Author: "Isei Tanida" / Topic: autophagy - Searchworks@Jio Institute Digital Library Search Results

57 results on '"Isei Tanida"'

1. Improved volume CLEM revealed that aberrant phagophores and RB1CC1/FIP200-containing clusters appear surround SQSTM1/p62 aggregates in Atg9a-deficient cells

Author: Soichiro Kakuta, Junji Yamaguchi, Chigure Suzuki, Isei Tanida, and Yasuo Uchiyama
Subjects: 3d-clem, autophagosome, autophagy, electron microscopy, fib-sem, isolation membrane, Cytology, QH573-671
Abstract: ATG9A is an important membrane protein in mammalian macroautophagy. The formation of autophagosomes and phagophores is blocked in atg9a KO cells. However, it remains possible that residual membrane formation activity exists in these cells. These precursor structures that precede phagophores are, if they exist, rare and may be difficult to find. Here, we introduce the modified volume correlative light and electron microscopy (CLEM) method to analyze these structures three-dimensionally. In addition to target proteins, mitochondria were labeled as a landmark for precise correlation of slice images by a confocal fluorescence microscope and a focused ion beam scanning electron microscope. We found phagophores and small membrane vesicles near SQSTM1/p62 aggregates in atg9a KO cells, indicating that phagophores could be formed in atg9a-deficient cells, although they were immature and inefficient. Furthermore, we found that RB1CC1/FIP200-positive structures formed clusters around SQSTM1/p62 with ferritin and TAX1BP1. Taken together, our method contributes to the understanding of undiscovered fine structures. Abbreviations: CLEM: correlative light and electron microscopy; EM: electron microscopy; ER: endoplasmic reticulum; FIB-SEM: focused ion beam scanning electron microscopy; FM: fluorescence microscopy; GFP: green fluorescent protein; KO: knock out; MEF: mouse embryonic fibroblast; PBS: phosphate-buffered saline; ROI: region of interest; SEM: scanning electron microscopy.
Published: 2023
Full Text: View/download PDF

2. Membranous Structures Directly Come in Contact With p62/SQSTM1 Bodies

Author: Mitsuo Suga, Yoko Furuta, Soichiro Kakuta, Akira Takebe, Yasuo Uchiyama, Tomohiro Haruta, Isei Tanida, Juan Alejandro Oliva Trejo, Shunsuke Takei, and Junji Yamaguchi
Subjects: 0301 basic medicine, Histology, Chemistry, Autophagy, Autophagosomes, Signal transducing adaptor protein, Articles, Endoplasmic Reticulum, Cell Membrane Structures, Cell biology, Selective autophagy, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Feature (computer vision), Cytoplasm, Sequestosome-1 Protein, Humans, Anatomy, Phospholipids, 030217 neurology & neurosurgery, HeLa Cells
Abstract: During autophagy, autophagosomes are formed to engulf cytoplasmic contents. p62/SQSTM-1 is an autophagic adaptor protein that forms p62 bodies. A unique feature of p62 bodies is that they seem to directly associate with membranous structures. We first investigated the co-localization of mKate2-p62 bodies with phospholipids using click chemistry with propargyl-choline. Propargyl-choline-labeled phospholipids were detected inside the mKate2-p62 bodies, suggesting that phospholipids were present inside the bodies. To clarify whether or not p62 bodies come in contact with membranous structures directly, we investigated the ultrastructures of p62 bodies using in-resin correlative light and electron microscopy of the Epon-embedded cells expressing mKate2-p62. Fluorescent-positive p62 bodies were detected as uniformly lightly osmificated structures by electron microscopy. Membranous structures were detected on and inside the p62 bodies. In addition, multimembranous structures with rough endoplasmic reticulum–like structures that resembled autophagosomes directly came in contact with amorphous-shaped p62 bodies. These results suggested that p62 bodies are unique structures that can come in contact with membranous structures directly
Published: 2021
Full Text: View/download PDF

3. Characterization of starvation-induced autophagy in cerebellar Purkinje cells of pHluorin-mKate2-human LC3B transgenic mice

Author: Juan Alejandro Oliva Trejo, Isei Tanida, Yasuo Uchiyama, Norihiro Tada, Chigure Suzuki, and Soichiro Kakuta
Subjects: Genetically modified mouse, Autophagosome, Cerebellum, Transgene, Green Fluorescent Proteins, Central nervous system, Hippocampus, lcsh:Medicine, Mice, Transgenic, Biology, Article, Purkinje Cells, Macroautophagy, Autophagy, medicine, Animals, Humans, lcsh:Science, Mice, Inbred ICR, Multidisciplinary, lcsh:R, Autophagosomes, Cellular neuroscience, Cell biology, Luminescent Proteins, medicine.anatomical_structure, nervous system, Starvation, Cerebral cortex, Female, lcsh:Q, biological phenomena, cell phenomena, and immunity, Microtubule-Associated Proteins
Abstract: We generated a new transgenic mouse model that expresses a pHluorin-mKate2 fluorescent protein fused with human LC3B (PK-LC3 mice) for monitoring autophagy activity in neurons of the central nervous system. Histological analysis revealed fluorescent puncta in neurons of the cerebral cortex, hippocampus, cerebellar Purkinje cells, and anterior spinal regions. Using CLEM analysis, we confirmed that PK-LC3-positive puncta in the perikarya of Purkinje cells correspond to autophagic structures. To validate the usability of PK-LC3 mice, we quantified PK-LC3 puncta in Purkinje cells of mice kept in normal feeding conditions and of mice starved for 24 hours. Our results showed a significant increase in autophagosome number and in individual puncta areal size following starvation. To confirm these results, we used morphometry at the electron microscopic level to analyze the volume densities of autophagosomes and lysosomes/autolysosomes in Purkinje cells of PK-LC3 mice. The results revealed that the volume densities of autophagic structures increase significantly after starvation. Together, our data show that PK-LC3 mice are suitable for monitoring autophagy flux in Purkinje cells of the cerebellum, and potentially other areas in the central nervous system.
Published: 2020
Full Text: View/download PDF

4. Establishment of a system for screening autophagic flux regulators using a modified fluorescent reporter and CRISPR/Cas9

Author: Miwa Himuro, Luka Suzuki, Yuya Nishida, Takeshi Miyatsuka, Rieko Yazawa, Toshiaki Shimizu, Hidenori Haruna, Shuhei Aoyama, Hirotaka Watada, Isei Tanida, and Noriyuki Takubo
Subjects: 0301 basic medicine, Green Fluorescent Proteins, Biophysics, Protein degradation, Autophagy-Related Protein 7, Biochemistry, Green fluorescent protein, 03 medical and health sciences, 0302 clinical medicine, Lysosome, Autophagy, medicine, Animals, Humans, CRISPR, Molecular Biology, Cells, Cultured, PI3K/AKT/mTOR pathway, Mice, Knockout, Chemistry, Cell Biology, Fibroblasts, Embryo, Mammalian, Cell biology, Luminescent Proteins, HEK293 Cells, 030104 developmental biology, medicine.anatomical_structure, Gene Expression Regulation, Microscopy, Fluorescence, 030220 oncology & carcinogenesis, CRISPR-Cas Systems, mCherry, Microtubule-Associated Proteins, Flux (metabolism)
Abstract: Autophagy is a mechanism of bulk protein degradation that plays an important role in regulating homeostasis in many organisms. Among several methods for evaluating its activity, a fluorescent reporter GFP-LC3-RFP-LC3ΔG, in which GFP-LC3 is cleaved by ATG4 following autophagic induction and degraded in lysosome, has been used for monitoring autophagic flux, which is the amount of lysosomal protein degradation. In this study, we modified this reporter by exchanging GFP for pHluorin, which is more sensitive to low pH, and RFP to mCherry, to construct pHluorin-LC3-mCherry reporter. Following starvation or mTOR inhibition, the increase of autophagic flux was detected by a decrease of the fluorescent ratio of pHluorin to mCherry; our reporter was also more sensitive to autophagy-inducing stimuli than the previous one. To establish monitoring cells for mouse genome-wide screening of regulators of autophagic flux based on CRISPR/Cas9 system, after evaluating knockout efficiency of clones of Cas9-expressing MEFs, we co-expressed our reporter and confirmed that autophagic flux was impaired in gRNA-mediated knockout of canonical autophagy genes. Finally, we performed genome-wide gRNA screening for genes inhibiting starvation-mediated autophagic flux and identified previously reported genes such as Atgs. Thus, we have successfully established a system for screening of genes regulating autophagic flux with our pHluorin-LC3-mCherry reporter in mice.
Published: 2019
Full Text: View/download PDF

5. Blocking LC3 lipidation and ATG12 conjugation reactions by ATG7 mutant protein containing C572S

Author: Akari Nitta, Ayumi Igarashi, Koji Aoki, Takashi Ueno, Isei Tanida, Yasuyo Deyama, Kazuya Hori, Manabu Sugai, and Eiki Kominami
Subjects: 0301 basic medicine, Autophagosome, ATG8, ATG5, Biophysics, Autophagy-Related Protein 7, Biochemistry, Autophagy-Related Protein 5, ATG12, 03 medical and health sciences, 0302 clinical medicine, Ubiquitin, Mutant protein, Autophagy, Humans, Molecular Biology, Cells, Cultured, biology, Chemistry, Phosphatidylethanolamines, Autophagosomes, Autophagy-Related Protein 8 Family, Cell Biology, Cell biology, 030104 developmental biology, 030220 oncology & carcinogenesis, biology.protein, Mutant Proteins, Autophagy-Related Protein 12
Abstract: Autophagy, a system for the bulk degradation of intracellular components, is essential for homeostasis and the healthy physiology and development of cells and tissues. Its deregulation is associated with human disease. Thus, methods to modulate autophagic activity are critical for analysis of its role in mammalian cells and tissues. Here we report a method to inhibit autophagy using a mutant variant of the protein ATG7, a ubiquitin E1-like enzyme essential for autophagosome formation. During autophagy, ATG7 activates the conjugation of LC3 (ATG8) with phosphatidylethanolamine (PE) and ATG12 with ATG5. Human ATG7 interactions with LC3 or ATG12 require a thioester bond involving the ATG7 cysteine residue at position 572. We generated TetOff cells expressing mutant ATG7 protein carrying a serine substitution of this critical cysteine residue (ATG7C572S). Because ATG7C572S forms stable intermediate complexes with LC3 or ATG12, its expression resulted in a strong blockage of the ATG-conjugation system and suppression of autophagosome formation. Consequently, ATG7C572S mutant protein can be used as an inhibitor of autophagy.
Published: 2019
Full Text: View/download PDF

6. Streptococcus pneumoniae triggers hierarchical autophagy through reprogramming of LAPosome-like vesicles via NDP52-delocalization

Author: Haruko Takeyama, Mikado Tomokiyo, Bin Chang, Soichiro Kakuta, Akihide Ryo, Mitsutaka Yoshida, Sayaka Shizukuishi, Makoto Ohnishi, Naoki Takada, Jun-Lin Guan, Isei Tanida, and Michinaga Ogawa
Subjects: Medicine (miscellaneous), Fluorescent Antibody Technique, Gene Expression, Vacuole, Biology, Models, Biological, General Biochemistry, Genetics and Molecular Biology, Pneumococcal Infections, Article, Cell Line, 03 medical and health sciences, Mice, 0302 clinical medicine, Bacterial Proteins, Genes, Reporter, Phagosomes, Macroautophagy, Xenophagy, Autophagy, Animals, Humans, Cellular microbiology, lcsh:QH301-705.5, ATG16L1, 030304 developmental biology, Phagosome, 0303 health sciences, Innate immune system, Intracellular parasite, Cytoplasmic Vesicles, Autophagosomes, Nuclear Proteins, Bacteriology, Bacterial pathogenesis, bacterial infections and mycoses, Autophagic Punctum, Cell biology, Streptococcus pneumoniae, lcsh:Biology (General), Host-Pathogen Interactions, General Agricultural and Biological Sciences, Reactive Oxygen Species, 030217 neurology & neurosurgery, Intracellular, Biomarkers
Abstract: In innate immunity, multiple autophagic processes eliminate intracellular pathogens, but it remains unclear whether noncanonical autophagy and xenophagy are coordinated, and whether they occur concomitantly or sequentially. Here, we show that Streptococcus pneumoniae, a causative of invasive pneumococcal disease, can trigger FIP200-, PI3P-, and ROS-independent pneumococcus-containing LC3-associated phagosome (LAPosome)-like vacuoles (PcLVs) in an early stage of infection, and that PcLVs are indispensable for subsequent formation of bactericidal pneumococcus-containing autophagic vacuoles (PcAVs). Specifically, we identified LC3- and NDP52-delocalized PcLV, which are intermediates between PcLV and PcAV. Atg14L, Beclin1, and FIP200 were responsible for delocalizing LC3 and NDP52 from PcLVs. Thus, multiple noncanonical and canonical autophagic processes are deployed sequentially against intracellular S. pneumoniae. The Atg16L1 WD domain, p62, NDP52, and poly-Ub contributed to PcLV formation. These findings reveal a previously unidentified hierarchical autophagy mechanism during bactericidal xenophagy against intracellular bacterial pathogens, and should improve our ability to control life-threating pneumococcal diseases., Ogawa, Takada et al. show that Streptococcus pneumoniae triggers the formation of pneumococcus-containing LC3-associated phagosome-like vacuoles in an early stage of infection. This study suggests a hierarchical autophagy mechanism activated by intracellular bacterial pathogens.
Published: 2020

