sphingolipid-to-glycerophospholipid metabolism in a yeast mutant lacking two ACS genes, FAA1 and FAA4. Here, in addition to the previously identified ACSL family members (ACSL1, 3, 4, 5, and 6), we found that ACSVL1, ACSVL4, and ACSBG1 also restored metabolism. All 8 ACSs were localized either exclusively or partly to the endoplasmic reticulum (ER), where SIP metabolism takes place. We previously proposed the entire SIP metabolic pathway from results obtained using yeast cells, i.e., SIP is metabolized to glycerophospholipids via trans-2-hexadecenal, trans-2-hexadecenoic acid, trans-2-hexadecenoyl-CoA, and palmitoyl-CoA. However, as SIP is not a naturally occurring long-chain base 1-phosphate in yeast, the validity of this pathway required further verification using mammalian cells. In the present study, we treated HeLa cells with the ACS inhibitor triacsin C and found that inhibition of ACSs resulted in accumulation of trans-2-hexadecenoic acid as in ACS mutant yeast. From these results, we conclude that SIP is metabolized by a common pathway in eukaryotes. (C) 2013 Elsevier Inc. All rights reserved.
Published: 2013

31. Mutation for Nonsyndromic Mental Retardation in the trans-2-Enoyl-CoA Reductase TER Gene Involved in Fatty Acid Elongation Impairs the Enzyme Activity and Stability, Leading to Change in Sphingolipid Profile

Author: Yusuke Ohno, Carole Ober, Kensuke Abe, Minal Çalışkan, Takayuki Sassa, Akio Kihara, and Ryo Taguchi
Subjects: Oxidoreductases Acting on CH-CH Group Donors, Saccharomyces cerevisiae Proteins, Mutation, Missense, Saccharomyces cerevisiae, Reductase, Biology, Ceramides, medicine.disease_cause, Biochemistry, Sphingolipid, chemistry.chemical_compound, Enzyme Stability, medicine, Humans, Missense mutation, Fatty Acid Metabolism, Molecular Biology, chemistry.chemical_classification, Mutation, Fatty acid metabolism, Fatty Acids, Homozygote, Membrane, food and beverages, Fatty acid, Cell Biology, Lipids, Molecular biology, Sphingomyelins, Amino acid, HEK293 Cells, chemistry, Mental Retardation, X-Linked, Fatty acid elongation, human activities, Fatty Acid, HeLa Cells
Abstract: Background: The P182L mutation in the trans-2-enoyl-CoA reductase (TER) gene required for very long-chain fatty acid (VLCFA) synthesis causes nonsyndromic mental retardation. Results: This mutation reduces the activity and stability of the TER enzyme. Conclusion: The impaired TER function affects VLCFA synthesis and thereby alters the cellular sphingolipid profile. Significance: Maintenance of a proper VLCFA level may be important for neural function. Very long-chain fatty acids (VLCFAs, chain length >C20) exist in tissues throughout the body and are synthesized by repetition of the fatty acid (FA) elongation cycle composed of four successive enzymatic reactions. In mammals, the TER gene is the only gene encoding trans-2-enoyl-CoA reductase, which catalyzes the fourth reaction in the FA elongation cycle. The TER P182L mutation is the pathogenic mutation for nonsyndromic mental retardation. This mutation substitutes a leucine for a proline residue at amino acid 182 in the TER enzyme. Currently, the mechanism by which the TER P182L mutation causes nonsyndromic mental retardation is unknown. To understand the effect of this mutation on the TER enzyme and VLCFA synthesis, we have biochemically characterized the TER P182L mutant enzyme using yeast and mammalian cells transfected with the TER P182L mutant gene and analyzed the FA elongation cycle in the B-lymphoblastoid cell line with the homozygous TER P182L mutation (TERP182L/P182L B-lymphoblastoid cell line). We have found that TER P182L mutant enzyme exhibits reduced trans-2-enoyl-CoA reductase activity and protein stability, thereby impairing VLCFA synthesis and, in turn, altering the sphingolipid profile (i.e. decreased level of C24 sphingomyelin and C24 ceramide) in the TERP182L/P182L B-lymphoblastoid cell line. We have also found that in addition to the TER enzyme-catalyzed fourth reaction, the third reaction in the FA elongation cycle is affected by the TER P182L mutation. These findings provide new insight into the biochemical defects associated with this genetic mutation.
Published: 2013

32. Congenital myopathy is caused by mutation of HACD1

Author: Miriam Regev, Emad Muhammad, Orit Reish, Yusuke Ohno, Todd E. Scheetz, Lilach Benyamini, Yakov Fellig, Ruti Parvari, Val C. Sheffield, Charles Searby, Adam P. DeLuca, and Akio Kihara
Subjects: Adult, Male, Adolescent, Genetic Linkage, Coenzyme A, RNA Stability, Consanguinity, Biology, chemistry.chemical_compound, Muscular Diseases, Genetic linkage, Genetics, medicine, Humans, Exome, Amino Acid Sequence, Child, Molecular Biology, Gene, Genetics (clinical), Exome sequencing, Fatty Acids, Homozygote, High-Throughput Nucleotide Sequencing, Infant, General Medicine, Articles, medicine.disease, Congenital myopathy, Pedigree, chemistry, Dehydratase, Child, Preschool, Mutation (genetic algorithm), Mutation, Female, Protein Tyrosine Phosphatases, Myopathies, Structural, Congenital
Abstract: Congenital myopathies are heterogeneous inherited diseases of muscle characterized by a range of distinctive histologic abnormalities. We have studied a consanguineous family with congenital myopathy. Genome-wide linkage analysis and whole-exome sequencing identified a homozygous non-sense mutation in 3-hydroxyacyl-CoA dehydratase 1 (HACD1) in affected individuals. The mutation results in non-sense mediated decay of the HACD1 mRNA to 31% of control levels in patient muscle and completely abrogates the enzymatic activity of dehydration of 3-hydroxyacyl-CoA, the third step in the elongation of very long-chain fatty acids (VLCFAs). We describe clinical findings correlated with a deleterious mutation in a gene not previously known to be associated with congenital myopathy in humans. We suggest that the mutation in the HACD1 gene causes a reduction in the synthesis of VLCFAs, which are components of membrane lipids and participants in physiological processes, leading to congenital myopathy. These data indicate that HACD1 is necessary for muscle function.
Published: 2013

