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1. A revision of Dryopteris sect. Diclisodon (Dryopteridaceae) based on morphological and molecular evidence with description of a new species

Author

Yun Xiong, Zheng-Yu Zuo, Xin-Yu Du, De-Zhu Li, Ting Zhao, and Jin-Mei Lu

Subjects
Frond, Phylogenetic tree, biology, Evolutionary biology, Key (lock), Molecular evidence, Plant Science, biology.organism_classification, Sect, Homonym (biology), Dryopteris, Ecology, Evolution, Behavior and Systematics, Dryopteridaceae
Abstract

Dryopteris sect. Diclisodon is a small section of ferns with about 12 species mainly distributed in East Asia. Here, we carried out morphological and phylogenetic analyses of this section. A new species from southwest China, D. gaoligongensis, is described and illustrated. Dryopteris gaoligongensis resembles D. indonesiana and D. sparsa, but differs by having a creeping rhizome and large 4-pinnate fronds. We also show that D. glabrior Ching & Z.Y. Liu is a distinct species; however, because it is a later homonym of D. glabrior Copeland, it should be renamed D. renchangiana. We conclude that a species previously known as D. nitidula, also an illegitimate homonym, should be recognized with a new name, D. sinonepalensis. We resolve the phylogenetic position of D. yoroii as sister to other sampled species of D. sect. Diclisodon. Our phylogenetic analyses confirm the distinctiveness of D. gaoligongensis, D. renchangiana, and D. sinonepalensis. A key to species of D. sect. Diclisodon in China is provided.

Published
2022

2. Adiantum japonicum, a new species of the Adiantum pedatum complex (Pteridaceae) from Japan

Author

Zhao, Ting, Zuo, Zheng-Yu, Ebihara, Atsushi, Nakato, Narumi, Soejima, Akiko, Li, De-Zhu, Wen, Jun, and Lu, Jin-Mei

Subjects
Pteridaceae, biology, Phylogenetic tree, Maximum likelihood, Morphology (biology), Biodiversity, Plant Science, biology.organism_classification, Rhizome, Tracheophyta, Adiantum, Adiantum pedatum, Evolutionary biology, Polypodiales, Polypodiopsida, Plantae, Ecology, Evolution, Behavior and Systematics, Taxonomy
Abstract

The Adiantum pedatum complex is disjunctly distributed in North America and eastern Asia. In this study, we carried out a detailed morphological study based on 137 specimens representing the biogeographic diversity of this complex. The sequences of eight chloroplast markers of 35 samples were analyzed with maximum likelihood and Bayesian inference. The morphological and phylogenetic analyses support the recognition of a new species of the A. pedatum complex from Japan. We propose the new species as A. japonicum based on the examinations of specimens from Japan and the comparative analyses of the whole complex. This new species can be distinguished from A. pedatum by the erect rhizome and shows significant molecular differences from other species in this complex. A taxonomic description with detailed morphological characters of the new species is presented.

Published
2021

3. Complete genome of the thermophilic purple sulfur Bacterium Thermochromatium tepidum compared to Allochromatium vinosum and other Chromatiaceae

Author

Wesley D. Swingley, W. Matthew Sattley, Brad M. Burchell, Kathryn N. Shaffer, Tara L. Renbarger, Lynn M. Stokes, D. Adam Nuccio, Emma D. Dewey, Mackenzie K. Hayward, Michael T. Madigan, Zheng-Yu Wang-Otomo, Jacob Schladweiler, Robert E. Blankenship, Jeffrey W. Touchman, Sonja A. Gurbani, and Catrina M. Kujawa

Subjects
biology, Chemistry, Thermophile, RuBisCO, Nitrogenase, Cell Biology, Plant Science, General Medicine, biology.organism_classification, Biochemistry, Genome, Chromatiaceae, Purple sulfur bacteria, biology.protein, Gene, Bacteria
Abstract

The complete genome sequence of the thermophilic purple sulfur bacterium Thermochromatium tepidum strain MCT (DSM 3771T) is described and contrasted with that of its mesophilic relative Allochromatium vinosum strain D (DSM 180T) and other Chromatiaceae. The Tch. tepidum genome is a single circular chromosome of 2,958,290 base pairs with no plasmids and is substantially smaller than the genome of Alc. vinosum. The Tch. tepidum genome encodes two forms of RuBisCO and contains nifHDK and several other genes encoding a molybdenum nitrogenase but lacks a gene encoding a protein that assembles the Fe–S cluster required to form a functional nitrogenase molybdenum-iron cofactor, leaving the phototroph phenotypically Nif–. Tch. tepidum contains genes necessary for oxidizing sulfide to sulfate as photosynthetic electron donor but is genetically unequipped to either oxidize thiosulfate as an electron donor or carry out assimilative sulfate reduction, both of which are physiological hallmarks of Alc. vinosum. Also unlike Alc. vinosum, Tch. tepidum is obligately phototrophic and unable to grow chemotrophically in darkness by respiration. Several genes present in the Alc. vinosum genome that are absent from the genome of Tch. tepidum likely contribute to the major physiological differences observed between these related purple sulfur bacteria that inhabit distinct ecological niches.

Published
2021

4. Behavioral and neurobiological changes in a novel mouse model of schizophrenia induced by the combination of cuprizone and MK-801

Author

Mingyang Wang, Xin-Min Li, Denglei Ma, Lin Li, Zheng-yu Sun, Jie-wen Zhang, Lan Zhang, Cuicui Yang, and Li-Hong Gu

Subjects
Male, 0301 basic medicine, medicine.medical_specialty, Psychosis, Anxiety, Hyperkinesis, Corpus callosum, Open field, Corpus Callosum, White matter, Cuprizone, Mice, 03 medical and health sciences, 0302 clinical medicine, Internal medicine, Animals, Medicine, Chelating Agents, Spatial Memory, Memory Disorders, Behavior, Animal, biology, business.industry, General Neuroscience, Recognition, Psychology, medicine.disease, White Matter, Myelin basic protein, Mice, Inbred C57BL, 030104 developmental biology, Endocrinology, medicine.anatomical_structure, Cerebral cortex, Schizophrenia, biology.protein, NMDA receptor, Schizophrenic Psychology, Dizocilpine Maleate, business, Injections, Intraperitoneal, 030217 neurology & neurosurgery
Abstract

Schizophrenia is a mental illness characterized by episodes of psychosis, apathy, social withdrawal, and cognitive impairment. White matter lesions and glutamatergic hypofunction are reported to be the key pathogeneses underlying the multiple clinical symptoms of schizophrenia. Cuprizone (CPZ) is a copper chelator that selectively injures oligodendrocytes, and MK-801 is an antagonist of the N-methyl d-aspartate (NMDA) receptor. To better mimic the psychosis and complicated pathogenesis of schizophrenia, a novel possible mouse model was established by the combination of CPZ and MK-801. After exposure to CPZ for 5 weeks, the mice received a daily intraperitoneal injection of MK-801 for 2-weeks. Behavioral changes in the mouse model were evaluated using Y-maze, object recognition, and open field tests. Pathological changes were observed by transmission electron microscopy, oil red O staining, immunohistochemistry, and western blotting. The results showed that the novel mouse model induced by CPZ plus MK-801 exhibited severe spatial and recognition memory deficits, hyperactivity, and anxiety disorder. Moreover, the mice showed obvious demyelination and white matter damage and decreased expression levels of myelin basic protein (MBP) and 2',3'-cyclic nucleotide-3'-phosphodiesterase (CNPase) in the corpus callosum. Furthermore, the phosphorylation levels of Fyn and NMDA receptor 2B in the corpus callosum and NMDA receptor 1 in the cerebral cortex were noticeably decreased. Taken together, the novel mouse model induced by the combination of cuprizone and MK-801 showed comprehensive behavioral and neurobiological changes, which might make it a suitable animal model for schizophrenia.

Published
2021

5. Photosynthetic Growth and Energy Conversion in an Engineered Phototroph Containing Thermochromatium tepidum Light-Harvesting Complex 1 and the Rhodobacter sphaeroides Reaction Center Complex

Author

Masaharu Kitashima, Zheng-Yu Wang-Otomo, Kenji V. P. Nagashima, Kazuhito Inoue, Yukihiro Kimura, Michael T. Madigan, and Sakiko Nagashima

Subjects
Photosynthetic reaction centre, Light-harvesting complex, Rhodobacter sphaeroides, biology, Strain (chemistry), Chemistry, Coenzyme Q – cytochrome c reductase, Thermophile, Mutant, Biophysics, Photosynthesis, biology.organism_classification, Biochemistry
Abstract

Light-harvesting complex 1 (LH1) of the thermophilic purple sulfur bacterium Thermochromatium tepidum can be expressed in the purple non-sulfur bacterium Rhodobacter sphaeroides and forms a functional RC-LH1 complex with the native Rba. sphaeroides reaction center (Nagashima, K. V. P., et al. Proc. Natl. Acad. Sci. U. S. A. 2017, 114, 10906-10911). Although there is a large uphill energy gap between Tch. tepidum LH1 and the Rba. sphaeroides RC in this chimeric complex, it has been shown that light energy can be transferred, consistent with that seen in the native Rba. sphaeroides RC-LH1 complex. In this study, the contribution of this chimeric complex to growth and photosynthetic energy conversion in the hybrid organism was quantified. The mutant synthesizing this chimeric complex was grown phototrophically under 940 nm light-emitting diode (LED) light preferentially absorbed by Tch. tepidum LH1 and showed faster growth at low intensities of this wavelength than both a mutant strain of Rba. sphaeroides lacking LH2 and a mutant lacking all light-harvesting complexes. When grown with 850 nm LED light, the strain containing the native Rba. sphaeroides LH1-RC grew faster than the chimeric strain. Electron transfer from the RC to the membrane-integrated cytochrome bc1 complex was also estimated by flash-induced absorption changes in heme b. The rate of ubiquinone transport through the LH1 ring structure in the chimeric strain was virtually the same as that in native Rba. sphaeroides. We conclude that Tch. tepidum LH1 can perform the physiological functions of native LH1 in Rba. sphaeroides.