7. Atg9a deficiency causes axon-specific lesions including neuronal circuit dysgenesis

Author: Shigeki Aoki, Keiji Tanaka, Chigure Suzuki, Yasuo Uchiyama, Tatsuya Saitoh, Tomohisa Nanao, Kenji Sakimura, Kentarou Ozawa, Masaaki Komatsu, Takehiko Sunabori, Isei Tanida, Soichirou Kakuta, and Junji Yamaguchi
Subjects: 0301 basic medicine, Neurite, Research Paper - Basic Science, Vesicular Transport Proteins, Autophagy-Related Proteins, degeneration, Anterior commissure, Nerve fiber, Biology, spongiosis, Corpus Callosum, Purkinje Cells, 03 medical and health sciences, Dysgenesis, Western blot, conditional knockout mice, Sequestosome-1 Protein, Conditional gene knockout, Neurites, medicine, Animals, Axon, Molecular Biology, Cells, Cultured, Mice, Knockout, axon, selective autophagy, Integrases, medicine.diagnostic_test, Autophagy, diffusion tensor MRI, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Proteins, Cell Biology, Anatomy, Atg9a, dysgenesis of commissure fibers, nonselective autophagy, Axons, Cell biology, Phenotype, 030104 developmental biology, medicine.anatomical_structure, Nerve Net
Abstract: Conditional knockout mice for Atg9a, specifically in brain tissue, were generated to understand the roles of ATG9A in the neural tissue cells. The mice were born normally, but half of them died within one wk, and none lived beyond 4 wk of age. SQSTM1/p62 and NBR1, receptor proteins for selective autophagy, together with ubiquitin, accumulated in Atg9a-deficient neurosoma at postnatal d 15 (P15), indicating an inhibition of autophagy, whereas these proteins were significantly decreased at P28, as evidenced by immunohistochemistry, electron microscopy and western blot. Conversely, degenerative changes such as spongiosis of nerve fiber tracts proceeded in axons and their terminals that were occupied with aberrant membrane structures and amorphous materials at P28, although no clear-cut degenerative change was detected in neuronal cell bodies. Different from autophagy, diffusion tensor magnetic resonance imaging and histological observations revealed Atg9a-deficiency-induced dysgenesis of the corpus callosum and anterior commissure. As for the neurite extensions of primary cultured neurons, the neurite outgrowth after 3 d culturing was significantly impaired in primary neurons from atg9a-KO mouse brains, but not in those from atg7-KO and atg16l1-KO brains. Moreover, this tendency was also confirmed in Atg9a-knockdown neurons under an atg7-KO background, indicating the role of ATG9A in the regulation of neurite outgrowth that is independent of autophagy. These results suggest that Atg9a deficiency causes progressive degeneration in the axons and their terminals, but not in neuronal cell bodies, where the degradations of SQSTM1/p62 and NBR1 were insufficiently suppressed. Moreover, the deletion of Atg9a impaired nerve fiber tract formation.
Published: 2018

8. 2185-P: Estimation of Autophagy Flux by a Novel Fluorescent Reporter in Organs Involved in Glucose Metabolism Including Pancreatic ß Cells

Author: Shuhei Aoyama, Isei Tanida, Yuya Nishida, Hirotaka Watada, Takeshi Miyatsuka, and Rieko Yazawa
Subjects: Downregulation and upregulation, Chemistry, Endocrinology, Diabetes and Metabolism, Autophagy, Internal Medicine, Glucose homeostasis, Pharmacology, Carbohydrate metabolism, mCherry, Flux (metabolism), Homeostasis, Green fluorescent protein
Abstract: Autophagy is a bulk degradation system which plays an important role to maintain cell homeostasis. We have shown that deficiency of autophagy in pancreatic β cells leads to their failure and deterioration of glucose tolerance. On the other hand, there has been controversy over induction of autophagic flux in β cells following different physiological contexts, as it has been difficult to estimate autophagy flux by using conventional methods such as estimation of LC3-lipidation. Recently, application of a novel autophagy flux, GFP-LC3-RFP-LC3ΔG, is reported, which enables us to evaluate autophagy flux by calculating ratio between the fluorescence of GFP and RFP, as GFP-LC3 is degraded specifically in autolysosomes, whereas RFP-LC3ΔG remains intact in cytosol as an internal control. To improve its usefulness, we modified it to construct pHluorin-LC3-mCherry. First, we expressed this probe in MIN6 cells and confirmed decrease of pHluorin/mCherry ratio following induction of autophagic flux in starvation or administration of specific mTOR inhibitor, Torin-1. Next, we generated knock-in mouse in which the probe is expressed under the control of CAG promotor in ROSA26 locus. Its expression was confirmed based on Western blot and fluorescent microscopy in almost all the tissues that we examined. Then we stimulated the mice with starvation and detected that pHluorin/mCherry ratio decreases after starvation in several organs, including liver and muscle which are deeply involved in glucose homeostasis. Finally, we investigated whether autophagic flux is changed after starvation in pancreatic beta cells and successfully demonstrated that the flux is increased following prolonged starvation. In addition, we also illustrated upregulation of autophagic flux in isolated islets after glucose and amino acid starvation. These results show dynamic change of autophagic flux after starvation in many tissues related to glucose homeostasis including βcells. Disclosure S. Aoyama: None. Y. Nishida: None. R. Yazawa: None. I. Tanida: None. T. Miyatsuka: None. H. Watada: Research Support; Self; Astellas Pharma Inc., Boehringer Ingelheim Pharmaceuticals, Inc., Daiichi Sankyo Company, Limited, Kissei Pharmaceutical Co., Ltd., Merck Sharp & Dohme Corp., Mitsubishi Tanabe Pharma Corporation, Novartis Pharmaceuticals Corporation, Novo Nordisk A/S, Pfizer Inc., Sanofi, Sumitomo Dainippon Pharma Co., Ltd., Takeda Pharmaceutical Company Limited, Teijin Pharma Limited. Speaker's Bureau; Self; Astellas Pharma Inc., Boehringer Ingelheim Pharmaceuticals, Inc., Daiichi Sankyo Company, Limited, Eli Lilly and Company, Merck Sharp & Dohme Corp., Mitsubishi Tanabe Pharma Corporation, Novo Nordisk A/S, Ono Pharmaceutical Co., Ltd., Sanofi, Takeda Pharmaceutical Company Limited, Terumo Medical Corporation. Other Relationship; Self; Boehringer Ingelheim Pharmaceuticals, Inc., Kowa Pharmaceutical Europe Co. Ltd., Merck Sharp & Dohme Corp., Mitsubishi Tanabe Pharma Corporation, Ono Pharmaceutical Co., Ltd., Sanwa Chemical Industry Co. Ltd., Takeda Pharmaceutical Company Limited.
Published: 2019
Full Text: View/download PDF

9. Molecular mechanisms of Streptococcus pneumoniae ‐targeted autophagy via pneumolysin, Golgi‐resident Rab41, and Nedd4‐1‐mediated K63‐linked ubiquitination

Author: Toshiyuki Yamaji, Ryuta Matsuda, Mitsutaka Yoshida, Akihide Ryo, Makoto Ohnishi, Masahiro Yamamoto, Shouji Yamamoto, Naoki Takada, Masato Koike, Mitsunori Fukuda, Miyo Murai, Yuko Yoshikawa, Hiroshi Kawabe, Mikado Tomokiyo, Hidetoshi Morita, Haruko Takeyama, Isei Tanida, Toru Yanagawa, Michinaga Ogawa, Jun-Lin Guan, Jun-ichiro Inoue, and Sayaka Shizukusihi
Subjects: 0301 basic medicine, Nedd4 Ubiquitin Protein Ligases, Immunology, NEDD4, macromolecular substances, Biology, medicine.disease_cause, Microbiology, Cell Line, 03 medical and health sciences, symbols.namesake, Bacterial Proteins, Ubiquitin, Virology, Streptococcus pneumoniae, Autophagy, medicine, Animals, Humans, Polyubiquitin, Pneumolysin, Ubiquitination, Epithelial Cells, Golgi apparatus, Cell biology, Ubiquitin ligase, 030104 developmental biology, rab GTP-Binding Proteins, Streptolysins, symbols, biology.protein, Intracellular
Abstract: Streptococcus pneumoniae is the most common causative agent of community-acquired pneumonia and can penetrate epithelial barriers to enter the bloodstream and brain. We investigated intracellular fates of S. pneumoniae and found that the pathogen is entrapped by selective autophagy in pneumolysin- and ubiquitin-p62-LC3 cargo-dependent manners. Importantly, following induction of autophagy, Rab41 was relocated from the Golgi apparatus to S. pneumoniae-containing autophagic vesicles (PcAV), which were only formed in the presence of Rab41-positive intact Golgi apparatuses. Moreover, subsequent localization and regulation of K48- and K63-linked polyubiquitin chains in and on PcAV were clearly distinguishable from each other. Finally, we found that E3 ligase Nedd4-1 was recruited to PcAV and played a pivotal role in K63-linked polyubiquitin chain (K63Ub) generation on PcAV, promotion of PcAV formation, and elimination of intracellular S. pneumoniae. These findings suggest that Nedd4-1-mediated K63Ub deposition on PcAV acts as a scaffold for PcAV biogenesis and efficient elimination of host cell-invaded pneumococci.
Published: 2018
Full Text: View/download PDF

10. 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
Full Text: View/download PDF

11. Use of pHlurorin-mKate2-human LC3 to Monitor Autophagic Responses

Author: Isei Tanida, Yasuo Uchiyama, and Takashi Ueno
Subjects: 0301 basic medicine, Cathepsin, Autophagosome, 030102 biochemistry & molecular biology, Autolysosome, Mutant, Autophagy, Biology, Fluorescence, Green fluorescent protein, Cell biology, 03 medical and health sciences, 030104 developmental biology, Lysosomal proteases
Abstract: In this chapter, we introduce the usage of pHluorin-mKate2-human LC3 for monitoring autophagy. Using EGFP and RFP, tandem fluorescent protein-tagged LC3 has been generated for monitoring autophagic structures. A critical point for this purpose is the sensitivity of the green fluorescent protein to acidic pH. A super-ecliptic pHluorin is most sensitive to acidic pH among EGFP, mWasabi, and pHluorin, indicating pHluorin is most suitable for monitoring autophagic structures. During autophagy, green-positive and red-positive fluorescent puncta of pHluorin-mKate2-human LC3 indicate signals of preautophagosomes and autophagosomes. After fusion of autophagosomes with lysosomes to form autolysosomes, green fluorescence of this intraautophagosomal protein is abolished according to acidification of autolysosomes. Therefore, these green-negative and red-positive fluorescent puncta reflect autolysosomes, in which intraluminal proteins are finally degraded by lysosomal proteases. To monitor autophagic flux, the accumulation of its green-negative and red-positive fluorescent puncta is monitored by inhibiting major lysosomal proteases, cathepsins. In addition, a mutant pHluorin-mKate2-human LC3△G is also introduced as a negative control probe.
Published: 2017
Full Text: View/download PDF

12. Techniques for Studying Autophagy

Author: Isei Tanida and Masato Koike
Subjects: Chemistry, Microscopy, Autophagy, Ultrastructure, Flux (metabolism), Cell biology
Published: 2014
Full Text: View/download PDF

13. Autophagy Deficiency in Renal Proximal Tubular Cells Leads to an Increase in Cellular Injury and Apoptosis under Normal Fed Conditions

Author: Juan Alejandro Oliva Trejo, Isei Tanida, Soichiro Kakuta, Chigure Suzuki, and Yasuo Uchiyama
Subjects: 0301 basic medicine, Autophagosome, Aging, Pathology, 030232 urology & nephrology, Apoptosis, urologic and male genital diseases, Kidney, Autophagy-Related Protein 7, lcsh:Chemistry, Kidney Tubules, Proximal, renal proximal tubular cell, Mice, 0302 clinical medicine, gene knockout mouse, Sequestosome-1 Protein, Hepatitis A Virus Cellular Receptor 1, lcsh:QH301-705.5, Spectroscopy, Mice, Knockout, education.field_of_study, TUNEL assay, Chemistry, Acute kidney injury, General Medicine, Computer Science Applications, medicine.anatomical_structure, Knockout mouse, Atg7, Microtubule-Associated Proteins, autophagy, medicine.medical_specialty, Article, Catalysis, Inorganic Chemistry, 03 medical and health sciences, Sequestosome 1, medicine, Animals, Physical and Theoretical Chemistry, education, Molecular Biology, atg7, urogenital system, Organic Chemistry, Autophagy, medicine.disease, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999
Abstract: Renal proximal tubular epithelial cells are significantly damaged during acute kidney injury. Renal proximal tubular cell-specific autophagy-deficient mice show increased sensitivity against renal injury, while showing few pathological defects under normal fed conditions. Considering that autophagy protects the proximal tubular cells from acute renal injury, it is reasonable to assume that autophagy contributes to the maintenance of renal tubular cells under normal fed conditions. To clarify this possibility, we generated a knock out mouse model which lacks Atg7, a key autophagosome forming enzyme, in renal proximal tubular cells (Atg7flox/flox, KAP-Cre+). Analysis of renal tissue from two months old Atg7flox/flox, KAP-Cre+ mouse revealed an accumulation of LC3, binding protein p62/sequestosome 1 (a selective substrate for autophagy), and more interestingly, Kim-1, a biomarker for early kidney injury, in the renal proximal tubular cells under normal fed conditions. TUNEL (TdT-mediated dUTP Nick End Labeling)-positive cells were also detected in the autophagy-deficient renal tubular cells. Analysis of renal tissue from Atg7flox/flox, KAP-Cre+ mice at different age points showed that tubular cells positive for p62 and Kim-1 continually increase in number in an age-dependent manner. Ultrastructural analysis of tubular cells from Atg7flox/flox, KAP-Cre+ revealed the presence of intracellular inclusions and abnormal structures. These results indicated that autophagy-deficiency in the renal proximal epithelial tubular cells leads to an increase in injured cells in the kidney even under normal fed conditions.
Published: 2019
Full Text: View/download PDF