33. Substrate specificity, plasma membrane localization, and lipid modification of the aldehyde dehydrogenase ALDH3B1

Author: Akio Kihara, Tatsuro Naganuma, Kanae Nakahara, Kensuke Abe, Takuya Kitamura, and Yusuke Ohno
Subjects: Aldehyde, Lipoylation, Aldehyde dehydrogenase, Lipid-anchored protein, Endoplasmic Reticulum, Sphingolipid, Substrate Specificity, Palmitoylation, Prenylation, Humans, Molecular Biology, chemistry.chemical_classification, Aldehydes, Sphingolipids, biology, Endoplasmic reticulum, Cell Membrane, Cell Biology, Lipid Metabolism, Aldehyde Oxidoreductases, HEK293 Cells, Biochemistry, chemistry, Gene Knockdown Techniques, biology.protein, lipids (amino acids, peptides, and proteins), Lipid modification, HeLa Cells, Plasma membrane
Abstract: The accumulation of reactive aldehydes is implicated in the development of several disorders. Aldehyde dehydrogenases (ALDHs) detoxify aldehydes by oxidizing them to the corresponding carboxylic acids. Among the 19 human ALDHs, ALDH3A2 is the only known ALDH that catalyzes the oxidation of long-chain fatty aldehydes including C16 aldehydes (hexadecanal and trans-2-hexadecenal) generated through sphingolipid metabolism. In the present study, we have identified that ALDH3B1 is also active in vitro toward C16 aldehydes and demonstrated that overexpression of ALDH3B1 restores the sphingolipid metabolism in the ALDH3A2-deficient cells. In addition, we have determined that ALDH3B1 is localized in the plasma membrane through its C-terminal dual lipidation (palmitoylation and prenylation) and shown that the prenylation is required particularly for the activity toward hexadecanal. Since knockdown of ALDH3B1 does not cause further impairment of the sphingolipid metabolism in the ALDH3A2-deficient cells, the likely physiological function of ALDH3B1 is to oxidize lipid-derived aldehydes generated in the plasma membrane and not to be involved in the sphingolipid metabolism in the endoplasmic reticulum. (C) 2013 Elsevier B.V. All rights reserved.
Published: 2013

34. Mechanistic Details of Early Steps in Coenzyme Q Biosynthesis Pathway in Yeast

Author: Fabien Pierrel, Akio Kihara, Mélanie Leroux, Ludovic Pelosi, Laurie Anne Payet, John C. Willison, Techniques de l'Ingénierie Médicale et de la Complexité - Informatique, Mathématiques et Applications, Grenoble - UMR 5525 (TIMC-IMAG), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Faculty of Pharmaceutical Sciences, Hokkaido University [Sapporo, Japan], and Fondation pour la Recherche Médicale (FRM), grant number «DPM20121125553»
Subjects: 0301 basic medicine, Saccharomyces cerevisiae Proteins, Ubiquinone, Clinical Biochemistry, Saccharomyces cerevisiae, Aldehyde dehydrogenase, Parabens, Biology, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, Biosynthesis, Gene Expression Regulation, Fungal, Drug Discovery, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Tyrosine, Molecular Biology, Gene, Pharmacology, chemistry.chemical_classification, 030102 biochemistry & molecular biology, Aldehyde Dehydrogenase, biology.organism_classification, Yeast, Biosynthetic Pathways, 030104 developmental biology, Enzyme, chemistry, Coenzyme Q – cytochrome c reductase, Benzaldehydes, biology.protein, Molecular Medicine, Oxidation-Reduction, Gene Deletion
Abstract: International audience; Coenzyme Q (Q) is a redox lipid that is central for the energetic metabolism of eukaryotes. The biosynthesis of Q from the aromatic precursor 4-hydroxybenzoic acid (4-HB) is understood fairly well. However, biosynthetic details of how 4-HB is produced from tyrosine remain elusive. Here, we provide key insights into this long-standing biosynthetic problem by uncovering molecular details of the first and last reactions of the pathway in the yeast Saccharomyces cerevisiae, namely the deamination of tyrosine to 4-hydroxyphenylpyruvate by Aro8 and Aro9, and the oxidation of 4-hydroxybenzaldehyde to 4-HB by Hfd1. Inactivation of the HFD1 gene in yeast resulted in Q deficiency, which was rescued by the human enzyme ALDH3A1. This suggests that a similar pathway operates in animals, including humans, and led us to propose that patients with genetically unassigned Q deficiency should be screened for mutations in aldehyde dehydrogenase genes, especially ALDH3A1.
Published: 2016