Published
2021

6. Increased mucin‐degrading bacteria by high protein diet leads to thinner mucus layer and aggravates experimental colitis

Author

Shuijiao Chen, Lulu Chen, Xiaowei Liu, Jingyan Wang, Zheng Yu, Yajun Liu, and Jun Yi

Subjects
Whey protein, Colon, Neuraminidase, High-protein diet, medicine.disease_cause, Microbiology, Mice, 03 medical and health sciences, 0302 clinical medicine, Casein, medicine, Animals, Colitis, Soy protein, Mice, Inbred BALB C, Bacteria, Hepatology, biology, business.industry, Dextran Sulfate, Mucin, Mucins, Gastroenterology, Caseins, medicine.disease, biology.organism_classification, Anti-Bacterial Agents, Mucus, Whey Proteins, 030220 oncology & carcinogenesis, Diet, High-Protein, Soybean Proteins, Female, 030211 gastroenterology & hepatology, business, Bacteroides thetaiotaomicron
Abstract

Background and aim Westernized high-fat diet increases the risk for inflammatory bowel diseases (IBDs), yet with insufficient understanding of the role of high-protein diet. We aimed to identify the effect of high-protein diets from different dietary proteins (casein, whey protein, soy protein) on experimental colitis and its impact on microbiota, structure and function of colonic mucus layer. Methods Female BALB/c mice were fed by standard diet, high-casein diet (HCD), high whey protein diet or high soy protein diet for 4 weeks. The susceptibility of dextran sulfate sodium (DSS)-induced colitis in mice and thickness of colonic mucus layer were compared after different dietary interventions, associated with the identification of the reversal effect of broad-spectrum antibiotic intervention (0.5 g/L of vancomycin and 1 g/L of neomycin sulfate, metronidazole and ampicillin in drinking water). Further analysis was performed on the synthesis of mucin, microbiota and sialidase involved in degradation of mucus layer. Results High-protein diets aggravated acute DSS-induced colitis independent of protein composition, while broad-spectrum antibiotics reversed this effect. HCD significantly altered the composition of bacteria in the colonic mucus layer, especially Bacteroides thetaiotaomicron and total mucin-degrading bacteria; besides, it increased sialidase concentration and reduced the thickness of mucus layer. However, it exhibited no significant effect on the synthesis of Muc2. Broad-spectrum antibiotics decreased the abundance of mucin-degrading bacteria and sialidase concentration while increased the thickness of mucus layer. Conclusion High-protein diet shifts microbial composition and thickness of colonic mucus layer, leading to the aggravation of acute DSS-induced colitis.

Published
2021

7. ErbB4 promotes inhibitory synapse formation by cell adhesion, independent of its kinase activity

Author

Zheng Yu, Dongyan Ren, Bin Luo, Erkang Fei, Ziyang Liu, Baoming Li, Mingtao Xiong, Dong Lin, Changqin Zhao, and Wenbing Chen

Subjects
0301 basic medicine, Receptor, ErbB-4, Neurogenesis, Neurosciences. Biological psychiatry. Neuropsychiatry, Molecular neuroscience, Hippocampus, Article, Receptor tyrosine kinase, Mice, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, Postsynaptic potential, Cell Adhesion, Animals, Humans, Kinase activity, Cell adhesion, Biological Psychiatry, Gephyrin, biology, Synapse assembly, Cell adhesion molecule, Chemistry, Cell biology, Psychiatry and Mental health, HEK293 Cells, 030104 developmental biology, Synapses, Schizophrenia, biology.protein, 030217 neurology & neurosurgery, RC321-571
Abstract

The precise control of the nervous system function under the vitality of synapses is extremely critical. Efforts have been taken to explore the underlying cellular and molecular mechanisms for synapse formation. Cell adhesion molecules have been found important for synapse assembly in the brain. Many trans-adhesion complexes have been identified to modulate excitatory synapse formation. However, little is known about the synaptogenic mechanisms for inhibitory synapses. ErbB4 is a receptor tyrosine kinase enriched in interneurons. Here, we showed that overexpressing ErbB4 in HEK293T cells induced gephyrin or GABAAR α1 puncta in co-cultured primary hippocampal neurons. This induction of ErbB4 was independent of its kinase activity. K751M, a kinase-dead mutant of ErbB4, can also induce gephyrin or GABAAR α1 puncta in the co-culture system. We further constructed K751M knock-in mice and found that the homozygous were viable at birth and fertile without changes in gross brain structure. The number of interneurons and inhibitory synapses onto pyramidal neurons (PyNs) were comparable between K751M and wild-type mice but decreased in ErbB4-Null mice. Moreover, ErbB4 can interact in trans with Slitrk3, a transmembrane postsynaptic protein at inhibitory synapses, through the extracellular RLD domain of ErbB4. The deletion of RLD diminished the induction of gephyrin or GABAAR α1 puncta by ErbB4. Finally, disruption of ErbB4–Slitrk3 interaction through neutralization of Slitrk3 by secretable RLD decreased inhibitory synapses onto PyNs and impaired GABAergic transmission. These results identify that ErbB4, as a cell adhesion molecule, promotes inhibitory synapse formation onto PyNs by interacting with Slitrk3 and in a kinase-independent manner, providing an unexpected mechanism of ErbB4 in inhibitory synapse formation.

Published
2021

8. Regulation of Nrf2 by phosphorylation: Consequences for biological function and therapeutic implications

Author

Tian Liu, Zheng-Yu Jiang, Yi-Fei Lv, Qidong You, and Jing-Long Zhao

Subjects
0301 basic medicine, NF-E2-Related Factor 2, Cellular homeostasis, Biology, medicine.disease_cause, digestive system, environment and public health, Biochemistry, Antioxidants, Glycogen Synthase Kinase 3, 03 medical and health sciences, 0302 clinical medicine, Physiology (medical), medicine, Post-translational regulation, Phosphorylation, Transcription factor, Protein kinase C, Kinase, respiratory system, Cell biology, Oxidative Stress, 030104 developmental biology, Casein kinase 2, 030217 neurology & neurosurgery, Oxidative stress
Abstract

The transcription factor nuclear factor erythroid-derived 2-like 2 (NRF2) participates in the activation of the antioxidant cytoprotective pathway and other important physiological processes to maintain cellular homeostasis. The dysregulation of NRF2 activity plays a role in various diseases, such as cardiovascular diseases, neurodegenerative diseases, and cancer. Thus, NRF2 activity is tightly regulated through multiple mechanisms, among which phosphorylation by kinases is critical in the posttranslational regulation of NRF2. For instance, PKC, casein kinase 2, and AMP-activated kinase positively, while GSK-3 negatively regulates NRF2 activity through phosphorylation of different sites. Here, we provide an overview of the phosphorylation regulation pattern of NRF2 and discuss the therapeutic potential of interventions targeting NRF2 phosphorylation.