14. Phospholipase C-related catalytically inactive protein, a novel microtubule-associated protein 1 light chain 3-binding protein, negatively regulates autophagosome formation

Author: Akiko Mizokami, Masato Hirata, Takashi Kanematsu, Kae Harada, Hiroshi Takeuchi, Miho Matsuda, Isei Tanida, and Hisanori Umebayashi
Subjects: Immunoprecipitation, Molecular Sequence Data, Biophysics, Phospholipase, Biochemistry, Catalysis, Green fluorescent protein, Mice, Phagosomes, Autophagy, Animals, Amino Acid Sequence, Molecular Biology, Cells, Cultured, Adaptor Proteins, Signal Transducing, Mice, Knockout, biology, Phospholipase C, Binding protein, Membrane Proteins, Cell Biology, Fibroblasts, Cell biology, Cytoskeletal Proteins, Type C Phospholipases, biology.protein, Apoptosis Regulatory Proteins, Protein A, Microtubule-Associated Proteins, Intracellular
Abstract: Upon starvation, cells undergo autophagy, an intracellular bulk-degradation process, to provide the required nutrients. Here, we observed that phospholipase C-related catalytically inactive protein (PRIP) binds to microtubule-associated protein 1 light chain 3 (LC3), a mammalian autophagy-related initiator that regulates the autophagy pathway. Then, we examined the involvement of PRIP in the nutrient depletion-induced autophagy pathway. Enhanced colocalization of PRIP with LC3 was clearly seen in nutrient-starved mouse embryonic fibroblasts under a fluorescent microscope, and interaction of the proteins was revealed by immunoprecipitation experiments with an anti-LC3 antibody. Under starvation conditions, there were more green fluorescent protein fused-LC3 dots in mouse embryonic fibroblasts from PRIP-deficient mice than in fibroblasts from wild type cells. The formation of new dots in a single cell increased, as assessed by time-lapse microscopy. Furthermore, the increase in autophagosome formation in PRIP-deficient cells was notably inhibited by exogenously overexpressed PRIP. Taken together, PRIP is a novel LC3-binding protein that acts as a negative modulator of autophagosome formation.
Published: 2013
Full Text: View/download PDF

15. Doxorubicin-induced glomerulosclerosis with proteinuria in GFP-GABARAP transgenic mice

Author: Isei Tanida, Etsuko Asanuma, Takashi Ueno, Kanae Nonaka, Miyuki Takagi-Akiba, Juan Alejandro Oliva Trejo, Katsuhiko Asanuma, Yasuhiko Tomino, Norihiro Tada, and Eiki Kominami
Subjects: Male, Genetically modified mouse, Physiology, Transgene, GABARAP, Green Fluorescent Proteins, Mice, Transgenic, Biology, Nephropathy, Podocyte, Mice, Pregnancy, Autophagy, medicine, Animals, Mice, Inbred BALB C, Kidney, Antibiotics, Antineoplastic, Glomerulosclerosis, Focal Segmental, Podocytes, Membrane Proteins, Glomerulosclerosis, medicine.disease, Mice, Inbred C57BL, Cytoskeletal Proteins, Disease Models, Animal, Proteinuria, medicine.anatomical_structure, Doxorubicin, Mice, Inbred DBA, Immunology, Cancer research, Female, Apoptosis Regulatory Proteins, Microtubule-Associated Proteins, Transcription Factor TFIIH, Transcription Factors
Abstract: Autophagy is a process of cellular degradation, and its dysfunction elicits many pathological symptoms. However, the contribution of autophagy to kidney glomerular function has not been fully clarified. We previously reported that LC3, a promising executor of autophagy, played an important role in recovery from podocyte damage in an experimental nephrosis model (Asanuma K, Tanida I, Shirato I, Ueno T, Takahara H, Nishitani T, Kominami E, Tomino Y. FASEB J 17: 1165–1167, 2003). γ-Aminobutyric acid A receptor-associated protein (GABARAP), has recently been characterized as another homolog of LC3, although its precise role in autophagy remains unclear. We recently generated green fluorescent protein (GFP)-GABARAP transgenic mice, in which GFP-GABARAP is abundantly expressed in glomerular podocytes. We found that the transgenic mice showed no obvious phenotype, and podocytes isolated from these mice manifested autophagic activity almost equivalent to that of wild-type mice when measured in vitro. Surprisingly, a single injection of doxorubicin caused a greater increase in proteinuria and sclerotic glomeruli in transgenic mice compared with wild-type mice. Under these conditions, neither GFP-GABARAP nor endogenous GABARAP appeared to be recruited to autophagosomes, and both remained in the cytosol. Moreover, the cytosolic GFP-GABARAP was significantly colocalized with p62 to form aggregates. These results indicate that the GFP-GABARAP/p62 complex is responsible for impairment of glomerular function and that it retards recovery from the effects of doxorubicin.
Published: 2012
Full Text: View/download PDF

16. The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation

Author: Manabu Yamasaki, Takashi Ueno, Masaaki Komatsu, and Isei Tanida
Subjects: Microtubule-associated protein, Ubiquitin-activating enzyme, Amino Acid Motifs, Molecular Sequence Data, Mutant, Lipid-anchored protein, Ubiquitin-Activating Enzymes, Plasma protein binding, Biology, Ubiquitin-conjugating enzyme, Autophagy-Related Protein 7, Autophagy-Related Protein 5, Substrate Specificity, Mice, Structure-Activity Relationship, Autophagy, Animals, Humans, Amino Acid Sequence, Molecular Biology, Peptide sequence, Cell Biology, Lipid Metabolism, Molecular biology, Mutation, Ubiquitin-Conjugating Enzymes, embryonic structures, Small Ubiquitin-Related Modifier Proteins, Mutant Proteins, Protein Multimerization, biological phenomena, cell phenomena, and immunity, Microtubule-Associated Proteins, Autophagy-Related Protein 12, Protein Binding
Abstract: ATG7 is an autophagy-related E1-like enzyme that is essential for two ubiquitination-like reactions, ATG12-conjugation and LC3-lipidation. The existence of functional sequences at the amino-terminal region of human ATG7 remains uncertain. Mutational analyses of ATG7 revealed that both mutant ATG7ΔFAP lacking the FAP motif and ATG7FAPtoDDD, in which the Phe15-Ala16-Pro17 sequence was changed to Asp-Asp-Asp, could not complement defects in endogenous ATG12-conjugation and LC3-lipidation when expressed in Atg7-deficient mouse embryonic fibroblasts (MEFs). However, wild-type ATG7 complemented the defects in these cells. Overexpression of GFP-ATG10 and GFP-ATG12 rescued a defect in ATG12-conjugation in Atg7-deficient MEFs expressing mutant ATG7ΔFAP and ATG7FAPtoDDD, whereas overexpression of all ATG proteins related to ATG12-conjugation and LC3-lipidation could not rescue a defect in LC3-lipidation in Atg7-deficient MEFs expressing these ATG7 mutants. Both ATG7ΔFAP and ATG7FAPtoDDD mutants showed severe defects in the formation of an E2-substrate intermediate of ATG3 with LC3 in LC3-lipidation, but were able to form an E1-substrate intermediate of ATG7 with LC3 and the E1- and E2-substrate intermediates in ATG12-conjugation with reduced efficiency. These ATG7 mutants could also form the ATG12-ATG3 conjugate. Co-immunoprecipitation experiments revealed that the FAP motif of ATG7 is essential for the interaction of ATG7 with ATG3, but not for ATG7-homodimerization. These results indicated that the FAP motif of ATG7 is indispensable for formation of the ATG3-LC3 E2-substrate intermediate through the interaction of ATG7 with ATG3.
Published: 2012
Full Text: View/download PDF

17. Hepatic steatosis inhibits autophagic proteolysis via impairment of autophagosomal acidification and cathepsin expression

Author: Kenichi Ikejima, Kousuke Izumi, Sumio Watanabe, Isei Tanida, Takashi Ueno, Shunhei Yamashina, and Yoshihiro Inami
Subjects: Male, Autophagosome, Biophysics, Cellular homeostasis, Biology, Protein degradation, Biochemistry, Cathepsin B, Mice, Phagosomes, Lysosome, Autophagy, medicine, Animals, Molecular Biology, Cathepsin, Proteins, Lipid metabolism, Cell Biology, Hydrogen-Ion Concentration, Cathepsins, Cell biology, Fatty Liver, Mice, Inbred C57BL, medicine.anatomical_structure, Hepatocytes, Acids
Abstract: Autophagy, one of protein degradation system, contributes to maintain cellular homeostasis and cell defense. Recently, some evidences indicated that autophagy and lipid metabolism are interrelated. Here, we demonstrate that hepatic steatosis impairs autophagic proteolysis. Though accumulation of autophagosome is observed in hepatocytes from ob/ob mice, expression of p62 was augmented in liver from ob/ob mice more than control mice. Moreover, degradation of the long-lived protein leucine was significantly suppressed in hepatocytes isolated from ob/ob mice. More than 80% of autophagosomes were stained by LysoTracker Red (LTR) in hepatocytes from control mice; however, rate of LTR-stained autophagosomes in hepatocytes were suppressed in ob/ob mice. On the other hand, clearance of autolysosomes loaded with LTR was blunted in hepatocytes from ob/ob mice. Although fusion of isolated autophagosome and lysosome was not disturbed, proteinase activity of cathepsin B and L in autolysosomes and cathepsin B and L expression of liver were suppressed in ob/ob mice. These results indicate that lipid accumulation blunts autophagic proteolysis via impairment of autophagosomal acidification and cathepsin expression.
Published: 2011
Full Text: View/download PDF

18. Autophagosome Formation and Molecular Mechanism of Autophagy

Author: Isei Tanida
Subjects: Autophagosome, Atg1, Physiology, ATG8, Clinical Biochemistry, Biology, Endoplasmic Reticulum, Biochemistry, ATG12, Phagosomes, Autophagy, Animals, Humans, Molecular Biology, General Environmental Science, Endoplasmic reticulum, Cell Membrane, Cell Biology, Cell biology, Oxidative Stress, Multiprotein Complexes, General Earth and Planetary Sciences, Rab, Lysosomes, Intracellular
Abstract: Autophagy (macroautophagy), or the degradation of large numbers of cytoplasmic components, is induced by extracellular and intracellular signals, including oxidative stress, ceramide, and endoplasmic reticulum stress. This dynamic process involves membrane formation and fusion, including autophagosome formation, autophagosome-lysosome fusion, and the degradation of intra-autophagosomal contents by lysosomal hydrolases. Autophagy is associated with tumorigenesis, neurodegenerative diseases, cardiomyopathy, Crohn's disease, fatty liver, type II diabetes, defense against intracellular pathogens, antigen presentation, and longevity. Among the proteins and multimolecular complexes that contribute to autophagosome formation are the PI(3)-binding proteins, the PI3-phosphatases, the Rab proteins, the Atg1/ULK1 protein-kinase complex, the Atg9•Atg2-Atg18 complex, the Vps34-Atg6/beclin1 class III PI3-kinase complex, and the Atg12 and Atg8/LC3 conjugation systems. Two ubiquitin-like modifications, the Atg12 and LC3 conjugations, are essential for membrane elongation and autophagosome formation. Recent findings have revealed that processes of selective autophagy, including pexophagy, mitophagy, ERphagy (reticulophagy), and the p62-dependent degradation of ubiquitin-positive aggregates, are physiologically important in various disease states, whereas "classical" autophagy is considered nonselective degradation. Processes of selective autophagy require specific Atg proteins in addition to the "core" Atg complexes. Finally, methods to monitor autophagic activity in mammalian cells are described.
Published: 2011
Full Text: View/download PDF

19. Autophagy basics

Author: Isei Tanida
Subjects: ATG12, Virology, Immunology, Autophagy, Biology, Microbiology, Cell biology
Published: 2010
Full Text: View/download PDF

20. Inhibition of hepatitis C virus replication by chloroquine targeting virus-associated autophagy

Author: Yoshiyuki Takei, Takashi Ueno, Tatsuo Sakai, Isei Tanida, Shunhei Yamashina, Kenichi Ikejima, Nobuyuki Enomoto, Sumio Watanabe, Tsuneo Kitamura, Tomokazu Mizui, Naoya Sakamoto, and Eiki Kominami
Subjects: Autophagosome, viruses, Hepatitis C virus, ATG5, Hepacivirus, HCV replicon, Transfection, Virus Replication, medicine.disease_cause, Antiviral Agents, Viral Proteins, Drug Delivery Systems, Interferon, Cell Line, Tumor, Autophagy, medicine, Humans, Replicon, RNA, Small Interfering, Original Article—Liver, Pancreas, and Biliary Tract, Dose-Response Relationship, Drug, Chemistry, Gastroenterology, Interferon-alpha, virus diseases, Chloroquine, Drug Synergism, biochemical phenomena, metabolism, and nutrition, Virology, Protein kinase R, digestive system diseases, Viral replication, Drug Therapy, Combination, medicine.drug
Abstract: Background Autophagy has been reported to play a pivotal role on the replication of various RNA viruses. In this study, we investigated the role of autophagy on hepatitis C virus (HCV) RNA replication and demonstrated anti-HCV effects of an autophagic proteolysis inhibitor, chloroquine. Methods Induction of autophagy was evaluated following the transfection of HCV replicon to Huh-7 cells. Next, we investigated the replication of HCV subgenomic replicon in response to treatment with lysosomal protease inhibitors or pharmacological autophagy inhibitor. The effect on HCV replication was analyzed after transfection with siRNA of ATG5, ATG7 and light-chain (LC)-3 to replicon cells. The antiviral effect of chloroquine and/or interferon-α (IFNα) was evaluated. Results The transfection of HCV replicon increased the number of autophagosomes to about twofold over untransfected cells. Pharmacological inhibition of autophagic proteolysis significantly suppressed expression level of HCV replicon. Silencing of autophagy-related genes by siRNA transfection significantly blunted the replication of HCV replicon. Treatment of replicon cells with chloroquine suppressed the replication of the HCV replicon in a dose-dependent manner. Furthermore, combination treatment of chloroquine to IFNα enhanced the antiviral effect of IFNα and prevented re-propagation of HCV replicon. Protein kinase R was activated in cells treated with IFNα but not with chloroquine. Incubation with chloroquine decreased degradation of long-lived protein leucine. Conclusion The results of this study suggest that the replication of HCV replicon utilizes machinery involving cellular autophagic proteolysis. The therapy targeted to autophagic proteolysis by using chloroquine may provide a new therapeutic option against chronic hepatitis C.
Published: 2009
Full Text: View/download PDF