35. Synthesis and degradation pathways, functions, and pathology of ceramides and epidermal acylceramides

Author: Akio Kihara
Subjects: 0301 basic medicine, Ceramide, Pathology, medicine.medical_specialty, Serine C-Palmitoyltransferase, Glycerophospholipids, Biology, Ceramides, Biochemistry, Dermatitis, Atopic, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Acetyltransferases, Sphingosine N-Acyltransferase, Sphingosine N-acyltransferase, medicine, Animals, Humans, Sphingosine, Epidermis (botany), Serine C-palmitoyltransferase, Fatty Acids, Cell Biology, Lipid signaling, Sphingolipid, carbohydrates (lipids), Alcohol Oxidoreductases, 030104 developmental biology, chemistry, lipids (amino acids, peptides, and proteins), Epidermis
Abstract: Ceramide (Cer) is a structural backbone of sphingolipids and is composed of a long-chain base and a fatty acid. Existence of a variety of Cer species, which differ in chain-length, hydroxylation status, and/or double bond number of either of their hydrophobic chains, has been reported. Ceramide is produced by Cer synthases. Mammals have six Cer synthases (CERS1-6), each of which exhibits characteristic substrate specificity toward acyl-CoAs with different chain-lengths. Knockout mice for each Cer synthase show corresponding, isozyme-specific phenotypes, revealing the functional differences of Cers with different chain-lengths. Cer diversity is especially prominent in epidermis. Changes in Cer levels, composition, and chain-lengths are associated with atopic dermatitis. Acylceramide (acyl-Cer) specifically exists in epidermis and plays an essential role in skin permeability barrier formation. Accordingly, defects in acyl-Cer synthesis cause the cutaneous disorder ichthyosis with accompanying severe skin barrier defects. Although the molecular mechanism by which acyl-Cer is generated was long unclear, most genes involved in its synthesis have been identified recently. In Cer degradation pathways, the long-chain base moiety of Cer is converted to acyl-CoA, which is then incorporated mainly into glycerophospholipids. This pathway generates the lipid mediator sphingosine 1-phosphate. This review will focus on recent advances in our understanding of the synthesis and degradation pathways, physiological functions, and pathology of Cers/acyl-Cers.
Published: 2016

36. A shift in sphingolipid composition from C24 to C16 increases susceptibility to apoptosis in HeLa cells

Author: Takayuki Sassa, Akio Kihara, Shota Suto, and Yuriko Okayasu
Subjects: Ceramide, Fatty Acid Elongases, Ultraviolet Rays, Apoptosis, Ceramides, Transfection, Sphingolipid, HeLa, chemistry.chemical_compound, Membrane Microdomains, Acetyltransferases, Sphingosine N-Acyltransferase, Humans, RNA, Small Interfering, Molecular Biology, Caspase 7, Gene knockdown, biology, Caspase 3, Tumor Suppressor Proteins, Lipid microdomain, Membrane Proteins, Lipid metabolism, Cell Biology, Lipid Metabolism, biology.organism_classification, Caspase, Cell biology, Biochemistry, chemistry, Very long-chain fatty acid, Gene Knockdown Techniques, Colorimetry, lipids (amino acids, peptides, and proteins), Cisplatin, HeLa Cells
Abstract: Sphingolipids, major lipid components of the eukaryotic plasma membrane, have a variety of physiological functions and have been associated with many diseases. They have also been implicated in apoptosis. Sphingolipids are heterogeneous in their acyl chain length, with long-chain (C16) and very long-chain (C24) sphingolipids being predominant in most mammalian tissues. We demonstrate that knockdown of ELOVL1 or CERS2, which catalyze synthesis of C24 acyl-CoAs and C24 ceramide, respectively, drastically reduced C24 sphingolipid levels with a complementary increase in C16 sphingolipids. Under ELOVL1 or CERS2 knockdown conditions, cisplatin-induced apoptosis significantly increased. Enhanced sensitivity to cisplatin-induced apoptosis exhibited close correlation with increases in caspase-3/7 activity. No significant alterations in sphingolipid metabolism such as ceramide generation were apparent with the cisplatin-induced apoptosis, and inhibitors of ceramide generation had no effect on the apoptosis. Apoptosis induced by UV radiation or C6 ceramides also increased in ELOVL1 or CERS2 knockdown cells. Changes in the composition of sphingolipid chain length may affect susceptibility to stimuli-induced apoptosis by affecting the properties of cell membranes, such as lipid microdomain/raft formation.
Published: 2012

37. The Sjögren-Larsson Syndrome Gene Encodes a Hexadecenal Dehydrogenase of the Sphingosine 1-Phosphate Degradation Pathway

Author: Kensuke Abe, Tatsuro Naganuma, Aya Ohkuni, Yusuke Ohno, Raphael A. Zoeller, Kanae Nakahara, Takuya Kitamura, and Akio Kihara
Subjects: Saccharomyces cerevisiae Proteins, Genes, Fungal, Mutant, CHO Cells, Palmitic Acids, Saccharomyces cerevisiae, Biology, chemistry.chemical_compound, Cricetulus, Sphingosine, Cricetinae, Coenzyme A Ligases, Animals, Humans, Sphingosine-1-phosphate, Molecular Biology, chemistry.chemical_classification, Cell Biology, Metabolism, Aldehyde Oxidoreductases, Yeast, Sjogren-Larsson Syndrome, Metabolic pathway, Enzyme, chemistry, Hexadecenoic Acid, Biochemistry, Mutation, lipids (amino acids, peptides, and proteins), Acyl Coenzyme A, Lysophospholipids, Metabolic Networks and Pathways
Abstract: Sphingosine 1-phosphate (S1P) functions not only as a bioactive lipid molecule, but also as an important intermediate of the sole sphingolipid-to-glycerolipid metabolic pathway. However, the precise reactions and the enzymes involved in this pathway remain unresolved. We report here that yeast HFD1 and the Sjögren-Larsson syndrome (SLS)-causative mammalian gene ALDH3A2 are responsible for conversion of the S1P degradation product hexadecenal to hexadecenoic acid. The absence of ALDH3A2 in CHO-K1 mutant cells caused abnormal metabolism of S1P/hexadecenal to ether-linked glycerolipids. Moreover, we demonstrate that yeast Faa1 and Faa4 and mammalian ACSL family members are acyl-CoA synthetases involved in the sphingolipid-to-glycerolipid metabolic pathway and that hexadecenoic acid accumulates in Δfaa1 Δfaa4 mutant cells. These results unveil the entire S1P metabolic pathway: S1P is metabolized to glycerolipids via hexadecenal, hexadecenoic acid, hexadecenoyl-CoA, and palmitoyl-CoA. From our results we propose a possibility that accumulation of the S1P metabolite hexadecenal contributes to the pathogenesis of SLS.
Published: 2012

38. Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system

Author: Akihiro Ishitomi, Yusuke Ohno, Yuki Yamazaki, Ren Ogata, Akio Kihara, and Atsushi Kashio
Subjects: Cell Physiology, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae, Substrate Specificity, Palmitoylation, Acetyltransferases, Gene Expression Regulation, Fungal, Humans, Cysteine, Molecular Biology, Integral membrane protein, Cellular localization, biology, Membrane Proteins, Cell Biology, Articles, biology.organism_classification, Protein subcellular localization prediction, Cell biology, Protein Structure, Tertiary, Biochemistry, Membrane protein, Acyltransferases, Function (biology)
Abstract: Twenty-one human DHHC proteins formed acyl intermediates. Seventeen of the proteins exhibited protein acyltransferase activities. DHHC1, 10, 14, and 16 are novel protein acyltransferases. DHHC proteins are classified into three classes based on substrate specificities., Palmitoylation plays important roles in the regulation of protein localization, stability, and activity. The protein acyltransferases (PATs) have a common DHHC Cys-rich domain. Twenty-three DHHC proteins have been identified in humans. However, it is unclear whether all of these DHHC proteins function as PATs. In addition, their substrate specificities remain largely unknown. Here we develop a useful method to examine substrate specificities of PATs using a yeast expression system with six distinct model substrates. We identify 17 human DHHC proteins as PATs. Moreover, we classify 11 human and 5 yeast DHHC proteins into three classes (I, II, and III), based on the cellular localization of their respective substrates (class I, soluble proteins; class II, integral membrane proteins; class III, lipidated proteins). Our results may provide an important clue for understanding the function of individual DHHC proteins.
Published: 2012

39. HACD1, a regulator of membrane composition and fluidity, promotes myoblast fusion and skeletal muscle growth

Author: S. Blot, Fanny Pilot-Storck, Yusuke Ohno, Anaëlle Rahier, Nicolas Blanchard-Gutton, Inès Barthélémy, Geneviève Aubin-Houzelstein, Alexandre Prola, Sébastien Storck, Richard J. Piercy, Jean Demarquoy, Vincent Gache, Laurent Tiret, Marie Maurer, Gemma Walmsley, Frédéric Relaix, Arnaud Ferry, Laurent Guillaud, Akio Kihara, Stéphane Guyot, Stéphanie Gadin, Jordan Blondelle, Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Hokkaido University [Sapporo, Japan], Procédés Microbiologiques et Biotechnologiques (PMB), Procédés Alimentaires et Microbiologiques (PAM), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Procédés Alimentaires et Microbiologiques [Dijon] (PAM), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté [COMUE] (UBFC)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté [COMUE] (UBFC), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Thérapie des maladies du muscle strié, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Bourgogne (UB), Comparative Neuromuscular Diseases Laboratory, Royal Veterinary College, Dijon, Institut Agro, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-IFR10, Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté [COMUE] (UBFC)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, and Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)
Subjects: Male, [SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineering, Cellular differentiation, Generalized muscle weakness, Biology, Muscle Development, centronuclear myopathy, Cell Line, Myoblasts, 03 medical and health sciences, chemistry.chemical_compound, Myoblast fusion, Mice, 0302 clinical medicine, Dogs, VLCFA, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Genetics, medicine, Myocyte, Animals, Humans, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, MUFA, Centronuclear myopathy, Muscle, Skeletal, Molecular Biology, 030304 developmental biology, Mice, Knockout, 0303 health sciences, PTPLA, Cell Membrane, Skeletal muscle, Cell Differentiation, Cell Biology, General Medicine, Articles, [SDV.IDA] Life Sciences [q-bio]/Food engineering, medicine.disease, Congenital myopathy, Lysophosphatidylcholine, medicine.anatomical_structure, LPC, chemistry, Biochemistry, Female, Protein Tyrosine Phosphatases, lpc, mufa, ptpla, vlcfa, 030217 neurology & neurosurgery
Abstract: International audience; The reduced diameter of skeletal myofibres is a hallmark of several congenital myopathies, yet the underlying cellular and molecular mechanisms remain elusive. In this study, we investigate the role of HACD1/PTPLA, which is involved in the elongation of the very long chain fatty acids, in muscle fibre formation. In humans and dogs, HACD1 deficiency leads to a congenital myopathy with fibre size disproportion associated with a generalized muscle weakness. Through analysis of HACD1-deficient Labradors, Hacd1-knockout mice, and Hacd1-deficient myoblasts, we provide evidence that HACD1 promotes myoblast fusion during muscle development and regeneration. We further demonstrate that in normal differentiating myoblasts, expression of the catalytically active HACD1 isoform, which is encoded by a muscle-enriched splice variant, yields decreased lysophosphatidylcholine content, a potent inhibitor of myoblast fusion, and increased concentrations of ≥C18 and monounsaturated fatty acids of phospholipids. These lipid modifications correlate with a reduction in plasma membrane rigidity. In conclusion, we propose that fusion impairment constitutes a novel, non-exclusive pathological mechanism operating in congenital myopathies and reveal that HACD1 is a key regulator of a lipid-dependent muscle fibre growth mechanism.
Published: 2015

40. Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Author: Tatsuro Naganuma, Takayuki Sassa, Yuichiro Sato, Akio Kihara, and Yusuke Ohno
Subjects: Fatty Acid Elongases, Very long chain fatty acid, Biophysics, Biology, ELOVL, Biochemistry, Catalysis, chemistry.chemical_compound, Structural Biology, Acetyltransferases, Genetics, High activity, Humans, Molecular Biology, chemistry.chemical_classification, Carbon chain, Elongase, HEK 293 cells, Fatty Acids, Membrane, Fatty acid, Cell Biology, Lipid, Malonyl Coenzyme A, HEK293 Cells, chemistry, Very long-chain fatty acid, lipids (amino acids, peptides, and proteins), Elongation, Long chain fatty acid
Abstract: Very long-chain fatty acids (VLCFAs) have a variety of physiological functions and are related to numerous disorders. The key step of VLCFA elongation is catalyzed by members of the elongase family, ELOVLs. Mammals have seven ELOVLs (ELOVL1-7), yet none of them has been purified and analyzed. In the presented study we purified ELOVL7 and measured its activity by reconstituting it into proteoliposomes. Purified ELOVL7 exhibited high activity toward acyl-CoAs with C18 carbon chain length. The calculated Km values toward C18:3(n-3)-CoA and malonyl-CoA were both in the μM range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity.
Published: 2011

41. ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis

Author: Yasuyuki Igarashi, Masao Yamanaka, Takayuki Sassa, Yukiko Mizutani, Susumu Mitsutake, Shota Suto, Akio Kihara, and Yusuke Ohno
Subjects: Male, Fatty Acid Elongases, Saccharomyces cerevisiae, In Vitro Techniques, Biology, Cell Line, Substrate Specificity, Acyl-CoA, chemistry.chemical_compound, Membrane Microdomains, monounsaturated fatty acid, Acetyltransferases, lipid metabolism, Sphingosine N-Acyltransferase, Sphingosine N-acyltransferase, Humans, Tissue Distribution, RNA, Messenger, RNA, Small Interfering, Ceramide synthase, DNA Primers, Sphingolipids, Multidisciplinary, Base Sequence, saturated fatty acid, Tumor Suppressor Proteins, Fatty Acids, Lipid microdomain, Membrane Proteins, acyl-CoA, Biological Sciences, polyunsaturated fatty acid, Sphingolipid, Recombinant Proteins, Membrane protein, Biochemistry, chemistry, Gene Knockdown Techniques, Saturated fatty acid, Female, Acyl Coenzyme A, HeLa Cells, Proto-oncogene tyrosine-protein kinase Src
Abstract: Very long-chain fatty acids (VLCFAs) exert a variety of cellular functions and are associated with numerous diseases. However, the precise pathway behind their elongation has remained elusive. Moreover, few regulatory mechanisms for VLCFAs synthesis have been identified. Elongases catalyze the first of four steps in the VLCFA elongation cycle; mammals have seven elongases (ELOVL1–7). In the present study, we determined the precise substrate specificities of all the ELOVLs by in vitro analyses. Particularly notable was the high activity exhibited by ELOVL1 toward saturated and monounsaturated C20- and C22-CoAs, and that it was essential for the production of C24 sphingolipids, which are unique in their capacity to interdigitate within the membrane as a result of their long chain length. We further established that ELOVL1 activity is regulated with the ceramide synthase CERS2, an enzyme essential for C24 sphingolipid synthesis. This regulation may ensure that the production of C24-CoA by elongation is coordinated with its utilization. Finally, knockdown of ELOVL1 caused a reduction in the activity of the Src kinase LYN, confirming that C24-sphingolipids are particularly important in membrane microdomain function.
Published: 2010

42. Ceramide biosynthesis in keratinocyte and its role in skin function

Author: Kiyomi Tsuji, Susumu Mitsutake, Yukiko Mizutani, Yasuyuki Igarashi, and Akio Kihara
Subjects: Keratinocytes, Ceramide, Biology, Ceramides, Models, Biological, Biochemistry, chemistry.chemical_compound, medicine, Stratum corneum, Animals, Humans, Ceramide synthase, Barrier function, Skin, Molecular Structure, integumentary system, Epidermis (botany), General Medicine, Lipid signaling, Water Loss, Insensible, Sphingolipid, Biosynthetic Pathways, medicine.anatomical_structure, chemistry, Oxidoreductases, Keratinocyte
Abstract: The enucleate layer of the epidermis, i.e. the stratum corneum, is responsible for certain critical protective functions, such as epidermal permeability barrier function. Within the epidermal membrane lamella component, ceramides are the dominant lipid class by weight (over 50%) and exhibit the greatest molecular heterogeneity in terms of sphingoid base and fatty acid composition. It is now evermore important to understand how ceramide production and functions are controlled in the epidermis, since decreased epidermal ceramide content has been linked to water loss and barrier dysfunction. During the past several years, critical enzymes in ceramide biosynthesis have been identified, including ceramide synthases (CerS) and ceramide hydroxylase/desaturase. In this review, we describe the molecular heterogeneity of ceramides synthesized in the epidermis and their possible roles in epidermal permeability barrier functions. We also describe recent studies that identified the family of CerS (CerS1-CerS6) in mammals. We further focus on the roles of specific isoforms of these enzymes in synthesizing the epidermal ceramides, especially in relation to chain-length specificity. In addition, we provide experimental information, including our recent findings, as to how applying ceramide or ceramide-containing substances to skin, orally or directly, can benefit skin health.
Published: 2009