Published
2021

9. Proteolysis-targeting chimeras: a kaleidoscope of targeted protein degradation

Author

Gao Xinxing, Yi Mou, Zheng-Yu Jiang, and Shuai Wen

Subjects
Pharmacology, medicine.diagnostic_test, biology, Chemistry, Ubiquitin-Protein Ligases, Proteolysis, Protein degradation, Kaleidoscope, Cell biology, Ubiquitin ligase, Drug Discovery, medicine, biology.protein, Humans, Molecular Medicine, Enzyme Inhibitors, computer, computer.programming_language
Published
2022

12. Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery

Author

Xiao-Li Xu, Lei Wang, Qidong You, and Zheng-Yu Jiang

Subjects
0303 health sciences, Small molecule inhibitors, biology, lcsh:RM1-950, Protein fate, Heat shock protein family, Protein level, Review, Computational biology, Protein Homeostasis, Small molecule, Protein–protein interaction, 03 medical and health sciences, lcsh:Therapeutics. Pharmacology, 0302 clinical medicine, 030220 oncology & carcinogenesis, Chaperone (protein), Heat shock protein, Molecular chaperone, biology.protein, Protein folding, General Pharmacology, Toxicology and Pharmaceutics, 030304 developmental biology
Abstract

Modulation of protein fate decision and protein homeostasis plays a significant role in altering the protein level, which acts as an orientation to develop drugs with new mechanisms. The molecular chaperones exert significant biological functions on modulation of protein fate decision and protein homeostasis under constantly changing environmental conditions through extensive protein–protein interactions (PPIs) with their client proteins. With the help of molecular chaperone machinery, the processes of protein folding, trafficking, quality control and degradation of client proteins could be arranged properly. The core members of molecular chaperones, including heat shock proteins (HSPs) family and their co-chaperones, are emerging as potential drug targets since they are involved in numerous disease conditions. Development of small molecule modulators targeting not only chaperones themselves but also the PPIs among chaperones, co-chaperones and clients is attracting more and more attention. These modulators are widely used as chemical tools to study chaperone networks as well as potential drug candidates for a broader set of diseases. Here, we reviewed the key checkpoints of molecular chaperone machinery HSPs as well as their co-chaperones to discuss the small molecules targeting on them for modulation of protein fate decision., Graphical abstract This review summarizes the current states on modulation of molecular chaperone by small molecules, focusing on the protein fate decision by comprehensive strategies and different mechanisms.Image 1

Published
2020

13. Myeloid cell leukemin-1 inhibitors: a growing arsenal for cancer therapy

Author

Zheng-Yu Jiang, Ze-Zhou Yu, Peng-Ju Zhu, and Qidong You

Subjects
0301 basic medicine, Poor prognosis, Myeloid, Cell, Cancer therapy, Antineoplastic Agents, Apoptosis, medicine.disease_cause, 03 medical and health sciences, 0302 clinical medicine, Drug Development, Neoplasms, hemic and lymphatic diseases, Puma, Drug Discovery, medicine, Animals, Humans, Pharmacology, biology, business.industry, biology.organism_classification, 030104 developmental biology, medicine.anatomical_structure, Proto-Oncogene Proteins c-bcl-2, 030220 oncology & carcinogenesis, Cancer research, Myeloid Cell Leukemia Sequence 1 Protein, Carcinogenesis, business
Abstract

B-cell lymphoma-2 (Bcl-2) family proteins, comprising proapoptotic proteins (Bax and Bak), antiapoptotic proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1, and A1) and BCL-2 homology domain 3 (BH3)-only proteins (Bid, Noxa, and Puma), have long been identified as pivotal apoptosis regulators. As an antiapoptotic member, myeloid cell leukemin-1 (Mcl-1) can bind with proapoptotic proteins and inhibit apoptosis. Mcl-1 is frequently overexpressed and closely associated with oncogenesis and poor prognosis in several cancers, posing a tremendous obstacle for cancer therapy. Recently, an increasing number of Mcl-1-selective small-molecule inhibitors have entered preclinical studies and advanced into clinical trials. In this review, we briefly introduce the role of Mcl-1 in apoptosis and highlight the recent development of Mcl-1 small-molecule inhibitors.

Published
2020

14. Petrocosmea nanchuanensis (Gesneriaceae), a new species from Chongqing, China

Author

Jun Zhang, Xavier-Ravi Baskaran, Zhi-Jing Qiu, Zheng-Yu Liu, Jin Hu, and Zhen-Yu Li

Subjects
Gynoecium, Asia, Petrocosmea, Lower lip, Stamen, Plant Science, Biology, Gesneriaceae, Magnoliopsida, Gesneriaceae new species Petrocosmea nanchuanensis, lcsh:Botany, Botany, Biodiversity & Conservation, China, Plantae, Ecology, Evolution, Behavior and Systematics, new species, Cenozoic, Longipedicellata, Leaf margin, biology.organism_classification, lcsh:QK1-989, Lamiales, Tracheophyta, Petrocosmea nanchuanensis, Research Article
Abstract

A new species, Petrocosmea nanchuanensis Z.Y. Liu, Z.Y. Li & Z.J. Qiu from Mt. Jinfo at Banhe valley of Nanchuan District in Chongqing Municipality (China) is described and illustrated for the first time. Even though this new species is similar to Petrocosmea barbata, it has several significant morphological differences, which includes smaller leaves, repand leaf margin, densely appressed longer pubescences on both surfaces of leaves, larger flower with length of its lower lips about three times longer than that of the upper lips, oblong lower lip lobes, shorter pistil, ovate anthers and styles that are shortly pubescent or approximately glabrous above the middle. The distinct features of P. nanchuanensis and four relative species namely, P. barbata, P. longipedicellata, P. cavaleriei and P. xanthomaculata were also represented in depth. However, P. nanchuanensis is most closely related to P. barbata, based on molecular studies.

Published
2020

15. Clinical features of LRP4/agrin‐antibody–positive myasthenia gravis: A multicenter study

Author

Ikjae Lee, Mazen M. Dimachkie, Andrea M. Corse, Carlayne E. Jackson, Hongyan Xu, Jerry M. Belsh, J. Americo Fernandes, Mamatha Pasnoor, Tuan Vu, Eroboghene E. Ubogu, James F. Howard, George A. Small, Robert P. Lisak, R. Bhavaraju Sanka, Vanessa Baute, James Caress, Lin Mei, Stephen N. Scelsa, Brandy Quarles, Zachary Simmons, Richard Nowak, Zheng Yu, Richard J. Barohn, Jin-Xiu Pan, Clifton L. Gooch, Michael H. Rivner, and Andrea Swenson

Subjects
0301 basic medicine, Adult, Male, medicine.medical_specialty, clinical features, Physiology, LRP4, neuromuscular transmission disorders, Class iii, 030105 genetics & heredity, Gastroenterology, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, Neuromuscular Transmission Disorders, Physiology (medical), Internal medicine, seronegative myasthenia gravis, medicine, Prevalence, Humans, LDL-Receptor Related Proteins, Clinical Research Articles, Autoantibodies, Clinical Research Article, myasthenia gravis, Agrin, biology, business.industry, Middle Aged, Clinical disease, medicine.disease, Myasthenia gravis, United States, Multicenter study, biology.protein, Female, Neurology (clinical), Antibody, Symptom Assessment, business, Standard therapy, agrin, 030217 neurology & neurosurgery
Abstract

Introduction Our aim in this study was to identify the prevalence and clinical characteristics of LRP4/agrin‐antibody–positive double‐seronegative myasthenia gravis (DNMG). Methods DNMG patients at 16 sites in the United States were tested for LRP4 and agrin antibodies, and the clinical data were collected. Results Of 181 DNMG patients, 27 (14.9%) were positive for either low‐density lipoprotein receptor–related protein 4 (LRP4) or agrin antibodies. Twenty‐three DNMG patients (12.7%) were positive for both antibodies. More antibody‐positive patients presented with generalized symptoms (69%) compared with antibody‐negative patients (43%) (P ≤ .02). Antibody‐positive patients’ maximum classification on the Myasthenia Gravis Foundation of America (MGFA) scale was significantly higher than that for antibody‐negative patients (P ≤ .005). Seventy percent of antibody‐positive patients were classified as MGFA class III, IV, or V compared with 39% of antibody‐negative patients. Most LRP4‐ and agrin‐antibody–positive patients (24 of 27, 89%) developed generalized myathenia gravis (MG), but with standard MG treatment 81.5% (22 of 27) improved to MGFA class I or II during a mean follow‐up of 11 years. Discussion Antibody‐positive patients had more severe clinical disease than antibody‐negative patients. Most DNMG patients responded to standard therapy regardless of antibody status.

Published
2020

16. Taxonomic scheme of the order Chaetophorales (Chlorophyceae, Chlorophyta) based on chloroplast genomes

Author

Huan Zhu, Benwen Liu, Zheng Yu Hu, Yu Xin Hu, and Guoxiang Liu

Subjects
0106 biological sciences, Nuclear gene, Chloroplasts, lcsh:QH426-470, lcsh:Biotechnology, Aphanochaetaceae, Gene order rearrangement, Germination, Chaetophoraceae, 010603 evolutionary biology, 01 natural sciences, DNA, Ribosomal, Synteny, Evolution, Molecular, 03 medical and health sciences, Chlorophyceae, Chlorophyta, lcsh:TP248.13-248.65, Oedogoniales, Genetics, Green algae, Genome, Chloroplast, Phylogeny, 030304 developmental biology, Chaetopeltidales, 0303 health sciences, Chaetophorales, biology, Phylogenetic tree, Genomics, Sequence Analysis, DNA, biology.organism_classification, Classification, Nuclear genes, lcsh:Genetics, Schizomeridaceae, Evolutionary biology, Biotechnology, Research Article
Abstract