21. Characterization of CAA0225, a Novel Inhibitor Specific for Cathepsin L, as a Probe for Autophagic Proteolysis

Author: Eiki Kominami, Takashi Ueno, Isei Tanida, Mitsuo Murata, Katsuyuki Takahashi, and Naoko Minematsu-Ikeguchi
Subjects: Ethylene Oxide, Male, Cytoplasm, Cathepsin L, Phenylalanine, Pharmaceutical Science, Cathepsin E, In Vitro Techniques, Biology, Cathepsin A, Cathepsin B, Cell Line, Cathepsin C, Mice, Structure-Activity Relationship, Cathepsin O, Cathepsin H, Cathepsin L1, Benzyl Compounds, Autophagy, Animals, Humans, Rats, Wistar, Adaptor Proteins, Signal Transducing, Pharmacology, Hydrolysis, Stereoisomerism, Dipeptides, General Medicine, Cathepsins, Molecular biology, Rats, Mice, Inbred C57BL, Cysteine Endopeptidases, Biochemistry, biology.protein, Epoxy Compounds, Apoptosis Regulatory Proteins, Lysosomes, Microtubule-Associated Proteins
Abstract: We screened a series of new epoxysuccinyl peptides for the development of a lysosomal cathepsin L-specific inhibitor. Among the compounds tested, (2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide] 3-{[2-(4-hydroxy-phenyl)-ethyl]-amide} (compound CAA0225) was the most potent inhibitor of cathepsin L. CAA0225 inhibited rat liver cathepsin L with IC50 values of 1.9 nM, but not rat liver cathepsin B (IC50, >1000-5000 nM). To assess the contribution of cathepsin L to lysosomal proteolysis, we evaluated autophagy, which is the process of lysosomal self-degradation of cell constituents. In HeLa and Huh-7 cells cultured under nutrient-deprived conditions CAA0225 significantly inhibited degradation of long-lived proteins; however, the magnitude of inhibition was comparable to that in the presence of CA-074-OMe, which is a cathepsin B-specific inhibitor. Thus the contributions of cathepsin L and cathepsin B to autophagic protein degradation of cytoplasmic proteins are nearly equal. During autophagy, microtubule-associated protein IA/IB light chain 3-II (LC3-II) and gamma-aminobutyric acid (A) receptor-associated protein (GABARAP)-II, which are specific markers of autophagosomal membranes that engulf cytoplasmic components, also undergo degradation upon fusion of autophagosomes with lysosomes. CAA0225 effectively inhibited degradation of LC3-II and GABARAP, whereas CA-074-OMe had only a marginal effect on their levels. Therefore we conclude that cathepsin L does not play a general role in the degradation of proteins in the lumen of autophagosomes, but rather is involved specifically in the degradation of autophagosomal membrane markers.
Published: 2009
Full Text: View/download PDF

22. Consideration about negative controls for LC3 and expression vectors for four colored fluorescent protein-LC3 negative controls

Author: Kentaro Hanada, Isei Tanida, Takashi Ueno, Shoichi Ishiura, Eiki Kominami, and Toshiyuki Yamaji
Subjects: chemistry.chemical_classification, Expression vector, Recombinant Fusion Proteins, Genetic Vectors, Autophagy, Mutant, Cell Biology, Biology, Molecular biology, Green fluorescent protein, Luminescent Proteins, Cytosol, Plasmid, Enzyme, chemistry, Reference Values, embryonic structures, Animals, Humans, biological phenomena, cell phenomena, and immunity, Microtubule-Associated Proteins, Molecular Biology, Intracellular
Abstract: A cytosolic form of LC3 is conjugated to phosphatidylethanolamine by Atg7, an E1-like enzyme, and Atg3, an E2-like enzyme, during autophagy. To monitor intracellular autophagosomes and autolysosomes, GFP-LC3 is a useful tool. However, GFP-LC3 can aggregate without being conjugated to phosphatidylethanolamine, especially when GFP-LC3 is transiently expressed (Kuma A, Matsui M, Mizushima N. Autophagy 2007; 3:323-8). Therefore, as a negative control, we investigated a mutant human LC3DeltaG protein in which the C-terminal Gly(120) essential for LC3-lipidation is deleted, and generated a set of expression plasmids for wild-type human LC3 and mutant LC3DeltaG fused to either CFP, GFP, YFP, or HcRed at the N terminus. We found that the mutant LC3DeltaG protein does not react with human Atg7 and Atg3, indicating that LC3-lipidation does not occur, and few puncta containing mutant LC3DeltaG form under starvation conditions. As observed with wildtype HcRed-LC3, mutant HcRed-LC3DeltaG also co-localizes with polyQ150-aggregates suggesting that the colocalization of HcRed- LC3 to polyQ150-aggregates is independent of LC3-lipidation. These mutant LC3DeltaG proteins will be useful negative controls in recognizing non-specific fluorescent protein-LC3 aggregates.
Published: 2008
Full Text: View/download PDF

23. Macroautophagy is essential for killing of intracellular Burkholderia pseudomallei in human neutrophils

Author: Manabu Ato, Isei Tanida, Michinaga Ogawa, Yasuo Uchiyama, Joanne M. Stevens, Richard W. Titball, Donporn Riyapa, Darawan Rinchai, Surachat Buddhisa, Mark P. Stevens, Kusumawadee Utispan, Masato Koike, and Ganjana Lertmemongkolchai
Subjects: Melioidosis, Burkholderia pseudomallei, Neutrophils, Intracellular Space, Cytoplasmic Granules, Type three secretion system, Microbiology, Cytosol, Phagosomes, medicine, Translational Brief Report, Autophagy, Humans, Secretion, Molecular Biology, Bacterial Secretion Systems, Phagosome, Cathepsin, Microbial Viability, biology, Lysosome-Associated Membrane Glycoproteins, Cell Biology, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, medicine.disease, bacterial infections and mycoses, Burkholderia, bacteria, Lysosomes, Microtubule-Associated Proteins, Intracellular, Biomarkers
Abstract: Neutrophils play a key role in the control of Burkholderia pseudomallei, the pathogen that causes melioidosis. Here, we show that survival of intracellular B. pseudomallei was significantly increased in the presence of 3-methyladenine or lysosomal cathepsin inhibitors. The LC3-flux was increased in B. pseudomallei-infected neutrophils. Concordant with this result, confocal microscopy analyses using anti-LC3 antibodies revealed that B. pseudomallei-containing phagosomes partially overlapped with LC3-positive signal at 3 and 6 h postinfection. Electron microscopic analyses of B. pseudomallei-infected neutrophils at 3 h revealed B. pseudomallei-containing phagosomes that occasionally fused with phagophores or autophagosomes. Following infection with a B. pseudomallei mutant lacking the Burkholderia secretion apparatus Bsa Type III secretion system, neither this characteristic structure nor bacterial escape into the cytosol were observed. These findings indicate that human neutrophils are able to recruit autophagic machinery adjacent to B. pseudomallei-containing phagosomes in a Type III secretion system-dependent manner.
Published: 2015

24. Lysosomal Turnover of GABARAP-Phospholipid Conjugate is Activated During Differentiation of C2C12 Cells to Myotubes without Inactivation of the mTor Kinase-Signaling Pathway

Author: Eiki Kominami, Isei Tanida, Mika Wakabayashi, Takashi Ueno, Yu-shin Sou, Masato Hirata, Naoko Minematsu-Ikeguchi, and Takashi Kanematsu
Subjects: Male, Recombinant Fusion Proteins, GABARAP, Muscle Fibers, Skeletal, Phospholipid, Endogeny, Biology, Cell Line, Mice, chemistry.chemical_compound, Autophagy, Animals, Humans, Tissue Distribution, Molecular Biology, Phospholipids, PI3K/AKT/mTOR pathway, Adaptor Proteins, Signal Transducing, Sirolimus, Antibiotics, Antineoplastic, Myogenesis, TOR Serine-Threonine Kinases, HEK 293 cells, Membrane Proteins, Cell Differentiation, Cell Biology, Cell biology, Cytoskeletal Proteins, Biochemistry, chemistry, Starvation, Apoptosis Regulatory Proteins, Lysosomes, Microtubule-Associated Proteins, Protein Kinases, C2C12, Signal Transduction
Abstract: Although conjugation of overexpressed GABARP to phospholipid has been reported during starvation-induced autophagy, it is unclear whether endogenous GABARAP-phospholipid conjugation is also activated under starvation conditions. We observed little accumulation of GABARAP-phospholipid conjugate (GABARAP-PL) in mouse liver and kidney under starvation conditions, whereas endogenous LC3-phospholipid conjugate (LC3-II) accumulated. A small amount of endogenous GABARAP-PL was observed in the heart, independent of starvation. In rapamycin-treated HEK293 cells, there was little accumulation of endogenous GABARAP-PL, even in the presence of lysosomal protease-inhibitors, whereas there was significant accumulation of endogenous LC3-II, together with inactivation of the mTor kinase-signaling pathway. In HeLa and C2C12 cells, GABARAP-PL accumulation in the presence of lysosomal protease inhibitors was independent of starvation-induced autophagy, whereas LC3-II accumulation was significant during starvation-induced autophagy. Interestingly, we observed activation of lysosomal turnover of GABARAP-PL during the differentiation of C2C12 cells to myotubes, along with increased lysosomal turnover of LC3-II. Under these conditions, S6 ribosomal protein was still phosphorylated, suggesting that the mTor kinase-signaling pathway is active during the differentiation of C2C12 cells to myotubes, in contrast to starvation-induced autophagy. These results indicated that lysosomal turnover of GABARAP-PL was activated during the differentiation of C2C12 cells to myotubes without inactivation of the mTor kinase-signaling pathway, whereas little lysosomal turnover of GABARAP-PL was activated during starvation-induced autophagy.
Published: 2006
Full Text: View/download PDF

25. Excess Peroxisomes Are Degraded by Autophagic Machinery in Mammals

Author: Junji Ezaki, Masaaki Komatsu, Sadaki Yokota, Isei Tanida, Takashi Ueno, Keiji Tanaka, Tomoki Chiba, Junichi Iwata, and Eiki Kominami
Subjects: Male, Autophagy, Mutant, Phthalate, Cell Biology, Biology, Peroxisome, Peroxisome degradation, Autophagy-Related Protein 7, Biochemistry, Yeast, Mice, Inbred C57BL, Mice, chemistry.chemical_compound, Liver, chemistry, Essential gene, Diethylhexyl Phthalate, Peroxisomes, Animals, Microtubule-Associated Proteins, Molecular Biology
Abstract: Peroxisomes are degraded by autophagic machinery termed "pexophagy" in yeast; however, whether this is essential for peroxisome degradation in mammals remains unknown. Here we have shown that Atg7, an essential gene for autophagy, plays a pivotal role in the degradation of excess peroxisomes in mammals. Following induction of peroxisomes by a 2-week treatment with phthalate esters in control and Atg7-deficient livers, peroxisomal degradation was monitored within 1 week after discontinuation of phthalate esters. Although most of the excess peroxisomes in the control liver were selectively degraded within 1 week, this rapid removal was exclusively impaired in the mutant liver. Furthermore, morphological analysis revealed that surplus peroxisomes, but not mutant hepatocytes, were surrounded by autophagosomes in the control. Our results indicated that the autophagic machinery is essential for the selective clearance of excess peroxisomes in mammals. This is the first direct evidence for the contribution of autophagic machinery in peroxisomal degradation in mammals.
Published: 2006
Full Text: View/download PDF