43. 2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length

Author: Yasuyuki Igarashi, Yukiko Mizutani, Akio Kihara, Hiroko Chiba, and Hiromasa Tojo
Subjects: Keratinocytes, Ceramide, fatty acid 2-hydroxylase, QD415-436, Biology, Ceramides, Biochemistry, Cell Line, Mixed Function Oxygenases, chemistry.chemical_compound, Endocrinology, epidermis, Sphingosine N-Acyltransferase, Stratum corneum, medicine, Humans, Ceramide synthase, Cells, Cultured, chemistry.chemical_classification, Messenger RNA, Epidermis (botany), Fatty Acids, Infant, Newborn, Cell Differentiation, Cell Biology, Lipid signaling, In vitro, carbohydrates (lipids), Enzyme, medicine.anatomical_structure, chemistry, Multigene Family, lipids (amino acids, peptides, and proteins), hydroxy fatty acids, Oxidoreductases, HeLa Cells
Abstract: Ceramide is unusually abundant in epidermal stratum corneum and is important for permeability barrier function. Ceramides in epidermis also comprise an unusual variety, including 2-hydroxy (alpha-hydroxy)-ceramide. Six mammalian ceramide synthase/longevity assurance homologue (CerS/LASS) family members have been identified as synthases responsible for ceramide (CER) production. We reveal here that of the six, CerS3/LASS3 mRNA is the most predominantly expressed in keratinocytes. Moreover, its expression is increased upon differentiation. CerS family members have known substrate specificities for fatty acyl-CoA chain length and saturation, yet their abilities to produce 2-hydroxy-CER have not been examined. In the present study, we demonstrate that all CerS members can produce 2-hydroxy-CER when overproduced in HEK 293T cells. Each produced a 2-hydroxy-CER with a chain length similar to that of the respective nonhydroxy-CER produced. In HeLa cells overproducing the FA 2-hydroxylase FA2H, knock-down of CerS2 resulted in a reduction in total long-chain 2-hydroxy-CERs, confirming enzyme substrate specificity for chain length. In vitro CerS assays confirmed the ability of CerS1 to utilize 2-hydroxy-stearoyl-CoA as a substrate. These results suggest that all CerS members can synthesize 2-hydroxy-CER with specificity for 2-hydroxy-fatty acyl-CoA chain length and that CerS3 may be important in CER and 2-hydroxy-CER synthesis in epidermis.
Published: 2008

44. A splicing isoform of LPP1, LPP1a, exhibits high phosphatase activity toward FTY720 phosphate

Author: Akio Kihara, Yasuyuki Igarashi, Yoshihiro Anada, and Masao Yamanaka
Subjects: T cell, Phosphatase, Phosphatidate Phosphatase, Biophysics, CHO Cells, Biology, Biochemistry, Dephosphorylation, chemistry.chemical_compound, Cricetulus, Sphingosine, Cricetinae, hemic and lymphatic diseases, medicine, Animals, Humans, Protein Isoforms, Sphingosine-1-phosphate, Receptor, Molecular Biology, Fingolimod Hydrochloride, Endothelial Cells, Cell Biology, Cell biology, Endothelial stem cell, Alternative Splicing, medicine.anatomical_structure, chemistry, Propylene Glycols, Phosphorylation, Immunosuppressive Agents
Abstract: The sphingolipid metabolite sphingosine 1-phosphate (S1P) plays an essential function in the egress of T cells from the thymus and secondary lymphoid organs. The novel immunomodulating agent FTY720 is phosphorylated in vivo to the functional form FTY720 phosphate (FTY720-P), which is structurally similar to S1P. FTY720-P inhibits the S1P-mediated T cell egress as an agonist of S1P receptors. FTY720-P is not stable in plasma and is dephosphorylated to FTY720. In the present study, we investigated activities toward FTY720-P of LPP family members (LPP1, LPP1a, LPP2, and LPP3), which exhibit broad substrate specificity. Of the four, LPP1a, the splicing isoform of LPP1, had the highest activity toward FTY720-P, and the highest affinity. Among blood-facing cells tested, only endothelial cells displayed high phosphatase activity for FTY720-P. Significant levels of LPP1a expression were found in endothelial cells, suggesting that LPP1a is important for the dephosphorylation of FTY720-P in plasma.
Published: 2008

45. Production and release of sphingosine 1-phosphate and the phosphorylated form of the immunomodulator FTY720

Author: Yasuyuki Igarashi and Akio Kihara
Subjects: Lymphocyte, Biology, chemistry.chemical_compound, Immune system, Sphingosine, hemic and lymphatic diseases, medicine, Animals, Humans, Platelet, Sphingosine-1-phosphate, Phosphorylation, Receptor, Molecular Biology, Fingolimod Hydrochloride, Biological Transport, Cell Biology, Sphingolipid, Cell biology, Receptors, Lysosphingolipid, medicine.anatomical_structure, chemistry, Biochemistry, Propylene Glycols, lipids (amino acids, peptides, and proteins), Lysophospholipids, Immunosuppressive Agents
Abstract: The bioactive lipid molecule sphingosine 1-phosphate (S1P) binds to specific cell surface receptors and regulates several cellular processes. S1P is abundant in plasma, and physiologically its most important target cells are lymphocytes and vascular endothelial cells. S1P plays a pivotal role in the immune system by regulating lymphocyte egress from the thymus and secondary lymphoid organs. The immunomodulator FTY720 impairs this egress, causing lymphopenia. Platelets had long been considered to be the major source of plasma S1P, however recent studies revealed the importance of erythrocytes as a major supply. The sphingosine analog FTY720 is a prodrug, and FTY720 phosphate (FTY720-P) its functional form. Although both erythrocytes and platelets can produce S1P, only platelets synthesize and release FTY720-P. This review will focus on the recent advances in our understanding of the metabolism and release of S1P and FTY720-P, especially in platelets and erythrocytes.
Published: 2008