Background: Order Chaetophorales currently includes six families, namely Schizomeridaceae, Aphanochaetaceae, Barrancaceae, Uronemataceae, Fritschiellaceae, and Chaetophoraceae. The phylogenetic relationships of Chaetophorales have been inferred primarily through phylogenetic analysis based on rDNA sequences. Most studies have primarily focused on intergeneric phylogenetic relationships within this order and the phylogenetic relationships with four other Chlorophycean orders (Chaetophorales, Chaetopeltidales and Oedogoniales, and Volvocales). The phylogenetic relationships among families in order Chaetophorales remain unclear. This study aimed to phylogenetically reconstruct order Chaetophorales and determine the taxonomic scheme and to further the current understanding of the evolution of order Chaetophorales . Results: In the present study, seven complete and five fragmentary chloroplast genomes were harvested. Phylogenomic and comparative genomic analysis were performed to determine the taxonomic scheme within Chaetophorales. Consequently, Oedogoniales was found to be a sister to a clade linking Chaetophorales and Chaetopeltidales. Schizomeriaceae, and Aphanochaetaceae clustered into a well-resolved basal clade in Chaetophorales, inconsistent with the results of phylogenetic analysis based on rDNA sequences. Comparative genomic analyses revealed that the chloroplast genomes of Schizomeriaceae and Aphanochaetaceae were highly conserved and homologous, highlighting the closest relationship in this order. Germination types of zoospores precisely correlated with the phylogenetic relationships. Conclusions: chloroplast genome structure analyses, synteny analyses, and zoospore germination analyses were concurrent with phylogenetic analyses based on the chloroplast genome, and all of them robustly determined the unique taxonomic scheme of Chaetophorales and the relationships of Oedogoniales, Chaetophorales, and Chaetopeltidales.

Published
2020

17. Human African trypanosomiasis: the current situation in endemic regions and the risks for non-endemic regions from imported cases

Author

Zhong-Dao Wu, De-Hua Lai, Geoff Hide, Jiang-Mei Gao, Zheng-Yu Qian, and Zhao-Rong Lun

Subjects
sub-Saharan Africa, medicine.medical_specialty, Endemic Diseases, Trypanosoma brucei gambiense, 030231 tropical medicine, Review Article, Biology, Positive correlation, 03 medical and health sciences, 0302 clinical medicine, Communicable Diseases, Imported, parasitic diseases, medicine, Humans, African trypanosomiasis, Non endemic, 030212 general & internal medicine, T. b. rhodesiense, Socioeconomics, China, Incidence, Public health, Incidence (epidemiology), Human African trypanosomiasis, Trypanosoma brucei rhodesiense, medicine.disease, Trypanosomiasis, African, Infectious Diseases, non-endemic disease countries, Animal Science and Zoology, Parasitology
Abstract

Human African trypanosomiasis (HAT) is caused by Trypanosoma brucei gambiense and Trypanosoma brucei rhodesiense and caused devastating epidemics during the 20th century. Due to effective control programs implemented in the last two decades, the number of reported cases has fallen to a historically low level. Although fewer than 977 cases were reported in 2018 in endemic countries, HAT is still a public health problem in endemic regions until it is completely eliminated. In addition, almost 150 confirmed HAT cases were reported in non-endemic countries in the last three decades. The majority of non-endemic HAT cases were reported in Europe, USA and South Africa, due to historical alliances, economic links or geographic proximity to disease-endemic countries. Furthermore, with the implementation of the ‘Belt and Road’ project, sporadic imported HAT cases have been reported in China as a warning sign of tropical diseases prevention. In this paper, we explore and interpret the data on HAT incidence and find no positive correlation between the number of HAT cases from endemic and non-endemic countries. This data will provide useful information for better understanding the imported cases of HAT globally in the post-elimination phase.

Published
2020

18. Combinational treatment of 5‐fluorouracil and casticin induces apoptosis in mouse leukemia <scp>WEHI</scp> ‐3 cells in vitro

Author

Wen-Wen Huang, Fu-Shin Chueh, Tzong-Der Way, Chia-Hsin Lin, Jing Gung Chung, Po-Yuan Chen, Zheng-Yu Cheng, Shu-Fen Peng, and Chao Lin Kuo

Subjects
Cell Survival, Health, Toxicology and Mutagenesis, Poly ADP ribose polymerase, Antineoplastic Agents, Apoptosis, 010501 environmental sciences, Management, Monitoring, Policy and Law, Toxicology, 01 natural sciences, Mice, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Cell Line, Tumor, medicine, Animals, Humans, Caspase, 0105 earth and related environmental sciences, Flavonoids, Membrane Potential, Mitochondrial, chemistry.chemical_classification, Reactive oxygen species, Leukemia, biology, Chemistry, Cytochromes c, Drug Synergism, General Medicine, medicine.disease, In vitro, Mitochondria, Cell culture, Caspases, 030220 oncology & carcinogenesis, biology.protein, Cancer research, Casticin, Fluorouracil, Reactive Oxygen Species, Signal Transduction
Abstract

Leukemia is one of the major diseases causing cancer-related deaths in the young population, and its cure rate is unsatisfying with side effects on patients. Fluorouracil (5-FU) is currently used as an anticancer drug for leukemia patients. Casticin, a natural polymethoxyflavone, exerts anticancer activity against many human cancer cell lines in vitro, but no other reports show 5-FU combined with casticin increased the mouse leukemia cell apoptosis in vitro. Herein, the antileukemia activity of 5-FU combined with casticin in WEHI-3 mouse leukemia cells was investigated in vitro. Treatment of two-drug combination had a higher decrease in cell viability and a higher increase in apoptotic cell death, the level of DNA condensation, and the length of comet tail than that of 5-FU or casticin treatment alone in WEHI-3 cells. In addition, the two-drug combination has a greater production rate of reactive oxygen species but a lower level of Ca2+ release and mitochondrial membrane potential (ΔΨm ) than that of 5-FU alone. Combined drugs also induced higher caspase-3 and caspase-8 activities than that of casticin alone and higher caspase-9 activity than that of 5-FU or casticin alone at 48 hours treatment. Furthermore, 5-FU combined with casticin has a higher expression of Cu/Zn superoxide dismutase (SOD [Cu/Zn]) and lower catalase than that of 5-FU or casticin treatment alone. The combined treatment has higher levels of Bax, Endo G, and cytochrome C of proapoptotic proteins than that of casticin alone and induced lower levels of B-cell lymphoma 2 (BCL-2) and BCL-X of antiapoptotic proteins than that of 5-FU or casticin only. Furthermore, the combined treatment had a higher expression of cleaved poly (ADP-ribose) polymerase (PARP) than that of casticin only. Based on these findings, we may suggest that 5-FU combined with casticin treatment increased apoptotic cell death in WEHI-3 mouse leukemia cells that may undergo mitochondria and caspases signaling pathways in vitro.

Published
2020

19. Nudix hydrolase 1 is a prognostic biomarker in hepatocellular carcinoma

Author

Jiong Bi, Jieyi Ma, Zheng Yu, Wen Li, Yucheng Hou, Longjuan Zhang, Ning Ma, Qifeng Ou, Ziming Wang, Rongchang Wang, Qiao Su, Fan Chen, and Xiao-Hui Huang

Subjects
Male, Aging, Carcinoma, Hepatocellular, medicine.drug_class, Biology, survival analysis, nomogram, medicine, Biomarkers, Tumor, Gene silencing, Humans, Gene, Survival analysis, Neoplasm Staging, Bile acid, Liver Neoplasms, Cell Biology, hepatocellular carcinoma, DNA, Neoplasm, Cell cycle, Middle Aged, medicine.disease, Prognosis, digestive system diseases, Phosphoric Monoester Hydrolases, Biomarker (cell), Up-Regulation, NUDT1, Gene Expression Regulation, Neoplastic, DNA Repair Enzymes, Hepatocellular carcinoma, Cancer research, biomarker, Transmembrane transporter activity, Female, Research Paper
Abstract

We investigated the prognostic significance of Nudix hydrolase 1 (NUDT1) in hepatocellular carcinoma (HCC). NUDT1 mRNA and protein levels were significantly higher in HCC tissues than normal liver tissues. The level of NUDT1 expression correlated with tumor grade, stage, size, differentiation, degree of vascular invasion, overall survival (OS), and disease-free survival (DFS) in HCC patients. Multivariate analysis showed that NUDT1 expression was an independent prognostic factor for OS and DFS in HCC patients. We constructed a prognostic nomogram with NUDT1 expression, AFP levels, vascular invasion, Child-Pugh classification, age, sex, AJCC staging, and tumor differentiation as variables. This nomogram was highly accurate in predicting the 5-year OS of HCC patients (c-index= 0.709; AUC= 0.740). NUDT1 silencing in HCC cells significantly reduced their survival, colony formation, migration, and invasiveness. Gene set enrichment analysis showed that biological pathways related to cell cycle, fatty acid metabolism, bile acid and bile salt metabolism, and PLK1 signaling were associated with NUDT1, as were the gene ontology terms "DNA binding transcription activator activity," "RNA polymerase II," "nuclear division," and "transmembrane transporter activity." Our study thus demonstrates that NUDT1 is a prognostic biomarker with therapeutic potential in HCC patients.