26. Lysosomal Turnover, but Not a Cellular Level, of Endogenous LC3 is a Marker for Autophagy

Author: Isei Tanida, Takashi Ueno, Naoko Minematsu-Ikeguchi, and Eiki Kominami
Subjects: Hydrolases, Biological Transport, Active, Endogeny, Cellular level, Cell Line, HeLa, chemistry.chemical_compound, Microscopy, Electron, Transmission, Leucine, Phagosomes, Pepstatins, Autophagy, Humans, Molecular Biology, Lysosomal proteases, Mannose 6-phosphate receptor, biology, HEK 293 cells, Cell Biology, biology.organism_classification, Cell biology, chemistry, Biochemistry, embryonic structures, biological phenomena, cell phenomena, and immunity, Lysosomes, Microtubule-Associated Proteins, Biomarkers, Pepstatin
Abstract: During starvation-induced autophagy in mammals, autophagosomes form and fuse with lysosomes, leading to the degradation of the intra-autophagosomal contents by lysosomal proteases. During the formation of autophagosomes, LC3 is lipidated, and this LC3-phospholipid conjugate (LC3-II) is localized on autophagosomes and autolysosomes. While intra-autophagosomal LC3-II may be degraded by lysosomal hydrolases, recent studies have regarded LC3-II accumulation as marker of autophagy. The effect of lysosomal turnover of endogenous LC3-II in this process, however, has not been considered. We therefore investigated the lysosomal turnover of endogenous LC3-II during starvation-induced autophagy using E64d and pepstatin A, which inhibit lysosomal proteases, including cathepsins B, D and L. We found that endogenous LC3-II significantly accumulated in the presence of E64d and pepstatin A under starvation conditions, increasing about 3.5 fold in HEK293 cells and about 6.7 fold in HeLa cells compared with that in their absence, whereas the amount of LC3-II in their absence is cell-line dependent. Morphological analyses indicated that endogenous LC3-positive puncta and autolysosomes increased in HeLa cells under starvation conditions in the presence of these inhibitors. These results indicate that endogenous LC3-II is considerably degraded by lysosomal hydrolases after formation of autolysosomes, and suggest that lysosomal turnover, not a transient amount, of this protein reflects starvation-induced autophagic activity.
Published: 2005
Full Text: View/download PDF

27. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice

Author: Yoshinori Ohsumi, Noboru Mizushima, Takashi Ueno, Yasuo Uchiyama, Masaaki Komatsu, Junji Ezaki, Tomoki Chiba, Isei Tanida, Shigeo Murata, Eiki Kominami, Satoshi Waguri, Junichi Iwata, and Keiji Tanaka
Subjects: Programmed cell death, Saccharomyces cerevisiae Proteins, Biology, Protein degradation, Autophagy-Related Protein 7, Article, Cell Line, Mice, Lysosome, medicine, Autophagy, Animals, ATG16L1, Research Articles, Inclusion Bodies, Mice, Knockout, Organelles, Autophagy database, Ubiquitin, Cell Biology, Intracellular Membranes, Cell biology, Mitochondria, medicine.anatomical_structure, Phenotype, Biochemistry, Animals, Newborn, Liver, Starvation, Hepatocytes, Starvation response, Microtubule-Associated Proteins, Hepatomegaly
Abstract: Autophagy is a membrane-trafficking mechanism that delivers cytoplasmic constituents into the lysosome/vacuole for bulk protein degradation. This mechanism is involved in the preservation of nutrients under starvation condition as well as the normal turnover of cytoplasmic component. Aberrant autophagy has been reported in several neurodegenerative disorders, hepatitis, and myopathies. Here, we generated conditional knockout mice of Atg7, an essential gene for autophagy in yeast. Atg7 was essential for ATG conjugation systems and autophagosome formation, amino acid supply in neonates, and starvation-induced bulk degradation of proteins and organelles in mice. Furthermore, Atg7 deficiency led to multiple cellular abnormalities, such as appearance of concentric membranous structure and deformed mitochondria, and accumulation of ubiquitin-positive aggregates. Our results indicate the important role of autophagy in starvation response and the quality control of proteins and organelles in quiescent cells.
Published: 2005

28. The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 lipidation, but not for Apg12 conjugation

Author: Takashi Ueno, Eiki Kominami, Harumi Yamazaki-Sato, and Isei Tanida
Subjects: Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Mutant, Saccharomyces cerevisiae, Biophysics, Lipid-anchored protein, Biology, CVT pathway, Ubiquitin-like modification, Aminopeptidases, Autophagy-Related Protein 7, Biochemistry, Structural Biology, Autophagy, Genetics, Amino Acid Sequence, Homodimer, Molecular Biology, chemistry.chemical_classification, Phosphatidylethanolamines, Proteins, Autophagy-Related Protein 8 Family, Cell Biology, biology.organism_classification, Apg8/Aut7 lipidation, Protein Structure, Tertiary, Amino acid, Protein Transport, Enzyme, chemistry, Apg3, Mutation, Apg12–Apg5 conjugate, Apg7, Autophagin, Microtubule-Associated Proteins, Autophagy-Related Protein 12
Abstract: In the yeast, Saccharomyces cerevisiae , two ubiquitin-like modifications, Apg12 conjugation with Apg5 and Apg8 lipidation with phosphatidylethanolamine, are essential for autophagy and the cytoplasm-to-vacuole transport of aminopeptidase I (Cvt pathway). As a unique E1-like enzyme, Apg7 activates two modifiers (Apg12 and Apg8) in an ATP-dependent manner and, for this activity, the carboxyl terminal 40 amino acids are essential. For a better understanding of the function of the carboxyl terminus of Apg7, we performed a sequential deletion of the region. A mutant expressing Apg7ΔC17 protein, which lacks the carboxyl 17 amino acids of Apg7, showed defects in both the Cvt pathway and autophagy. Apg8 lipidation is inhibited in the mutant, while Apg12 conjugation occurs normally. A mutant expressing Apg7ΔC13 protein showed a defect in the Cvt pathway, but not autophagy, suggesting that the activity of Apg7 for Apg8 lipidation is more essential for the Cvt pathway than for autophagy. Mutant Apg7ΔC17 protein is still able to interact with Apg8, Apg12 and Apg3, and forms a homodimer, indicating that the deletion of the carboxyl terminal 17 amino acids has little effect on these interactions and Apg7 dimerization. These results suggest that the carboxyl terminal 17 amino acids of Apg7 play a specific role in Apg8 lipidation indispensable for the Cvt pathway and autophagy.
Published: 2003
Full Text: View/download PDF

29. A super-ecliptic, pHluorin-mKate2, tandem fluorescent protein-tagged human LC3 for the monitoring of mammalian autophagy

Author: Yasuo Uchiyama, Isei Tanida, and Takashi Ueno
Subjects: Fluorescence-lifetime imaging microscopy, Microtubule-associated protein, Imaging Techniques, Science, Recombinant Fusion Proteins, Mutant, Green Fluorescent Proteins, Biology, Research and Analysis Methods, Biochemistry, Green fluorescent protein, Substrate Specificity, Cell Line, Tumor, Fluorescence Imaging, Fluorescence microscope, Autophagy, Animals, Humans, Cell Analysis, Mammals, Multidisciplinary, Biology and Life Sciences, Cell Biology, Hydrogen-Ion Concentration, Fluorescence, Cell biology, Luminescent Proteins, Bioassays and Physiological Analysis, In Vivo Imaging, Cell culture, Medicine, Mutant Proteins, Cellular Structures and Organelles, mCherry, Lysosomes, Acids, Microtubule-Associated Proteins, Research Article
Abstract: Tandem fluorescent protein-tagged LC3s that were comprised of a protein tag that emits green fluorescence (e.g., EGFP or mWasabi) fused with another tag that emits red fluorescence (e.g. mCherry or TagRFP) were used for monitoring the maturation step of mammalian autophagosomes. A critical point for this tandem fluorescent-tagged LC3 was the sensitivity of green fluorescence at an acidic pH. EGFP and mWasabi continue to emit a weak, but significant, fluorescence at a pH of approximately 6. To overcome this issue, we focused on super-ecliptic pHluorin, which is a more pH-sensitive GFP variation. The green fluorescence of EGFP and mWasabi in the cells was still observed at weakly acidic levels (pH 6.0-6.5). In contrast, the fluorescence of pHluorin was more significantly quenched at pH 6.5, and was almost completely abolished at pH 5.5-6.0, indicating that pHluorin is more suitable for use in a tandem fluorescent protein-tag for monitoring autophagy. A pHluorin-mKate2 tandem fluorescence protein showed pH-sensitive green fluorescence and pH-resistant far-red fluorescence. We therefore generated expression plasmids for pHluorin-mKate2-tagged human LC3 (PK-hLC3), which could be used as a modifier for LC3-lipidation. The green and far-red fluorescent puncta of PK-hLC3 were increased under starvation conditions. Puncta that were green-negative, but far-red positive, were increased when autolysosomes accumulated, but few puncta of the mutant PK-hLC3ΔG that lacked the carboxyl terminal Gly essential for autophagy were observed in the cells under the same conditions. These results indicated that the PK-hLC3 were more appropriate for the pH-sensitive monitoring of the maturation step of autophagosomes.
Published: 2014

30. Phospholipase C-related catalytically inactive protein participates in the autophagic elimination of Staphylococcus aureus infecting mouse embryonic fibroblasts

Author: Junzo Hisatsune, Satoshi Asano, Fuminori Kato, Kae Harada-Hada, Takashi Kanematsu, Kana Harada, Masato Hirata, Isei Tanida, Michinaga Ogawa, and Motoyuki Sugai
Subjects: Staphylococcus aureus, Autophagosome maturation, Science, Staphylococcus, Immunology, Vacuole, Biology, Phospholipase, Biochemistry, Microbiology, Mice, Phagosomes, Autophagy, Animals, Microbial Pathogens, Cells, Cultured, Adaptor Proteins, Signal Transducing, Mice, Knockout, Innate Immune System, Multidisciplinary, Innate immune system, Phospholipase C, Signal transducing adaptor protein, Biology and Life Sciences, Transfection, Cell Biology, Fibroblasts, Staphylococcal Infections, Immunity, Innate, Cell biology, Bacterial Pathogens, Medical Microbiology, Immune System, embryonic structures, Medicine, Cellular Structures and Organelles, Lysosomes, Microtubule-Associated Proteins, Research Article
Abstract: Autophagy is an intrinsic host defense system that recognizes and eliminates invading bacterial pathogens. We have identified microtubule-associated protein 1 light chain 3 (LC3), a hallmark of autophagy, as a binding partner of phospholipase C-related catalytically inactive protein (PRIP) that was originally identified as an inositol trisphosphate-binding protein. Here, we investigated the involvement of PRIP in the autophagic elimination of Staphylococcus aureus in infected mouse embryonic fibroblasts (MEFs). We observed significantly more LC3-positive autophagosome-like vacuoles enclosing an increased number of S. aureus cells in PRIP-deficient MEFs than control MEFs, 3 h and 4.5 h post infection, suggesting that S. aureus proliferates in LC3-positive autophagosome-like vacuoles in PRIP-deficient MEFs. We performed autophagic flux analysis using an mRFP-GFP-tagged LC3 plasmid and found that autophagosome maturation is significantly inhibited in PRIP-deficient MEFs. Furthermore, acidification of autophagosomes was significantly inhibited in PRIP-deficient MEFs compared to the wild-type MEFs, as determined by LysoTracker staining and time-lapse image analysis performed using mRFP-GFP-tagged LC3. Taken together, our data show that PRIP is required for the fusion of S. aureus-containing autophagosome-like vacuoles with lysosomes, indicating that PRIP is a novel modulator in the regulation of the innate immune system in non-professional phagocytic host cells.
Published: 2014

31. The Human Homolog of Saccharomyces cerevisiae Apg7p Is a Protein-activating Enzyme for Multiple Substrates Including Human Apg12p, GATE-16, GABARAP, and MAP-LC3

Author: Emiko Tanida-Miyake, Takashi Ueno, Eiki Kominami, and Isei Tanida
Subjects: Male, Autophagosome, Autophagy-Related Protein 8 Family, Saccharomyces cerevisiae Proteins, GABARAP, Molecular Sequence Data, Mutant, Saccharomyces cerevisiae, Vacuole, Biology, Autophagy-Related Protein 7, Biochemistry, Substrate Specificity, Fungal Proteins, Animals, Humans, Amino Acid Sequence, Rats, Wistar, Molecular Biology, Adaptor Proteins, Signal Transducing, DNA Primers, Base Sequence, Sequence Homology, Amino Acid, Microfilament Proteins, Autophagy, Proteins, Cell Biology, biology.organism_classification, Rats, Cell biology, Mutagenesis, Site-Directed, Apoptosis Regulatory Proteins, Carrier Proteins, Microtubule-Associated Proteins
Abstract: Autophagy is a process that involves the bulk degradation of cytoplasmic components by the lysosomal/vacuolar system. In the yeast, Saccharomyces cerevisiae, an autophagosome is formed in the cytosol. The outer membrane of the autophagosome is fused with the vacuole, releasing the inner membrane structure, an autophagic body, into the vacuole. The autophagic body is subsequently degraded by vacuolar hydrolases. Taking advantage of yeast genetics, apg (autophagy-defective) mutants were isolated that are defective in terms of formation of autophagic bodies under nutrient starvation conditions. One of the APG gene products, Apg12p, is covalently attached to Apg5p via the C-terminal Gly of Apg12p as in the case of ubiquitylation, and this conjugation is essential for autophagy. Apg7p is a novel E1 enzyme essential for the Apg12p-conjugation system. In mammalian cells, the human Apg12p homolog (hApg12p) also conjugates with the human Apg5p homolog. In this study, the unique characteristics of hApg7p are shown. A two-hybrid experiment indicated that hApg12p interacts with hApg7p. Site-directed mutagenesis revealed that Cys(572) of hApg7p is an authentic active site cysteine residue essential for the formation of the hApg7p.hApg12p intermediate. Overexpression of hApg7p enhances the formation of the hApg5p.hApg12p conjugate, indicating that hApg7p is an E1-like enzyme essential for the hApg12p conjugation system. Cross-linking experiments and glycerol-gradient centrifugation analysis showed that the mammalian Apg7p homolog forms a homodimer as in yeast Apg7p. Each of three human Apg8p counterparts, i.e. the Golgi-associated ATPase enhancer of 16 kDa, GABA(A) receptor-associated protein, and microtubule-associated protein light chain 3, coimmunoprecipitates with hApg7p and conjugates with mutant hApg7p(C572S) to form a stable intermediate via an ester bond. These results indicate that hApg7p is an authentic protein-activating enzyme for hApg12p and the three Apg8p homologs.
Published: 2001
Full Text: View/download PDF