46. Rapid trafficking of c-Src, a non-palmitoylated Src-family kinase, between the plasma membrane and late endosomes/lysosomes

Author: Akio Kihara, Naoto Yamaguchi, Kousuke Kasahara, Yasuyuki Igarashi, Daisuke Matsuda, Yuji Nakayama, Yasunori Fukumoto, Kikuko Ikeda, and Takahisa Kuga
Subjects: Cell Survival, Endosome, Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Proto-Oncogene Proteins pp60(c-src), Palmitic Acid, Endosomes, Biology, src Homology Domains, Focal adhesion, symbols.namesake, Dogs, Palmitoylation, LYN, Chlorocebus aethiops, Animals, Humans, Amino Acid Sequence, Src family kinase, Secretory pathway, Focal Adhesions, Cell Membrane, Cell Biology, Golgi apparatus, Cell biology, Protein Transport, src-Family Kinases, COS Cells, symbols, Lysosomes, HeLa Cells, Proto-oncogene tyrosine-protein kinase Src
Abstract: Src-family kinases (SFKs) are co-expressed with multiple combinations of each member in a single cell and involved in various signalings. Recently, we showed by sucrose-density gradient fractionation that the subcellular distribution of c-Src is distinct from that of Lyn. However, little is known about the trafficking of c-Src in living cells. Here, we show by time-lapse monitoring combined with photobleaching techniques that c-Src, a non-palmitoylated SFK, is rapidly exchanged between the plasma membrane and intracellular organelles representing late endosomes/lysosomes possibly through its cytosolic release. Although Lyn, a palmitoylated SFK, is exocytosed to the plasma membrane via the Golgi apparatus along the secretory pathway, lack of palmitoylation directs Lyn away from the exocytotic transport to the c-Src-type trafficking between the plasma membrane and late endosomes/lysosomes. Intriguingly, c-Src and a non-palmitoylated Lyn mutant are efficiently delivered and immobilized to focal adhesions when their SH2 domains are able to mediate protein-protein interactions in place of intramolecular bindings. However, palmitoylation of Lyn inhibits its recruitment to focal adhesions. These results suggest that palmitoylation of SFKs is critical for SFK localization and trafficking and implicate that two distinct trafficking pathways for SFKs may be involved in SFKs' specific functions.
Published: 2007

47. Lack of sphingosine 1-phosphate-degrading enzymes in erythrocytes

Author: Mika Ikeda, Takamitsu Sano, Yasuyuki Igarashi, Akio Kihara, Kiyoharu Ito, Yoshihiro Anada, and Motohiro Tani
Subjects: Blood Platelets, Erythrocytes, Biophysics, Biochemistry, Sphingolipid, chemistry.chemical_compound, Sphingosine, Humans, Platelet, Sphingosine-1-phosphate, Kinase activity, Molecular Biology, Cells, Cultured, Aldehyde-Lyases, Whole blood, chemistry.chemical_classification, organic chemicals, In vitro toxicology, Membrane Proteins, Cell Biology, Lipid, Phosphoric Monoester Hydrolases, Cell biology, Erythrocyte, Enzyme, chemistry, Sphingosine 1-phosphate, lipids (amino acids, peptides, and proteins), Lysophospholipids
Abstract: Platelets are known to store a large amount of the bioactive lipid molecule sphingosine 1-phosphate (S1P) and to release it into the plasma in a stimuli-dependent manner. Erythrocytes can also release S1P, independently from any stimuli. We measured the S1P and sphingosine (Sph) levels in erythrocytes by HPLC and found that the contribution of erythrocyte S1P to whole blood S1P levels is actually higher than that of platelets. In vitro assays demonstrated that erythrocytes possess much weaker Sph kinase activity compared to platelets but lack the S1P-degrading activities of either S1P lyase or S1P phosphohydrolase. This combination may enable erythrocytes to maintain a high S1P content relative to Sph. The absence of both S1P-degrading enzymes has not been reported for other cell types. Thus, erythrocytes may be specialized cells for storing and supplying plasma S1P.
Published: 2007

48. Metabolism and biological functions of two phosphorylated sphingolipids, sphingosine 1-phosphate and ceramide 1-phosphate

Author: Susumu Mitsutake, Yasuyuki Igarashi, Yukiko Mizutani, and Akio Kihara
Subjects: Blood Platelets, Ceramide, Cell signaling, Sphingosine kinase, Biology, Ceramides, Biochemistry, chemistry.chemical_compound, Sphingosine, Ceramide kinase, Animals, Humans, Sphingosine-1-phosphate, Phosphorylation, Sphingolipids, Cell Biology, Lipid signaling, Sphingolipid, Cell biology, carbohydrates (lipids), chemistry, lipids (amino acids, peptides, and proteins), Lysophospholipids, Signal Transduction
Abstract: Sphingolipids are major lipid constituents of the eukaryotic plasma membrane. Without certain sphingolipids, cells and/or embryos cannot survive, indicating that sphingolipids possess important physiological functions that are not substituted for by other lipids. One such role may be signaling. Recent studies have revealed that some sphingolipid metabolites, such as long-chain bases (LCBs; sphingosine (Sph) in mammals), long-chain base 1-phosphates (LCBPs; sphingosine 1-phosphate (S1P) in mammals), ceramide (Cer), and ceramide 1-phosphate (C1P), act as signaling molecules. The addition of phosphate groups to LCB/Sph and Cer generates LCBP/S1P and C1P, respectively. These phospholipids exhibit completely different functions than those of their precursors. In this review, we describe recent advances in understanding the functions of LCBP/S1P and C1P in mammals and in the yeast Saccharomyces cerevisiae. Since LCB/Sph, LCBP/S1P, Cer, and C1P are mutually convertible, regulation of not only the total amount of the each lipid but also of the overall balance in cellular levels is important. Therefore, we describe in detail their metabolic pathways, as well as the genes involved in each reaction.
Published: 2007