Published
2020

20. Role of serum cystatin C in the prediction of contrast-induced nephropathy after intra-arterial interventions

Author

Zheng-Yu Wang, Yong-Li Wang, Jian Wei, Long Jin, Zhen-Chang Wang, and Xiu-Yuan Hao

Subjects
Adult, Male, medicine.medical_specialty, Serum cystatin C, Contrast-induced nephropathy, Urology, lcsh:Medicine, Contrast Media, Renal function, Lower risk, Nephropathy, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Humans, Medicine, Cystatin C, Aged, Creatinine, biology, Receiver operating characteristic, business.industry, lcsh:R, Endovascular Procedures, Area under the curve, Angiography, Digital Subtraction, Arteries, Original Articles, General Medicine, Acute Kidney Injury, Middle Aged, medicine.disease, female genital diseases and pregnancy complications, Serum creatinine, chemistry, 030220 oncology & carcinogenesis, biology.protein, Female, business, 030217 neurology & neurosurgery, Glomerular Filtration Rate, Intra-arterial intervention
Abstract

Background: The diagnosis of contrast-induced nephropathy (CIN) is usually based on changes in serum creatinine (sCr). However, sCr has poor sensitivity as a biomarker of kidney injury. The aim of this study was to investigate the usefulness of serum cystatin C (sCysC) to predict CIN after intra-arterial interventions. Methods: A total of 360 consecutive patients underwent intra-arterial procedures using digital subtraction angiography. SCr, sCysC, and estimated glomerular filtration rate were measured at 1 to 2 days before and at 48, 72 h, and 7 days after the procedure. Results: Thirty-one patients (8.61%) developed CIN. Receiver operating characteristic (ROC) curve analysis showed that preoperative sCysC levels had good discriminatory power (area under the curve [AUC] = 0.634; 95% confidence interval [CI] = 0.526-0.743) for evaluating the risk of CIN after an endovascular procedure, with a sensitivity of 53.33% and specificity of 73.70%. ROC analysis showed that sCysC at 48 h after contrast medium administration was predictive of CIN after an endovascular procedure (AUC = 0.735; 95% CI = 0.647-0.822) with satisfactory sensitivity of 74.20% and specificity of 63.90%. Diabetes mellitus was an independent risk factor for CIN (odds ratio = 2.778; 95% CI = 1.045-7.382; P = 0.040). Conclusions: SCysC is an appropriate biomarker to predict the occurrence of CIN. Baseline sCysC before an intervention is useful to obtain a preliminary estimate of the risk of CIN. A 48-h cut-off value of sCysC of 0.99 mg/L after an endovascular procedure may help to rule out patients at lower risk of CIN. Key words: Contrast-induced nephropathy; Intra-arterial intervention; Serum cystatin C; Serum creatinine

Published
2020

21. Icariin Attenuates Diabetic Cardiomyopathy and Downregulates Extracellular Matrix Proteins in Heart Tissue of Type 2 Diabetic Rats

Author

Yuyin Ding, Jiye Aa, Xuan-Sheng Ding, Zheng-Yu Song, Hui Wang, Jun-Ye Tao, and Chen Qiao

Subjects
Male, Cardiotonic Agents, Diabetic Cardiomyopathies, Inflammation, Pharmacology, Diet, High-Fat, 030226 pharmacology & pharmacy, Streptozocin, Diabetes Mellitus, Experimental, Rats, Sprague-Dawley, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Insulin resistance, Fibrosis, Diabetic cardiomyopathy, medicine, Animals, Flavonoids, Epimedium, Extracellular Matrix Proteins, biology, business.industry, Myocardium, Type 2 Diabetes Mellitus, Heart, General Medicine, medicine.disease, biology.organism_classification, Streptozotocin, Rats, Diabetes Mellitus, Type 2, chemistry, cardiovascular system, medicine.symptom, business, Icariin, 030217 neurology & neurosurgery, medicine.drug
Abstract

Objective: Diabetic cardiomyopathy (DCM) is a serious complication of type 2 diabetes mellitus (T2DM), resulting in unfavorable prognosis. Icariin (ICA) is a major flavonoid isolated from the traditional oriental herbal medicine Epimedium that has been recently proved to show potential therapeutic efficacy on T2DM. The aim of this study was to investigate the underlying mechanism of how ICA improved DCM in rat models. Methods: To corroborate myocardial improvement by ICA, we managed to establish the T2DM rat model by streptozotocin (STZ) administration and high-glucose-high-fat diet. Results: The rats with T2DM showed severe insulin resistance, left ventricular dysfunction, aberrant lipids deposition, cardiac inflammation, and fibrosis compared with the control group. All these pathological symptoms were ameliorated by the treatment of ICA. The levels of extracellular matrix proteins of heart tissue significantly declined in ICA-treated rats. Conclusion: ICA may exert as a protector in T2DM-induced DCM by reducing extracellular matrix proteins in the heart tissue, implicating its potential role for the treatment of human DCM.

Published
2020

22. Distribution and Dimethylsulfoniopropionate Degradation of Dimethylsulfoniopropionate‐Consuming Bacteria in the Yellow Sea and East China Sea

Author

Rui Xu, Xue-Dan Wang, Jing-Guang Lai, Gui-Peng Yang, Sheng-Hui Zhang, Zheng-Yu Zhang, Juan Yu, Li-Jun Zhao, and Jiyuan Tian

Subjects
biology, Oceanography, biology.organism_classification, Dimethylsulfoniopropionate, chemistry.chemical_compound, Geophysics, chemistry, Space and Planetary Science, Geochemistry and Petrology, Environmental chemistry, Earth and Planetary Sciences (miscellaneous), Environmental science, Degradation (geology), DMSP lyase, Bacteria, China sea
Published
2021

23. Risk factors for progression of juvenile-onset non-radiographic axial spondyloarthritis to juvenile-onset ankylosing spondylitis: a nested case–control study

Author

Hao-Guang Li, Ling Lin, Dan-Min Wang, Shu-Xin Huang, Zheng-Yu Xiao, Feng-Cai Shen, and Zhi-Duo Hou

Subjects
medicine.medical_specialty, Immunology, Arthritis, Logistic regression, Gastroenterology, Rheumatology, Risk Factors, Internal medicine, Spondyloarthritis, Spondylarthritis, medicine, Immunology and Allergy, Humans, autoimmune diseases, Spondylitis, Ankylosing, Spondylitis, Retrospective Studies, Ankylosing spondylitis, biology, business.industry, C-reactive protein, Enthesitis, Buttock Pain, spondylitis, medicine.disease, juvenile, ankylosing, arthritis, Case-Control Studies, Nested case-control study, biology.protein, Medicine, medicine.symptom, business, Axial Spondyloarthritis
Abstract

ObjectiveTo evaluate the clinical characteristics of juvenile-onset non-radiographic axial spondyloarthritis (nr-axSpA) and to investigate risk factors associated with progression to juvenile-onset ankylosing spondylitis (JoAS).MethodsA nested case–control study was conducted using the retrospectively collected data of 106 patients with juvenile-onset nr-axSpA (age at disease onset, ResultsOverall, 58.5% of patients with juvenile-onset nr-axSpA presented with peripheral symptoms at disease onset. In 82.1% of these patients, axial with peripheral involvement occurred during the disease course. The rate of disease onset at >12 years and disease duration of ≤10 years were significantly higher in those with progression to JoAS than in those without progression to JoAS (83.0% vs 52.8%, p=0.001; 92.5% vs 56.6%, pConclusionPeripheral involvement was prevalent in juvenile-onset nr-axSpA. IBP, buttock pain, enthesitis, elevated baseline CRP levels and SIJ-MRI positivity in patients with the disease are associated with higher risk of progression to JoAS.

Published
2021

24. Exciton Origin of Color-Tuning in Ca2+-Binding Photosynthetic Bacteria

Author

Arvi Freiberg, Alexandra Lehtmets, Liina Kangur, Margus Rätsep, Zheng-Yu Wang-Otomo, and Kõu Timpmann

Subjects
QH301-705.5, Exciton, Light-Harvesting Protein Complexes, spectral red-shift, 010402 general chemistry, Photosynthesis, 01 natural sciences, Purple bacteria, Catalysis, Article, Ca2+-binding bacteria, Inorganic Chemistry, Absorbance, chemistry.chemical_compound, Pigment, Algae, Bacterial Proteins, 0103 physical sciences, Physical and Theoretical Chemistry, Biology (General), Molecular Biology, QD1-999, Bacteriochlorophylls, Spectroscopy, molecular excitons, photosynthesis, 010304 chemical physics, biology, Bacteria, Organic Chemistry, General Medicine, biology.organism_classification, light-harvesting, 0104 chemical sciences, Computer Science Applications, Chemistry, chemistry, Chemical physics, visual_art, visual_art.visual_art_medium, Calcium, Bacteriochlorophyll, Photosynthetic bacteria
Abstract

Flexible color adaptation to available ecological niches is vital for the photosynthetic organisms to thrive. Hence, most purple bacteria living in the shade of green plants and algae apply bacteriochlorophyll a pigments to harvest near infra-red light around 850–875 nm. Exceptions are some Ca2+-containing species fit to utilize much redder quanta. The physical basis of such anomalous absorbance shift equivalent to ~5.5 kT at ambient temperature remains unsettled so far. Here, by applying several sophisticated spectroscopic techniques, we show that the Ca2+ ions bound to the structure of LH1 core light-harvesting pigment–protein complex significantly increase the couplings between the bacteriochlorophyll pigments. We thus establish the Ca-facilitated enhancement of exciton couplings as the main mechanism of the record spectral red-shift. The changes in specific interactions such as pigment–protein hydrogen bonding, although present, turned out to be secondary in this regard. Apart from solving the two-decade-old conundrum, these results complement the list of physical principles applicable for efficient spectral tuning of photo-sensitive molecular nano-systems, native or synthetic.