32. A ubiquitin-like system mediates protein lipidation

Author: Noboru Mizushima, Takeshi Noda, Takayoshi Kirisako, Mariko Ohsumi, Yoshinori Satomi, Eiki Kominami, Isei Tanida, Yoshinobu Ichimura, Naotada Ishihara, Yoshinori Ohsumi, Toshifumi Takao, and Yasutsugu Shimonishi
Subjects: Saccharomyces cerevisiae Proteins, ATG8, Molecular Sequence Data, Autophagy-Related Proteins, Lipid-anchored protein, Saccharomyces cerevisiae, Biology, Protein degradation, Protein lipidation, Autophagy-Related Protein 7, Fungal Proteins, ATG12, Autophagy, Amino Acid Sequence, Ubiquitins, Binding Sites, Multidisciplinary, Phosphatidylethanolamines, Cell Membrane, Autophagy-Related Protein 8 Family, Cell biology, Biochemistry, Ubiquitin-Conjugating Enzymes, Autophagosome membrane, Autophagin, Microtubule-Associated Proteins, Autophagy-Related Protein 12
Abstract: Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole1,2. Apg8/Aut7 is an essential factor for autophagy in yeast3,4,5. We previously found that the carboxy-terminal arginine of nascent Apg8 is removed by Apg4/Aut2 protease, leaving a glycine residue at the C terminus6. Apg8 is then converted to a form (Apg8-X) that is tightly bound to the membrane6. Here we report a new mode of protein lipidation. Apg8 is covalently conjugated to phosphatidylethanolamine through an amide bond between the C-terminal glycine and the amino group of phosphatidylethanolamine. This lipidation is mediated by a ubiquitination-like system. Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7 (refs 7, 8), and is transferred subsequently to the E2 enzymes Apg3/Aut1 (ref. 9). Apg7 activates two different ubiquitin-like proteins, Apg12 (ref. 10) and Apg8, and assigns them to specific E2 enzymes, Apg10 (ref. 11) and Apg3, respectively. These reactions are necessary for the formation of Apg8-phosphatidylethanolamine. This lipidation has an essential role in membrane dynamics during autophagy6.
Published: 2000
Full Text: View/download PDF

33. Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy

Author: Takashi Ueno, Isei Tanida, Noboru Mizushima, Mariko Ohsumi, Yoshinori Ohsumi, Miho Kiyooka, and Eiki Kominami
Subjects: Autophagy-Related Protein 8 Family, Cytoplasm, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, Saccharomyces cerevisiae, Molecular Sequence Data, Biology, Aminopeptidases, Autophagy-Related Protein 7, Article, Autophagy-Related Protein 5, Fungal Proteins, Adenosine Triphosphate, Cytosol, Autophagy, Amino Acid Sequence, Cysteine, Binding site, Molecular Biology, Cytoplasm-to-vacuole targeting, Binding Sites, Base Sequence, Proteins, Cell Biology, biology.organism_classification, Precipitin Tests, Yeast, Biochemistry, Vacuoles, Conjugate
Abstract: In the yeast Saccharomyces cerevisiae, the Apg12p–Apg5p conjugating system is essential for autophagy. Apg7p is required for the conjugation reaction, because Apg12p is unable to form a conjugate with Apg5p in the apg7/cvt2mutant. Apg7p shows a significant similarity to a ubiquitin-activating enzyme, Uba1p. In this article, we investigated the function of Apg7p as an Apg12p-activating enzyme. Hemagglutinin-tagged Apg12p was coimmunoprecipitated with c-myc–tagged Apg7p. A two-hybrid experiment confirmed the interaction. The coimmunoprecipitation was sensitive to a thiol-reducing reagent. Furthermore, a thioester conjugate of Apg7p was detected in a lysate of cells overexpressing both Apg7p and Apg12p. These results indicated that Apg12p interacts with Apg7p via a thioester bond. Mutational analyses of Apg7p suggested that Cys507of Apg7p is an active site cysteine and that both the ATP-binding domain and the cysteine residue are essential for the conjugation of Apg7p with Apg12p to form the Apg12p–Apg5p conjugate. Cells expressing mutant Apg7ps, Apg7pG333A, or Apg7pC507Ashowed defects in autophagy and cytoplasm-to-vacuole targeting of aminopeptidase I. These results indicated that Apg7p functions as a novel protein-activating enzyme necessary for Apg12p–Apg5p conjugation.
Published: 1999

34. MAP‐LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN nephrosis

Author: Isao Shirato, Eiki Kominami, Tomohito Nishitani, Isei Tanida, Yasuhiko Tomino, Katsuhiko Asanuma, Takashi Ueno, and Hisatsugu Takahara
Subjects: Endosome, Nephrosis, Cellular differentiation, Vacuole, Puromycin Aminonucleoside, Biology, Kidney, Models, Biological, Biochemistry, Podocyte, Mice, chemistry.chemical_compound, Phagosomes, Lysosome, Autophagy, Genetics, medicine, Animals, Molecular Biology, Kidney metabolism, Cell Differentiation, medicine.disease, Clone Cells, Rats, Cell biology, medicine.anatomical_structure, chemistry, Puromycin, Vacuoles, embryonic structures, biological phenomena, cell phenomena, and immunity, Microtubule-Associated Proteins, Protein Processing, Post-Translational, Biomarkers, Biotechnology
Abstract: Microtubule-associated protein 1 light chain 3 (LC3) is a unique modifier protein. LC3-I, the cytosolic form, is modified to LC3-II, the membrane-bound form, by a mechanism similar to ubiquitylation by E1- and E2-like enzymes, Apg7p and Apg3p, respectively. In the present study, we found that LC3-I is processed to LC3-II during the differentiation and recovery from puromycin aminonucleoside-induced nephrosis of podocytes. LC3 is especially expressed in the podocytes of rat kidney as the membrane-bound form LC3-II. Biochemical analysis using a conditionally immortalized mouse podocyte clone (MPC) revealed that LC3-I is processed to LC3-II during the differentiation of cells into mature podocytes and accumulates in the membrane-rich fraction of the cell lysate. LC3-II-localized vesicles, which differ from lysosomes and endosomes, in differentiated MPC cells are morphologically similar to autophagic vacuoles during starvation-induced autophagy. During starvation-induced autophagy, autophagosomes fuses with lysosome and LC3-II on autophagosomes is finally degraded by lysosomal proteases. However, in differentiated MPC cells, little LC3-II on the vesicles is degraded by lysosomal proteases, suggesting that little LC3-II-localized vesicles in differentiated MPC cells fuse with lysosome. Furthermore, the LC3-II level in differentiated MPC cells increases with recovery from damage caused by experimental puromycin aminonucleoside-induced nephrosis. These results suggest that LC3-II-localized vesicles play an important role in the physiological function of podocytes.
Published: 2003
Full Text: View/download PDF

35. Liver autophagy contributes to the maintenance of blood glucose and amino acid levels

Author: Norihiro Tada, Takashi Ueno, Hikari Taka, Yuka Hiraoka, Katsuyuki Takahashi, Tsutomu Fujimura, Dong Mei Zheng, Junji Ezaki, Kenji Takehana, Junichi Iwata, Mitsue Takeda-Ezaki, Mitsutaka Yoshida, Masaaki Komatsu, Isei Tanida, Norihiko Furuya, Naomi Matsumoto, Keiji Tanaka, and Eiki Kominami
Subjects: Blood Glucose, medicine.medical_specialty, Proteolysis, medicine.medical_treatment, Biology, Glucagon, Mice, Internal medicine, medicine, Autophagy, Animals, Insulin, Amino Acids, Muscle, Skeletal, Molecular Biology, Triglycerides, chemistry.chemical_classification, medicine.diagnostic_test, Catabolism, Fatty Acids, Gluconeogenesis, Cell Biology, Fasting, Basic Research Paper, Amino acid, Mice, Inbred C57BL, Endocrinology, chemistry, Liver, Starvation, Vacuoles, Blood sugar regulation, Microtubule-Associated Proteins
Abstract: Both anabolism and catabolism of the amino acids released by starvation-induced autophagy are essential for cell survival, but their actual metabolic contributions in adult animals are poorly understood. Herein, we report that, in mice, liver autophagy makes a significant contribution to the maintenance of blood glucose by converting amino acids to glucose via gluconeogenesis. Under a synchronous fasting-initiation regimen, autophagy was induced concomitantly with a fall in plasma insulin in the presence of stable glucagon levels, resulting in a robust amino acid release. In liver-specific autophagy (Atg7)-deficient mice, no amino acid release occurred and blood glucose levels continued to decrease in contrast to those of wild-type mice. Administration of serine (30 mg/animal) exerted a comparable effect, raising the blood glucose levels in both control wild-type and mutant mice under starvation. Thus, the absence of the amino acids that were released by autophagic proteolysis is a major reason for a decrease in blood glucose. Autophagic amino acid release in control wild-type livers was significantly suppressed by the prior administration of glucose, which elicited a prompt increase in plasma insulin levels. This indicates that insulin plays a dominant role over glucagon in controlling liver autophagy. These results are the first to show that liver-specific autophagy plays a role in blood glucose regulation.
Published: 2011

36. Caffeine induces apoptosis by enhancement of autophagy via PI3K/Akt/mTOR/p70S6K inhibition

Author: Shigeto Sato, Hiroki Kobayashi, Sumihiro Kawajiri, Takahiro Fujimaki, Yoko Imamichi, Shinji Saiki, Isei Tanida, Masaya Imoto, Fumiaki Sato, Nobutaka Hattori, Yukiko Sasazawa, and Kei-Ichi Ishikawa
Subjects: Programmed cell death, P70-S6 Kinase 1, Apoptosis, Biology, Membrane Fusion, chemistry.chemical_compound, Mice, Phosphatidylinositol 3-Kinases, Caffeine, Cell Line, Tumor, Phagosomes, Autophagy, Animals, Humans, Propidium iodide, Molecular Biology, Protein kinase B, PI3K/AKT/mTOR pathway, Phosphoinositide-3 Kinase Inhibitors, Sirolimus, TOR Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, 70-kDa, Cell Biology, Basic Research Paper, Cell biology, Enzyme Activation, chemistry, Ribosomal protein s6, Lysosomes, Proto-Oncogene Proteins c-akt, Signal Transduction
Abstract: Caffeine is one of the most frequently ingested neuroactive compounds. All known mechanisms of apoptosis induced by caffeine act through cell cycle modulation or p53 induction. It is currently unknown whether caffeine-induced apoptosis is associated with other cell death mechanisms, such as autophagy. Herein we show that caffeine increases both the levels of microtubule-associated protein 1 light chain 3-II and the number of autophagosomes, through the use of western blotting, electron microscopy and immunocytochemistry techniques. Phosphorylated p70 ribosomal protein S6 kinase (Thr389), S6 ribosomal protein (Ser235/236), 4E-BP1 (Thr37/46) and Akt (Ser473) were significantly decreased by caffeine. In contrast, ERK1/2 (Thr202/204) was increased by caffeine, suggesting an inhibition of the Akt/mTOR/p70S6K pathway and activation of the ERK1/2 pathway. Although insulin treatment phosphorylated Akt (Ser473) and led to autophagy suppression, the effect of insulin treatment was completely abolished by caffeine addition. Caffeine-induced autophagy was not completely blocked by inhibition of ERK1/2 by U0126. Caffeine induced reduction of mitochondrial membrane potentials and apoptosis in a dose-dependent manner, which was further attenuated by the inhibition of autophagy with 3-methyladenine or Atg7 siRNA knockdown. Furthermore, there was a reduced number of early apoptotic cells (annexin V positive, propidium iodide negative) among autophagy-deficient mouse embryonic fibroblasts treated with caffeine than in their wild-type counterparts. These results support previous studies on the use of caffeine in the treatment of human tumors and indicate a potential new target in the regulation of apoptosis.
Published: 2011

37. Measurement of autophagy in cells and tissues

Author: Isei, Tanida and Satoshi, Waguri
Subjects: Cell Extracts, Cells, Blotting, Western, Fluorescent Antibody Technique, Models, Biological, Cell Line, Mice, Phagosomes, Autophagy, Animals, Humans, Electrophoresis, Polyacrylamide Gel, Lysosomes, Microtubule-Associated Proteins
Abstract: Two major proteolysis systems, the ubiquitin-proteasome system, and the autophagy-lysosome system, contribute to degradation of various types of protein and/or protein aggregates. In general, the autophagy-lysosome system is involved in bulk intracellular degradation of proteins and organelles, while the ubiquitin-proteasome system is selective. During autophagy, a cytosolic form of LC3 (LC3-I) is conjugated to phosphatidylethanolamine to form LC3-phosphatidylethanolamine conjugate (LC3-II), which is recruited to autophagosomal membranes, and LC3-II is degraded by lysosomal hydrolases after the fusion of autophagosomes with lysosomes. Therefore, lysosomal turnover of LC3-II reflects starvation-induced autophagic activity, and detection of LC3 by immunoblotting or immunofluorescence has become a reliable method for monitoring autophagy. When autophagy is impaired, the level of p62/SQSTM1, a ubiquitin- and LC3-binding protein, is increased in addition to the accumulation of ubiquitinated proteins. Here, we describe basic protocols to analyze endogenous LC3-II, p62, and autophagy-related proteins by immunoblotting, immunofluorescence, and electron microscopy.
Published: 2010