49. Essential role of the cytochrome P450 CYP4F22 in the production of acylceramide, the key lipid for skin permeability barrier formation

Author: Nozomi Kamiyama, Hisashi Tsujimura, Junko Ishikawa, Kazumitsu Sugiura, Masashi Akiyama, Shota Nakamichi, Yusuke Ohno, Akio Kihara, Ayano Naoe, Urara Yokose, and Aya Ohkuni
Subjects: Ceramide, acylceramide, Biology, Ceramides, Endoplasmic Reticulum, Permeability, chemistry.chemical_compound, CYP4F22, Cytochrome P-450 Enzyme System, lipid, medicine, Humans, ceramide, Skin, chemistry.chemical_classification, Multidisciplinary, integumentary system, Ichthyosis, Endoplasmic reticulum, Fatty acid, Cytochrome P450, Biological Sciences, medicine.disease, Lipid Metabolism, Sphingolipid, Biochemistry, chemistry, Membrane protein, Child, Preschool, biology.protein, Female, sphingolipid
Abstract: A skin permeability barrier is essential for terrestrial animals, and its impairment causes several cutaneous disorders such as ichthyosis and atopic dermatitis. Although acylceramide is an important lipid for the skin permeability barrier, details of its production have yet to be determined, leaving the molecular mechanism of skin permeability barrier formation unclear. Here we identified the cytochrome P450 gene CYP4F22 (cytochrome P450, family 4, subfamily F, polypeptide 22) as the long-sought fatty acid ω-hydroxylase gene required for acylceramide production. CYP4F22 has been identified as one of the autosomal recessive congenital ichthyosis-causative genes. Ichthyosis-mutant proteins exhibited reduced enzyme activity, indicating correlation between activity and pathology. Furthermore, lipid analysis of a patient with ichthyosis showed a drastic decrease in acylceramide production. We determined that CYP4F22 was a type I membrane protein that locates in the endoplasmic reticulum (ER), suggesting that the ω-hydroxylation occurs on the cytoplasmic side of the ER. The preferred substrate of the CYP4F22 was fatty acids with a carbon chain length of 28 or more (≥C28). In conclusion, our findings demonstrate that CYP4F22 is an ultra-long-chain fatty acid ω-hydroxylase responsible for acylceramide production and provide important insights into the molecular mechanisms of skin permeability barrier formation. Furthermore, based on the results obtained here, we proposed a detailed reaction series for acylceramide production.
Published: 2015

50. Histological analyses by matrix-assisted laser desorption/ionization-imaging mass spectrometry reveal differential localization of sphingomyelin molecular species regulated by particular ceramide synthase in mouse brains

Author: Akio Kihara, Masayuki Sugimoto, Yukari Tanaka, Yuji Kuge, Takeshi Yoshioka, Yoshito Numata, Yoichi Shimizu, Shota Sakai, Kenichi Higashino, Masato Wakabayashi, and Yasuyuki Igarashi
Subjects: Gene isoform, Sphingomyelin, Male, Ceramide, Very long chain fatty acid, Mass spectrometry imaging, chemistry.chemical_compound, Mice, Imaging mass spectrometry, Fourier transform ion cyclotron resonance, Ceramide synthase, Sphingosine N-Acyltransferase, Animals, Humans, Molecular Biology, Brain Chemistry, ATP synthase, biology, Brain, Cell Biology, Hep G2 Cells, Sphingomyelins, Matrix-assisted laser desorption/ionization, chemistry, Biochemistry, Very long-chain fatty acid, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, biology.protein, lipids (amino acids, peptides, and proteins)
Abstract: Sphingomyelin (SM) is synthesized by SM synthase (SMS) from ceramide (Cer). SM regulates signaling pathways and maintains organ structure. SM comprises a sphingoid base and differing lengths of acyl-chains, but the importance of its various forms and regulatory synthases is not known. It has been reported that Cer synthase (CerS) has restricted substrate specificity, whereas SMS has no specificity for different lengths of acyl-chains. We hypothesized that the distribution of each SM molecular species was regulated by expression of the CerS family. Thus, we compared the distribution of SM species and CerS mRNA expression using molecular imaging. Spatial distribution of each SM molecular species was investigated using ultra-high-resolution imaging mass spectrometry (IMS). IMS revealed that distribution of SM molecular species varied according to the lengths of acyl-chains found in each brain section. Furthermore, a combination study using in situ hybridization and IMS revealed the spatial expression of CerS1 to be associated with the localization of SM (d18:1/18:0) in cell body-rich gray matter, and CerS2 to be associated with SM (d18:1/24:1) in myelin-rich white matter. Our study is the first comparison of spatial distribution between SM molecular species and CerS isoforms, and revealed their distinct association in the brain. These observations were demonstrated by suppression of CerS2 using siRNA in HepG2 cells; that is, siRNA for CerS2 specifically decreased C22 very long-chain fatty acid (VLCFA)- and C24 VLCFA-containing SMs. Thus, histological analyses of SM species by IMS could be a useful approach to consider their molecular function and regulative mechanism.
Published: 2015

Catalog

Books, media, physical & digital resources

See catalog results

Searchworks

Select search scope, currently: Articles Catalog books, media & more in Jio Institute collections Articles journal articles & other e-resources

Search

Search Constraints

Refine your results

Search Limiters

Topic

Publication Year Range

Language

Journal

Database

Publisher

76 results on '"Akio Kihara"'

Search Results

Catalog

Select search scope, currently: Articles

Catalog

books, media & more in Jio Institute collections

Articles

journal articles & other e-resources