Published
2021

25. Protein Kinases: Potential Drug Targets Against Schistosoma japonicum

Author

Kaijuan Wu, Xingyu Zhai, Shuaiqin Huang, Liping Jiang, Zheng Yu, and Jing Huang

Subjects
0301 basic medicine, Microbiology (medical), Drug, Asia, media_common.quotation_subject, 030231 tropical medicine, Immunology, Schistosomiasis, Drug resistance, Review, Biology, Microbiology, Schistosoma japonicum, 03 medical and health sciences, 0302 clinical medicine, Cellular and Infection Microbiology, schistosomiasis, parasitic diseases, drug targets, medicine, kinase inhibitors, Animals, Protein kinase A, media_common, protein kinases, Kinase, food and beverages, medicine.disease, biology.organism_classification, QR1-502, Praziquantel, 030104 developmental biology, Infectious Diseases, Pharmaceutical Preparations, Neglected tropical diseases, medicine.drug
Abstract

Schistosoma japonicum (S. japonicum) infection can induce serious organ damage and cause schistosomiasis japonica which is mainly prevalent in Asia and currently one of the most seriously neglected tropical diseases. Treatment of schistosomiasis largely depends on the drug praziquantel (PZQ). However, PZQ exhibits low killing efficacy on juvenile worms and the potential emergence of its drug resistance is a continual concern. Protein kinases (PKs) are enzymes that catalyze the phosphorylation of proteins and can participate in many signaling pathways in vivo. Recent studies confirmed the essential roles of PKs in the growth and development of S. japonicum, as well as in schistosome-host interactions, and researches have screened drug targets about PKs from S. japonicum (SjPKs), which provide new opportunities of developing new treatments on schistosomiasis. The aim of this review is to present the current progress on SjPKs from classification, different functions and their potential to become drug targets compared with other schistosomes. The efficiency of related protein kinase inhibitors on schistosomes is highlighted. Finally, the current challenges and problems in the study of SjPKs are proposed, which can provide future guidance for developing anti-schistosomiasis drugs and vaccines.

Published
2021

26. A Novel Membrane Protein in the Rhodobacter sphaeroides LH1-RC Photocomplex

Author

S. Kawamura, R. Kikuchi, Malgorzata Hall, Bruno M. Humbel, Yukihiro Kimura, Akira Mizoguchi, Nagashima Kvp, Ryo Kanno, Kazutoshi Tani, Leiye Yu, Zheng-Yu Wang-Otomo, and Michael T. Madigan

Subjects
chemistry.chemical_compound, Rhodobacter sphaeroides, Monomer, Rhodobacter, Membrane protein, biology, Chemistry, Stereochemistry, Hypothetical protein, Molecule, biology.organism_classification, Ring (chemistry), Integral membrane protein
Abstract

We present a cryo-EM structure of the monomeric light-harvesting-reaction center (LH1-RC) core complex from photosynthetic purple bacterium Rhodobacter (Rba.) sphaeroides at 2.9 Å resolution. The LH1 complex forms a C-shaped structure composed of 14 αβ-polypeptides around the RC with a large ring opening. From the cryo-EM density map, a previously unrecognized integral membrane protein, referred to as protein-U, was identified. Protein-U has a U-shaped conformation near the LH1-ring opening and was annotated as a hypothetical protein in the Rba. sphaeroides genome. Deletion of protein-U resulted in a mutant strain that expressed a much-reduced amount of the dimeric LH1-RC, indicating an important role for protein-U in dimerization of the LH1-RC complex. PufX was located opposite protein-U on the LH1-ring opening, and both its position and conformation differed from that of previous reports of dimeric LH1-RC structures obtained at low-resolution. Twenty-six molecules of the carotenoid spheroidene arranged in two distinct configurations were resolved in the Rba. sphaeroides LH1 and were positioned within the complex to block its pores. Our findings offer a new view of the core photocomplex of Rba. sphaeroides and the connections between structure and function in bacterial photocomplexes in general.

Published
2021

27. Community Dynamics of Fungi During the Progression of Human Non-Small-Cell Lung Cancer

Author

Wen Zhou, Juanjuan Xiang, Jingqun Tang, Anqi Chen, Minghua Wu, Yiming Zhao, Liyu Chen, Zheng Yu, Wei Jia, Leliang Zheng, and Junqi Yi

Subjects
Text mining, business.industry, Community dynamics, medicine, Cancer research, Non small cell, Biology, Lung cancer, medicine.disease, business, respiratory tract diseases
Abstract

Background: Lung cancer is the most common cancer worldwide. The correlation between lung microbiota dysbiosis and lung cancer has been explored. However, the characteristics of the lung mycobiome in lung cancer patients has not been fully examined. In this study, we performed metagenomic sequencing on bronchoalveolar lavage (BAL) from 24 patients with non-small-cell lung cancer (NSCLC) and 14 non-cancerous controls with benign mass. Results: We observed greater fungal diversity and connectivity in NSCLC patients compared to non-cancer controls. Network analysis revealed that the sum of degrees in NSCLC was more numerous, suggesting the connections of fungal communities were more active. The community networks were reconstructed in 4 main ecological modules. The module and network hubs included Vanderwaltozyma polyspora, Apiotrichum porosum, Lobosporangium transversal, Capronia epimyces and Pseudomicrostroma glucosiphilum. Random forest analysis and DESeq2 were performed to screen out distinct species in two seperate groups and 3 fungi Alternaria arborescens, Eremoyces bilateralis and Malassezia restricta were identified as potential diagnosis biomarkers for NSCLC patients. In these 3 fungi, the relative abundance of Alternaria arborescens was gradually increasing as NSCLC progressed. Conclusions: Taken together, our study innovatively proposes that changes in the structure of fungal communities in lung cancer may be closely related to lung carcinogenesis as well as its progression and the distinct species listed above could be used to detect and monitor NSCLC.

Published
2021

28. Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum

Author

Long-Jiang Yu, Malgorzata Hall, Bruno M. Humbel, Michael T. Madigan, Akira Mizoguchi, X.-C. Ji, Zheng-Yu Wang-Otomo, Kazutoshi Tani, Yukihiro Kimura, and Ryo Kanno

Subjects
Rhodospirillum, Phototroph, biology, Chemistry, Cryo-electron microscopy, Stereochemistry, Protein subunit, Rhodospirillum rubrum, Center (category theory), biology.organism_classification, Biochemistry, Quinone, chemistry.chemical_compound, Geranylgeraniol, Side chain, Molecule, Bacteriochlorophyll
Abstract

Rhodospirillum (Rsp.) rubrum is one of the most widely used model organisms in bacterial photosynthesis. This purple phototroph is characterized by the presence of both rhodoquinone (RQ) and ubiquinone as electron carriers and bacteriochlorophyll (BChl) a esterified at the propionic acid side chain by geranylgeraniol (BChl aG) instead of phytol. Despite intensive efforts, the structure of the light-harvesting-reaction center (LH1-RC) core complex from Rsp. rubrum remains at low resolutions. Using cryo-EM, here we present a robust new view of the Rsp. rubrum LH1-RC at 2.76 A resolution. The LH1 complex forms a closed, slightly elliptical ring structure with 16 αβ-polypeptides surrounding the RC. Our biochemical analysis detected RQ molecules in the purified LH1-RC, and the cryo-EM density map specifically positions RQ at the QA site in the RC. The geranylgeraniol side chains of BChl aG coordinated by LH1 β-polypeptides exhibit a highly homologous tail-up conformation that allows for interactions with the bacteriochlorin rings of nearby LH1 α-associated BChls aG. The structure also revealed key protein-protein interactions in both N- and C-terminal regions of the LH1 αβ-polypeptides, mainly within a face-to-face structural subunit. Our high-resolution Rsp. rubrum LH1-RC structure provides new insight for evaluating past experimental and computational results obtained with this old organism over many decades and lays the foundation for more detailed exploration of light-energy conversion, quinone transport, and structure-function relationships in this pigment-protein complex.