38. Measurement of Autophagy in Cells and Tissues

Author: Satoshi Waguri and Isei Tanida
Subjects: medicine.diagnostic_test, biology, Chemistry, Proteolysis, Autophagy, Protein aggregation, Immunofluorescence, Cell biology, Cytosol, Ubiquitin, embryonic structures, Organelle, medicine, biology.protein, biological phenomena, cell phenomena, and immunity, Intracellular
Abstract: Two major proteolysis systems, the ubiquitin-proteasome system, and the autophagy-lysosome system, contribute to degradation of various types of protein and/or protein aggregates. In general, the autophagy-lysosome system is involved in bulk intracellular degradation of proteins and organelles, while the ubiquitin-proteasome system is selective. During autophagy, a cytosolic form of LC3 (LC3-I) is conjugated to phosphatidylethanolamine to form LC3-phosphatidylethanolamine conjugate (LC3-II), which is recruited to autophagosomal membranes, and LC3-II is degraded by lysosomal hydrolases after the fusion of autophagosomes with lysosomes. Therefore, lysosomal turnover of LC3-II reflects starvation-induced autophagic activity, and detection of LC3 by immunoblotting or immunofluorescence has become a reliable method for monitoring autophagy. When autophagy is impaired, the level of p62/SQSTM1, a ubiquitin- and LC3-binding protein, is increased in addition to the accumulation of ubiquitinated proteins. Here, we describe basic protocols to analyze endogenous LC3-II, p62, and autophagy-related proteins by immunoblotting, immunofluorescence, and electron microscopy.
Published: 2010
Full Text: View/download PDF

39. Autophagic compartments gain access to the MHC class II compartments in thymic epithelium

Author: Takashi Ueno, Isei Tanida, Sachiko Seki, Tohru Ikeda, Michiyuki Kasai, Toshiaki Mizuochi, and Eiki Kominami
Subjects: Immunology, Blotting, Western, Context (language use), Thymus Gland, Major histocompatibility complex, Cell Line, Mice, MHC class I, Autophagy, Immunology and Allergy, Animals, MHC class II, Antigen Presentation, biology, Histocompatibility Antigens Class II, Colocalization, Epithelial Cells, Cell biology, Blot, Mice, Inbred C57BL, Self Tolerance, Microscopy, Fluorescence, Cytoplasm, biology.protein, Microtubule-Associated Proteins
Abstract: The presentation of self-peptides in the context of MHC molecules by thymic epithelial cells (TECs) is essential for T cell repertoire selection in the thymus. However, the underlying mechanisms of this process have not been fully elucidated. To address whether autophagy, a catabolic process involving the degradation of a cell’s components through the lysosomal machinery, intersects the MHC class II-restricted Ag presentation pathway in TECs, we investigated the colocalization of LC3, a peculiar autophagy marker molecule, with MHC class II compartments in in vitro-established TEC lines by immunofluorescence microscopy and Western blotting analyses. We found that in both cortical and medullary TEC lines, LC3 was colocalized with the H2-DM-positive lysosomal compartments, in which MHC class II plus class II-associated invariant chain peptides complexes are formed. Furthermore, our analysis of thymic cryosections from 1-day-old mice revealed that LC3 colocalizes with the H2-DM-positive compartments in TECs. These results strongly suggest that the cytoplasmic self-Ags gain access to the H2-DM-positive compartments via the autophagic process in the thymus.
Published: 2009

40. LC3 and Autophagy

Author: Isei, Tanida, Takashi, Ueno, and Eiki, Kominami
Subjects: Mice, Cell Line, Tumor, Phagosomes, Blotting, Western, Autophagy, Animals, Immunoprecipitation, Electrophoresis, Polyacrylamide Gel, Microtubule-Associated Proteins, Cells, Cultured
Abstract: Microtubule-associated protein 1A/1B-light chain 3 (LC3) is a soluble protein with a molecular mass of approximately 17 kDa that is distributed ubiquitously in mammalian tissues and cultured cells. During autophagy, autophagosomes engulf cytoplasmic components, including cytosolic proteins and organelles. Concomitantly, a cytosolic form of LC3 (LC3-I) is conjugated to phosphatidylethanolamine to form LC3-phosphatidylethanolamine conjugate (LC3-II), which is recruited to autophagosomal membranes. Autophagosomes fuse with lysosomes to form autolysosomes, and intra-autophagosomal components are degraded by lysosomal hydrolases. At the same time, LC3-II in autolysosomal lumen is degraded. Thus, lysosomal turnover of the autophagosomal marker LC3-II reflects starvation-induced autophagic activity, and detecting LC3 by immunoblotting or immunofluorescence has become a reliable method for monitoring autophagy and autophagy-related processes, including autophagic cell death. Here we describe basic protocols to assay for endogenous LC3-II by immunoblotting, immunoprecipitation, and immunofluorescence.
Published: 2008

41. Loss of Pten, a tumor suppressor, causes the strong inhibition of autophagy without affecting LC3 lipidation

Author: Isei Tanida, Sumio Watanabe, Wataru Sato, Masaaki Komatsu, Tak W. Mak, Yasuo Horie, Shigetoshi Ohshima, Mitsutaka Yoshida, Takashi Ueno, and Eiki Kominami
Subjects: Cell signaling, Mice, Transgenic, Vacuole, Mice, Downregulation and upregulation, Phagosomes, Autophagy, Tensin, PTEN, Animals, Insulin, Genes, Tumor Suppressor, Molecular Biology, PI3K/AKT/mTOR pathway, Cells, Cultured, biology, Akt/PKB signaling pathway, PTEN Phosphohydrolase, Cell Biology, Lipid Metabolism, Cell biology, Mice, Inbred C57BL, Starvation, biology.protein, Hepatocytes, Apoptosis Regulatory Proteins, Microtubule-Associated Proteins, Signal Transduction
Abstract: (1)Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its function as a negative regulator of the class I phosphatidyl-inositol 3-kinase/Akt pathway antagonizes insulin-dependent cell signaling. The targeted deletion of Pten in mouse liver leads to insulin hypersensitivity and the upregulation of the phosphatidyl-inositol 3-kinase/Akt signaling pathway. In this study, we investigated the effects of Pten deficiency on autophagy, a major cellular degradative system responsible for the turnover of cell constituents. The autophagic degradation of [(14)C-leucine-labeled proteins of hepatocytes isolated from Pten-deficient livers was strongly inhibited, compared with that of control hepatocytes. However, no significant difference was found in the levels of the Atg12-Atg5 conjugate and LC3-II, the lipidated form of LC3, an intrinsic autophagosomal membrane marker, between control and Pten-deficient livers. Electron microscopic analyses showed that numerous autophagic vacuoles (autophagosomes plus autolysosomes) were present in the livers of control mice that had been starved for 48 hours, whereas they were markedly reduced in Pten-deficient livers under the same conditions. In vivo administration of leupeptin to control livers caused the inhibition of autophagic proteolysis, resulting in the accumulation of autolysosomes. These autolysosomes could be separated as a denser autolysosomal fraction from other cell membranes by Percoll density gradient centrifugation. In leupeptin-administered mutant livers, however, the accumulation of denser autolysosomes was reduced substantially. Collectively, we conclude that enhanced insulin signaling in Pten deficiency suppresses autophagy at the formation and maturation steps of autophagosomes, without inhibiting ATG conjugation reactions.
Published: 2008

42. LC3 and Autophagy

Author: Eiki Kominami, Isei Tanida, and Takashi Ueno
Subjects: Programmed cell death, medicine.diagnostic_test, Immunoprecipitation, Autophagy, Biology, Immunofluorescence, Cell biology, Blot, Cytosol, Biochemistry, Cytoplasm, embryonic structures, Organelle, medicine, biological phenomena, cell phenomena, and immunity
Abstract: Microtubule-associated protein 1A/1B-light chain 3 (LC3) is a soluble protein with a molecular mass of approximately 17 kDa that is distributed ubiquitously in mammalian tissues and cultured cells. During autophagy, autophagosomes engulf cytoplasmic components, including cytosolic proteins and organelles. Concomitantly, a cytosolic form of LC3 (LC3-I) is conjugated to phosphatidylethanolamine to form LC3-phosphatidylethanolamine conjugate (LC3-II), which is recruited to autophagosomal membranes. Autophagosomes fuse with lysosomes to form autolysosomes, and intra-autophagosomal components are degraded by lysosomal hydrolases. At the same time, LC3-II in autolysosomal lumen is degraded. Thus, lysosomal turnover of the autophagosomal marker LC3-II reflects starvation-induced autophagic activity, and detecting LC3 by immunoblotting or immunofluorescence has become a reliable method for monitoring autophagy and autophagy-related processes, including autophagic cell death. Here we describe basic protocols to assay for endogenous LC3-II by immunoblotting, immunoprecipitation, and immunofluorescence.
Published: 2008
Full Text: View/download PDF

43. [Mammalian Atg-conjugation systems: key players essential for the formation of autophagosomes]

Author: Isei Tanida
Subjects: Intracellular Signaling Peptides and Proteins, Membrane Proteins, Proteins, Autophagy-Related Protein 8 Family, Membrane Fusion, Autophagy-Related Protein 5, Cytoskeletal Proteins, Mice, Phagosomes, Autophagy, Small Ubiquitin-Related Modifier Proteins, Animals, Humans, Apoptosis Regulatory Proteins, Carrier Proteins, Lysosomes, Microtubule-Associated Proteins, Autophagy-Related Protein 12, Phospholipids, Protein Binding
Published: 2006

44. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation

Author: Atushi Isoai, Takashi Ueno, Hiromichi Kumagai, Eriko Fujita, Isei Tanida, Randal J. Kaufman, Eiki Kominami, Takashi Momoi, Satoshi Ogawa, and Yoriko Kouroku
Subjects: Programmed cell death, ATG5, Eukaryotic Initiation Factor-2, Biology, BAG3, Endoplasmic Reticulum, Models, Biological, Autophagy-Related Protein 5, ATG12, Mice, eIF-2 Kinase, Leucine, Pepstatins, Autophagy, Animals, RNA, Messenger, Phosphorylation, Protein Structure, Quaternary, Molecular Biology, Caspase 12, Sirolimus, Cell Death, Endoplasmic reticulum, Adenine, Cell Biology, Molecular biology, Cell biology, Enzyme Activation, Gene Expression Regulation, Unfolded protein response, biological phenomena, cell phenomena, and immunity, Lysosomes, Peptides, Microtubule-Associated Proteins
Abstract: Expanded polyglutamine 72 repeat (polyQ72) aggregates induce endoplasmic reticulum (ER) stress-mediated cell death with caspase-12 activation and vesicular formation (autophagy). We examined this relationship and the molecular mechanism of autophagy formation. Rapamycin, a stimulator of autophagy, inhibited the polyQ72-induced cell death with caspase-12 activation. PolyQ72, but not polyQ11, stimulated Atg5-Atg12-Atg16 complex-dependent microtubule-associated protein 1 (MAP1) light chain 3 (LC3) conversion from LC3-I to -II, which plays a key role in autophagy. The eucaryotic translation initiation factor 2 alpha (eIF2alpha) A/A mutation, a knock-in to replace a phosphorylatable Ser51 with Ala51, and dominant-negative PERK inhibited polyQ72-induced LC3 conversion. PolyQ72 as well as ER stress stimulators upregulated Atg12 mRNA and proteins via eIF2alpha phosphorylation. Furthermore, Atg5 deficiency as well as the eIF2alpha A/A mutation increased the number of cells showing polyQ72 aggregates and polyQ72-induced caspase-12 activation. Thus, autophagy formation is a cellular defense mechanism against polyQ72-induced ER-stress-mediated cell death by degrading polyQ72 aggregates, with PERK/eIF2alpha phosphorylation being involved in polyQ72-induced LC3 conversion.
Published: 2006

45. The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers

Author: Isei Tanida, Takashi Ueno, Atsuo Suzuki, Yu-shin Sou, Tsunehiro Mizushima, Masaaki Komatsu, Keiji Tanaka, Taichi Kumanomidou, Eiki Kominami, and Takashi Yamane
Subjects: Autophagosome, Models, Molecular, Proteases, medicine.medical_treatment, ATG8, GABARAP, Autophagy-Related Proteins, Biology, Crystallography, X-Ray, Catalysis, Substrate Specificity, Structural Biology, Catalytic triad, medicine, Autophagy, Humans, Protein Precursors, Molecular Biology, Protease, Binding Sites, Cysteine protease, Protein tertiary structure, Protein Structure, Tertiary, Cysteine Endopeptidases, Biochemistry, Structural Homology, Protein, Protein Processing, Post-Translational, Protein Binding
Abstract: Autophagy is an evolutionarily conserved pathway in which the cytoplasm and organelles are engulfed within double-membrane vesicles, termed autophagosomes, for the turnover and recycling of these cellular constituents. The yeast Atg8 and its human orthologs, such as LC3 and GABARAP, have a unique feature as they conjugate covalently to phospholipids, differing from ubiquitin and other ubiquitin-like modifiers that attach only to protein substrates. The lipidated Atg8 and LC3 localize to autophagosomal membranes and play indispensable roles for maturation of autophagosomes. Upon completion of autophagosome formation, some populations of lipidated Atg8 and LC3 are delipidated for recycling. Atg4b, a specific protease for LC3 and GABARAP, catalyzes the processing reaction of LC3 and GABARAP precursors to mature forms and de-conjugating reaction of the modifiers from phospholipids. Atg4b is a unique enzyme whose primary structure differs from that of any other proteases that function as processing and/or de-conjugating enzymes of ubiquitin and ubiquitin-like modifiers. However, the tertiary structures of the substrates considerably resemble that of ubiquitin except for the N-terminal additional domain. Here we determined the crystal structure of human Atg4b by X-ray crystallography at 2.0 A resolution, and show that Atg4b is a cysteine protease whose active catalytic triad site consists of Cys74, His280 and Asp278. The structure is comprised of a left lobe and a small right lobe, designated the "protease domain" and the "auxiliary domain", respectively. Whereas the protease domain structure of Atg4b matches that of papain superfamily cysteine proteinases, the auxiliary domain contains a unique structure with yet-unknown function. We propose that the R229 and W142 residues in Atg4b are specifically essential for recognition of substrates and catalysis of both precursor processing and de-conjugation of phospholipids.
Published: 2005

46. Solution structure of microtubule-associated protein light chain 3 and identification of its functional subdomains

Author: Hiroyuki Shinoda, Eiki Kominami, Takahide Kouno, Takashi Ueno, Takashi Kanematsu, Yoshihiro Mori, Mineyuki Mizuguchi, Keiichi Kawano, Masato Hirata, and Isei Tanida
Subjects: Autophagosome, Models, Molecular, Magnetic Resonance Spectroscopy, Microtubule-associated protein, Protein Conformation, Phosphorylcholine, Plasma protein binding, Biology, Biochemistry, Microtubules, Protein structure, Cytosol, Phagocytosis, Microtubule, Autophagy, Escherichia coli, Humans, Cysteine, Molecular Biology, Dose-Response Relationship, Drug, C-terminus, Phosphatidylethanolamines, Signal transducing adaptor protein, Cell Biology, Surface Plasmon Resonance, Recombinant Proteins, Protein Structure, Tertiary, Tubulin, embryonic structures, Mutation, biology.protein, Biophysics, biological phenomena, cell phenomena, and immunity, Microtubule-Associated Proteins, Gene Deletion, Protein Binding
Abstract: Microtubule-associated protein (MAP) light chain 3 (LC3) is a human homologue of yeast Apg8/Aut7/Cvt5 (Atg8), which is essential for autophagy. MAP-LC3 is cleaved by a cysteine protease to produce LC3-I, which is located in cytosolic fraction. LC3-I, in turn, is converted to LC3-II through the actions of E1- and E2-like enzymes. LC3-II is covalently attached to phosphatidylethanolamine on its C terminus, and it binds tightly to autophagosome membranes. We determined the solution structure of LC3-I and found that it is divided into N- and C-terminal subdomains. Additional analysis using a photochemically induced dynamic nuclear polarization technique also showed that the N-terminal subdomain of LC3-I makes contact with the surface of the C-terminal subdomain and that LC3-I adopts a single compact conformation in solution. Moreover, the addition of dodecylphosphocholine into the LC3-I solution induced chemical shift perturbations primarily in the C-terminal subdomain, which implies that the two subdomains have different sensitivities to dodecylphosphocholine micelles. On the other hand, deletion of the N-terminal subdomain abolished binding of tubulin and microtubules. Thus, we showed that two subdomains of the LC3-I structure have distinct functions, suggesting that MAP-LC3 can act as an adaptor protein between microtubules and autophagosomes.
Published: 2005

47. Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal Met121 to expose Gly120 for lipidation and targeting to autophagosomal membranes

Author: Takashi Ueno, Isei Tanida, and Eiki Kominami
Subjects: Saccharomyces cerevisiae Proteins, ATG8, Recombinant Fusion Proteins, Mutant, Molecular Sequence Data, Glycine, Lipid-anchored protein, Cleavage (embryo), Cell Fractionation, Biochemistry, Autophagy-Related Protein 7, law.invention, Cell Line, Methionine, Ubiquitin, law, Autophagy, Animals, Humans, Amino Acid Sequence, Molecular Biology, Phospholipids, biology, Cell Biology, Intracellular Membranes, In vitro, Protein Structure, Tertiary, Recombinant DNA, biology.protein, RNA Interference, Autophagin, Microtubule-Associated Proteins, Sequence Alignment, Subcellular Fractions
Abstract: Human light chain 3/MAP1LC3B, an autophagosomal ortholog of yeast Atg8, is conjugated to phospholipid (PL) via ubiquitylation-like reactions mediated by human Atg7 and Atg3. Since human Atg4B was found to cleave the carboxyl terminus of MAP1LC3B in vitro, we hypothesized that this exposes its carboxyl-terminal Gly(120). It was recently reported, however, that when Myc-MAP1LC3B-His is expressed in HEK293 cells, its carboxyl terminus is not cleaved. (Tanida, I., Sou, Y.-s., Ezaki, J., Minematsu-Ikeguchi, N., Ueno, T., and Kominami, E. (2004) J. Biol. Chem. 279, 36268-36276). To clarify this contradiction, we sought to determine whether the carboxyl terminus of MAP1LC3B is cleaved to expose Gly(120) for further ubiquitylation-like reactions. When MAP1LC3B-3xFLAG and Myc-MAP1LC3B-His were expressed in HEK293 cells, their carboxyl termini were cleaved, whereas there was little cleavage of mutant proteins MAP1LC3B(G120A)-3xFLAG and Myc-MAP1LC3B(G120A)-His, containing Ala in place of Gly(120). An in vitro assay showed that Gly(120) is essential for carboxyl-terminal cleavage by human Atg4B as well as for formation of the intermediates Atg7-MAP1LC3B (ubiquitin-activating enzyme-substrate) and Atg3-MAP1LC3B (ubiquitin carrier protein-substrate). Recombinant MAP1LC3B-PL was fractionated into the 100,000 x g pellet in a manner similar to that shown for endogenous MAP1LC3B-PL. RNA interference of MAP1LC3B mRNA resulted in a decrease in both endogenous MAP1LC3B-PL and MAP1LC3B. These results indicate that the carboxyl terminus of MAP1LC3B is cleaved to expose Gly(120) for further ubiquitylation-like reactions.
Published: 2004

48. Role for Rab7 in maturation of late autophagic vacuoles

Author: Takashi Ueno, Isei Tanida, Eiki Kominami, Stefanie Jäger, Eeva-Liisa Eskelinen, Paul Saftig, Cecilia Bucci, Jager, S., Bucci, Cecilia, Tanida, I., Ueno, T., Kominami, E., Saftig, P., and Eskelinen, E. L.
Subjects: Autophagosome, Cytoplasm, Endosome, Autophagosome maturation, Recombinant Fusion Proteins, Membrane Traffic, Vacuole, Biology, Mice, Antigens, CD, Lysosomal-Associated Membrane Protein 1, Rab7, Rab protein, Lysosome, Lysosomal-Associated Membrane Protein 2, medicine, Autophagy, Animals, Humans, Cells, Cultured, Membrane Glycoproteins, LAMP1, Cytoplasmic Vesicles, Lysosome-Associated Membrane Glycoproteins, rab7 GTP-Binding Proteins, Cell Biology, Fibroblasts, Cell biology, medicine.anatomical_structure, rab GTP-Binding Proteins, Vacuoles, Monoglycerides, RNA Interference, Lysophospholipids, Biomarkers, HeLa Cells
Abstract: The small GTP binding protein Rab7 has a role in the late endocytic pathway and lysosome biogenesis. The role of mammalian Rab7 in autophagy is, however, unknown. We have addressed this by inhibiting Rab7 function with RNA interference and overexpression of dominant negative Rab7. We show here that Rab7 was needed for the formation of preferably perinuclear, large aggregates, where the autophagosome marker LC3 colocalised with Rab7 and late endosomal and lysosomal markers. By electron microscopy we showed that these large aggregates corresponded to autophagic vacuoles surrounding late endosomal or lysosomal vesicles. Our experiments with quantitative electron microscopy showed that Rab7 was not needed for the initial maturation of early autophagosomes to late autophagic vacuoles, but that it participated in the final maturation of late autophagic vacuoles. Finally, we showed that the recruitment of Rab7 to autophagic vacuoles was retarded in cells deficient in the lysosomal membrane proteins Lamp1 and Lamp2, which we have recently shown to accumulate late autophagic vacuoles during starvation. In conclusion, our results showed a role for Rab7 in the final maturation of late autophagic vacuoles.
Published: 2004

49. LC3 conjugation system in mammalian autophagy

Author: Eiki Kominami, Isei Tanida, and Takashi Ueno
Subjects: Autophagosome, Programmed cell death, ATG8, GABARAP, Biology, Biochemistry, Article, Species Specificity, Lysosome, Neoplasms, medicine, Autophagy, Animals, Humans, Mammals, Autophagosomes, Cell Differentiation, GATE-16, Cell Biology, Bacterial Infections, Neuromuscular Diseases, Cell biology, Crosstalk (biology), medicine.anatomical_structure, Lytic cycle, embryonic structures, biological phenomena, cell phenomena, and immunity, Atg8, Microtubule-Associated Proteins, Signal Transduction
Abstract: Autophagy is the bulk degradation of proteins and organelles, a process essential for cellular maintenance, cell viability, differentiation and development in mammals. Autophagy has significant associations with neurodegenerative diseases, cardiomyopathies, cancer, programmed cell death, and bacterial and viral infections. During autophagy, a cup-shaped structure, the preautophagosome, engulfs cytosolic components, including organelles, and closes, forming an autophagosome, which subsequently fuses with a lysosome, leading to the proteolytic degradation of internal components of the autophagosome by lysosomal lytic enzymes. During the formation of mammalian autophagosomes, two ubiquitylation-like modifications are required, Atg12-conjugation and LC3-modification. LC3 is an autophagosomal ortholog of yeast Atg8. A lipidated form of LC3, LC3-II, has been shown to be an autophagosomal marker in mammals, and has been used to study autophagy in neurodegenerative and neuromuscular diseases, tumorigenesis, and bacterial and viral infections. The other Atg8 homologues, GABARAP and GATE-16, are also modified by the same mechanism. In non-starved rats, the tissue distribution of LC3-II differs from those of the lipidated forms of GABARAP and GATE-16, GABARAP-II and GATE-16-II, suggesting that there is a functional divergence among these three modified proteins. Delipidation of LC3-II and GABARAP-II is mediated by hAtg4B. We review the molecular mechanism of LC3-modification, the crosstalk between LC3-modification and mammalian Atg12-conjugation, and the cycle of LC3-lipidation and delipidation mediated by hAtg4B, as well as recent findings concerning the other two Atg8 homologues, GABARAP and GATE-16. We also highlight recent findings regarding the pathobiology of LC3-modification, including its role in microbial infection, cancer and neuromuscular diseases.
Published: 2004

50. The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification

Author: Takashi Ueno, Emiko Tanida-Miyake, Mariko Ohsumi, Takahiro Nemoto, Isei Tanida, Masahiro Yokota, Eiki Kominami, and Naoko Minematsu-Ikeguchi
Subjects: DNA, Complementary, Saccharomyces cerevisiae Proteins, Mutant, Molecular Sequence Data, Autophagy-Related Proteins, Vacuole, Biology, In Vitro Techniques, Biochemistry, Autophagy-Related Protein 7, Models, Biological, Cell Line, Gene product, Ligases, Mice, Two-Hybrid System Techniques, Autophagy, Animals, Humans, Amino Acid Sequence, Molecular Biology, chemistry.chemical_classification, Base Sequence, Sequence Homology, Amino Acid, HEK 293 cells, Proteins, Cell Biology, Yeast, Recombinant Proteins, Cell biology, Cytosol, Enzyme, chemistry, embryonic structures, Ubiquitin-Conjugating Enzymes, Mutagenesis, Site-Directed, biological phenomena, cell phenomena, and immunity, Oxidoreductases, Microtubule-Associated Proteins, Autophagy-Related Protein 12, Conjugate
Abstract: Autophagy is a process for the bulk degradation of cytosolic compartments by lysosomes/vacuoles. The formation of autophagosomes involves a dynamic rearrangement of the membrane for which two ubiquitin-like modifications (the conjugation of Apg12p and the modification of a soluble form of MAP-LC3 to a membrane-bound form) are essential. In yeast, Apg10p is an E2-like enzyme essential for Apg12p conjugation. The isolated mouse APG10 gene product interacts with mammalian Apg12p dependent on mammalian Apg7p (E1-like enzyme), and facilitates Apg12p conjugation. The interaction of Apg10p with Apg12p is dependent on the carboxyl-terminal glycine of Apg12p. Mutational analysis of the predicted active site cysteine (Cys161) within mouse Apg10p shows that mutant Apg10pC161S, which can form a stable intermediate with Apg12p, inhibits Apg12p conjugation even in the presence of Apg7p, while overexpression of Apg7p facilitates formation of an Apg12p-Apg5p conjugate. Furthermore, the coexpression of Apg10p with Apg7p facilitates the modification of a soluble form of MAP-LC3 to a membrane-bound form, a second modification essential for autophagy. Mouse Apg10p interacts with MAP-LC3 in HEK293 cells, while no mutant Apg10pC161S forms any intermediate with MAP-LC3. Direct interaction between Apg10p and MAP-LC3 is also demonstrated by yeast two-hybrid analysis. The inability of mutant Apg10pC161S to form any intermediate with MAP-LC3 has ruled out the possibility that MAP-LC3 interacts with Apg10p as a substrate.
Published: 2003

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

Publication Type

Journal

Database

Publisher

57 results on '"Isei Tanida"'

Search Results

Catalog

Select search scope, currently: Articles

Catalog

books, media & more in Jio Institute collections

Articles

journal articles & other e-resources