Published
2021

29. Evidence that sensitization to triple‐knockout pig cells will not be detrimental to subsequent allotransplantation

Author

Abhijit Jagdale, Zheng-Yu Wang, Huy Q Nguyen, Hayato Iwase, Takayuki Yamamoto, Mohamed H Bikhet, David K. C. Cooper, Hidetaka Hara, and David Ayares

Subjects
0301 basic medicine, Swine, Xenotransplantation, medicine.medical_treatment, Transplantation, Heterologous, Immunology, 030230 surgery, Peripheral blood mononuclear cell, Animals, Genetically Modified, 03 medical and health sciences, 0302 clinical medicine, Antigen, biology.animal, medicine, Animals, Sensitization, Transplantation, biology, business.industry, 030104 developmental biology, medicine.anatomical_structure, Leukocytes, Mononuclear, biology.protein, Heterografts, Antibody, business, Papio, Baboon, Allotransplantation
Abstract

The current evidence is that sensitization to a pig xenograft does not result in the development of antibodies that cross-react with alloantigens, and therefore, sensitization to a pig xenograft would not be detrimental to the outcome of a subsequent allograft. This evidence relates almost entirely to the transplantation of cells or organs from wild-type or α1,3-galactosyltransferase gene-knockout (GTKO) pigs. However, it is not known whether recipients of triple-knockout (TKO) pig grafts who become sensitized to TKO pig antigens develop antibodies that cross-react with alloantigens and thus be detrimental to a subsequent organ allotransplant. We identified a single baboon (B1317) in which no (or minimal) serum anti-TKO pig antibodies could be measured-in our experience unique among baboons. We sensitized it by repeated subcutaneous injections of TKO pig peripheral blood mononuclear cells (PBMCs) in the absence of any immunosuppressive therapy. After TKO pig PBMC injection, there was a transient increase in anti-TKO pig IgM, followed by a sustained increase in IgG binding to TKO cells. In contrast, there was no serum IgM or IgG binding to PBMCs from any of a panel of baboon PBMCs (n = 8). We conclude that sensitization to TKO pig PBMCs in the baboon did not result in the development of antibodies that also bound to baboon cells, suggesting that there would be no detrimental effect of sensitization on a subsequent organ allotransplant.

Published
2021

30. Metformin Increases Sarcolemma Integrity and Ameliorates Neuromuscular Deficits in a Murine Model of Duchenne Muscular Dystrophy

Author

Xia Dong, Tiankun Hui, Jie Chen, Zheng Yu, Dongyan Ren, Suqi Zou, Shunqi Wang, Erkang Fei, Huifeng Jiao, and Xinsheng Lai

Subjects
musculoskeletal diseases, Duchenne muscular dystrophy, medicine.medical_specialty, congenital, hereditary, and neonatal diseases and abnormalities, Neuromuscular disease, Physiology, Neuromuscular transmission, Neuromuscular junction, AMP-activated protein kinase, Internal medicine, Physiology (medical), medicine, QP1-981, skeletal muscle, biology, neuromuscular junction, business.industry, Skeletal muscle, AMPK, medicine.disease, Metformin, medicine.anatomical_structure, Endocrinology, biology.protein, business, metformin, medicine.drug
Abstract

Duchenne muscular dystrophy (DMD) is a genetic neuromuscular disease characterized by progressive muscle weakness and wasting. Stimulation of AMP-activated protein kinase (AMPK) has been demonstrated to increase muscle function and protect muscle against damage in dystrophic mice. Metformin is a widely used anti-hyperglycemic drug and has been shown to be an indirect activator of AMPK. Based on these findings, we sought to determine the effects of metformin on neuromuscular deficits in mdx murine model of DMD. In this study, we found metformin treatment increased muscle strength accompanied by elevated twitch and tetanic force of tibialis anterior (TA) muscle in mdx mice. Immunofluorescence and electron microscopy analysis of metformin-treated mdx muscles revealed an improvement in muscle fiber membrane integrity. Electrophysiological studies showed the amplitude of miniature endplate potentials (mEPP) was increased in treated mice, indicating metformin also improved neuromuscular transmission of the mdx mice. Analysis of mRNA and protein levels from muscles of treated mice showed an upregulation of AMPK phosphorylation and dystrophin-glycoprotein complex protein expression. In conclusion, metformin can indeed improve muscle function and diminish neuromuscular deficits in mdx mice, suggesting its potential use as a therapeutic drug in DMD patients.

Published
2021

31. Discovery of the pan-genotypic hepatitis C virus NS3/4A protease inhibitor voxilaprevir (GS-9857): A component of Vosevi®

Author

Kyla Ramey, Katana Ashley Anne, Kato Darryl, Tran Chinh Viet, Cheng Y. Yang, Link John O, Debi Jin, Yujin Wang, Kobayashi Tetsuya, Karki Kapil Kumar, Armando G. Villaseñor, Todd C. Appleby, Kelly Wang, Sangi Michael, Jeff Zablocki, Randy Vivian, Brian E. Schultz, Yang Zheng-Yu, Guofeng Cheng, Dustin Siegel, Zipfel Sheila, Ona Barauskas, James G. Taylor, Martinez Ruben, Katie Chan, and Adam J. Schrier

Subjects
Cyclopropanes, Aminoisobutyric Acids, Macrocyclic Compounds, Proline, Sofosbuvir, Lactams, Macrocyclic, Hepatitis C virus, Voxilaprevir, medicine.medical_treatment, Clinical Biochemistry, Pharmaceutical Science, Hepacivirus, Microbial Sensitivity Tests, Viral Nonstructural Proteins, medicine.disease_cause, Antiviral Agents, Heterocyclic Compounds, 4 or More Rings, 01 natural sciences, Biochemistry, Structure-Activity Relationship, Leucine, Quinoxalines, Drug Discovery, Genotype, medicine, Humans, Protease Inhibitors, Protease inhibitor (pharmacology), Molecular Biology, Sulfonamides, NS3, Protease, Dose-Response Relationship, Drug, Molecular Structure, biology, 010405 organic chemistry, Chemistry, Organic Chemistry, Virology, 0104 chemical sciences, Drug Combinations, 010404 medicinal & biomolecular chemistry, Alanine transaminase, biology.protein, Molecular Medicine, Carbamates, medicine.drug
Abstract

Treatment of hepatitis C virus (HCV) infection has been historically challenging due the high viral genetic complexity wherein there are eight distinct genotypes and at least 86 viral subtypes. While HCV NS3/4A protease inhibitors are an established treatment option for genotype 1 infection, limited coverage of genotypes 2 and/or 3 combined with serum alanine transaminase (ALT) elevations for some compounds has limited the broad utility of this therapeutic class. Our discovery efforts were focused on identifying an NS3/4A protease inhibitor with pan-genotypic antiviral activity, improved coverage of resistance associated substitutions, and a decreased risk of hepatotoxicity. Towards this goal, distinct interactions with the conserved catalytic triad of the NS3/4A protease were identified that improved genotype 3 antiviral activity. We further discovered that protein adduct formation strongly correlated with clinical ALT elevation for this therapeutic class. Improving metabolic stability and decreasing protein adduct formation through structural modifications ultimately resulted in voxilaprevir. Voxilaprevir, in combination with sofosbuvir and velpatasvir, has demonstrated pan-genotypic antiviral clinical activity. Furthermore, hepatotoxicity was not observed in Phase 3 clinical trials with voxilaprevir, consistent with our design strategy. Vosevi® (sofosbuvir, velpatasvir, and voxilaprevir) is now an approved pan-genotypic treatment option for the most difficult-to-cure individuals who have previously failed direct acting antiviral therapy.

Published
2019

32. HLA Class I–sensitized Renal Transplant Patients Have Antibody Binding to SLA Class I Epitopes

Author

Zheng-Yu Wang, James R. Butler, Devin E. Eckhoff, Joseph M. Ladowski, Clarkson Smith, Luz M. Reyes, Joseph Tector, Juliet L. Easlick, Jose Estrada, Gregory R. Martens, Matthew Tector, and Richard A. Sidner

Subjects
Antigenicity, Swine, Transplantation, Heterologous, Fc receptor, Human leukocyte antigen, 030230 surgery, Epitope, Epitopes, 03 medical and health sciences, 0302 clinical medicine, Antigen, Animals, Humans, Alleles, Transplantation, biology, Histocompatibility Testing, Histocompatibility Antigens Class I, fungi, Kidney Transplantation, Histocompatibility, Disease Models, Animal, Immunology, biology.protein, 030211 gastroenterology & hepatology, Antibody
Abstract

Background Highly sensitized patients are difficult to match with suitable renal allograft donors and may benefit from xenotransplant trials. We evaluate antibody binding from sensitized patients to pig cells and engineered single allele cells to identify anti-human leukocyte antigen (HLA) antibody cross-species reactivity with swine leukocyte antigen (SLA). These novel testing strategies assess HLA/SLA epitopes and antibody-binding patterns and introduce genetic engineering of SLA epitopes. Methods Sensitized patient sera were grouped by calculated panel reactive antibody and luminex single antigen reactivity profile and were tested with cloned GGTA1/CMAH/B4GalNT2 glycan knockout porcine cells. Pig reactivity was assessed by direct flow cytometric crossmatch and studied following elution from pig cells. To study the antigenicity of individual class I HLA and SLA alleles in cells, irrelevant sera binding to lymphoblastoid cells were minimized by CRISPR/Cas9 elimination of endogenous class I and class II HLA, B-cell receptor, and Fc receptor genes. Native HLA, SLA, and mutants of these proteins after mutating 144K to Q were assessed for antibody binding. Results Those with predominately anti-HLA-B&C antibodies, including Bw6 and Bw4 sensitization, frequently have low pig reactivity. Conversely, antibodies eluted from porcine cells are more commonly anti-HLA-A. Single HLA/SLA expressing engineered cells shows variable antigenicity and mutation of 144K to Q reduces antibody binding for some sensitized patients. Conclusions Anti-HLA antibodies cross-react with SLA class I in predictable patterns, which can be identified with histocompatibility strategies, and SLA class I is a possible target of genetic engineering.

Published
2019

33. The local immune landscape determines tumor PD-L1 heterogeneity and sensitivity to therapy

Author

Wei-Ming Lin, Xiang-Ming Lao, Bo Li, Dong-Ping Chen, Chun-Xiang Huang, Ming Mu, Limin Zheng, Zheng-Yu Liu, Dong-Ming Kuang, Qiyi Zhao, Zhi-liang Gao, and Yuan Wei

Subjects
Adult, Male, 0301 basic medicine, Myeloid, Adolescent, T-Lymphocytes, medicine.medical_treatment, Inflammation, Mice, SCID, B7-H1 Antigen, Mice, 03 medical and health sciences, 0302 clinical medicine, Immune system, Cancer immunotherapy, Mice, Inbred NOD, Neoplasms, PD-L1, medicine, Animals, Humans, Aged, biology, business.industry, Macrophages, Cancer, Hep G2 Cells, General Medicine, Middle Aged, medicine.disease, Xenograft Model Antitumor Assays, Immune checkpoint, Neoplasm Proteins, 030104 developmental biology, medicine.anatomical_structure, 030220 oncology & carcinogenesis, Cancer cell, Cancer research, biology.protein, Female, Immunotherapy, medicine.symptom, business, Research Article
Abstract

Programmed death-1 receptor ligand 1 (PD-L1) is a promising therapeutic target in aggressive cancers. However, immune landscapes and cancer hallmarks of human PD-L1(+) tumors as well as their roles in determining therapeutic efficacies are unknown. Here, we showed, in detailed studies of gene data regarding 9769 patients of 32 types of human cancers, that PD-L1 could not exclusively represent the IFN-γ signature and potentially signified proinflammatory myeloid responses in a tumor. PD-L1 heterogeneity endowed by local immune landscapes controlled cancer hallmarks and clinical outcomes of patients. Mechanically, NF-κB signal elicited by macrophage inflammatory responses generated PD-L1(+) cancer cells exhibiting capabilities to aggressively survive, support angiogenesis, and metastasize, whereas STAT1 signal triggered by activated T cells induced PD-L1(+) cancer cells susceptive to apoptosis. Importantly, PD-L1(+) cancer cells generated by macrophages established great resistance to conventional chemotherapy, cytotoxicity of tumor-specific effector T cells, and therapy of immune-checkpoint blockade. Therapeutic strategy combining immune-checkpoint blockade with macrophage depletion or NF-κB inhibition in vivo effectively and successfully elicited cancer regression. Our results provide insight into the functional features of PD-L1(+) tumors and suggest that strategies to influence functional activities of inflammatory cells may benefit immune-checkpoint blockade therapy.

Published
2019

34. Identification of novel genes associated with duck OASL in response to influenza A virus

Author

Yinhua Huang, Chu-ze Gao, Zheng-yu Liu, Enguang Rong, Yanling Xing, Lingling Chang, Xiaoxue Wang, Jia-xiang Hu, and Jinhua Liu

Subjects
0106 biological sciences, Immunoprecipitation, Agriculture (General), Plant Science, Biology, 01 natural sciences, Biochemistry, S1-972, Food Animals, duck OASL, Gene expression, influenza A virus, KEGG, Gene, Genetics, Messenger RNA, Ecology, Weighted correlation network analysis, 04 agricultural and veterinary sciences, compensatory mechanism, FYVE domain, 040103 agronomy & agriculture, 0401 agriculture, forestry, and fisheries, ANKFY1, Animal Science and Zoology, Ankyrin repeat, Agronomy and Crop Science, 010606 plant biology & botany, Food Science
Abstract

2´-5´-Oligoadenylate synthetase like protein (OASL) plays a key role in response to viral infections through selectively activating the OAS/RNase L or OASL/RIG-I signaling pathway. Although classic pathway of OASL is well-known, its regulated genes or co-actors are largely unknown. To study the possible molecular mechanism of duck OASL (dOASL), we performed RNA-sequencing (RNA-seq) and immunoprecipitation and mass spectrometry (IP-MS) at the level of mRNA and protein, respectively. For RNA-seq, we used DF1 cell lines (DF1dOASL+/+, DF1cOASL–/–, and DF1) with or without the CK/0513 H5N1 virus (A/chicken/huabei/0513/2007) infection. 1 737 differentially expressed genes (DEGs) were identified as candidate target genes regulated by dOASL. Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis and Weighted Correlation Network Analysis (WGCNA) were performed. We identified one important yellow co-expression module correlated with antiviral immune response. In this module, Ankyrin repeat and FYVE domain containing 1 (ANKFY1), harboring a BTB domain similar to the methyl CpG-binding protein 1 (MBD1) which bound to OASL in human, was regulated by dOASL. At protein level, 133 host proteins were detected. Interestingly, ANKFY1 was one of them binding to dOASL protein. Further phylogenomic and chromosomal syntenic analysis demonstrated MBD1 was absent in birds, while mammals retained. It is suggested that OASL-ANKFY1 interaction might act as a compensatory mechanism to regulate gene expression in birds. Our findings will provide a useful resource for the molecular mechanism research of dOASL.

Published
2019

35. A Dual Role for Ca2+ in Expanding the Spectral Diversity and Stability of Light-Harvesting 1 Reaction Center Photocomplexes of Purple Phototrophic Bacteria

Author

Yukihiro Kimura, Zheng-Yu Wang-Otomo, Mizuki Takenouchi, Shinji Takenaka, Shiori Nakagawa, Jörg Overmann, Yoshitaka Saga, Michie Imanishi, Shinichi Takaichi, and Michael T. Madigan

Subjects
Photosynthetic reaction centre, 0303 health sciences, Phototroph, Strain (chemistry), biology, Chemistry, 030302 biochemistry & molecular biology, Thiorhodovibrio, chemistry.chemical_element, Spectral diversity, Photochemistry, biology.organism_classification, Biochemistry, Sulfur, 03 medical and health sciences, Dual role, Bacteria
Abstract

The light-harvesting 1 reaction center (LH1-RC) complex in the purple sulfur bacterium Thiorhodovibrio (Trv.) strain 970 cells exhibits its LH1 Qy transition at 973 nm, the lowest-energy Qy absorpt...

Published
2019

36. Molecular expression characteristics confirm the malignancy concealed by morphological alterations in endometrial cancer after fertility-preserving treatment

Author

E. Yang, Dan Nie, Lei Li, Ting Wen Yi Hu, and Zheng Yu Li

Subjects
Adult, Oncology, medicine.medical_specialty, ARID1A, Malignancy, Atypical hyperplasia, Malignant transformation, 03 medical and health sciences, 0302 clinical medicine, Internal medicine, Biopsy, medicine, Humans, PTEN, Retrospective Studies, 030219 obstetrics & reproductive medicine, biology, medicine.diagnostic_test, business.industry, Endometrial cancer, Fertility Preservation, Obstetrics and Gynecology, General Medicine, medicine.disease, Endometrial Neoplasms, 030220 oncology & carcinogenesis, biology.protein, Biomarker (medicine), Female, business
Abstract

Fertility-preserving treatment (FPT) has been widely used for young patients with early stage endometrial cancer (EC). However, the literature on the effectiveness and safety of FPT remains controversial. The aim of this study was to investigate malignant transformation in EC after FPT by immunohistochemistry (IHC). A retrospective analysis of pre- and post-treatment biopsy specimens from 24 patients with grade 1 endometrioid adenocarcinoma (EAC) or complex atypical hyperplasia (CAH) was performed. The expression levels of ARID1A, PTEN, and β-catenin were assessed by IHC. The protein expression levels of ARID1A, PTEN, and β-catenin were not significantly different between pre- and post-treatment specimens. However, there was a significant difference between pre-treatment and normal specimens as well as between post-treatment and normal specimens. The protein expression of β-catenin was significantly increased in patients with progression compared with those without progression after FPT. The morphologic normalization of patients with EC after FPT may not be accompanied by the absence of tumor malignancy, and β-catenin may serve as a biomarker for the response to FPT. These results may contribute to a better understanding of the malignant transformation of EC after FPT and the optimization of treatment strategies for young patients with birth plans.

Published
2019

37. Integration of Neural Reward Processing and Appetite-Related Signaling in Obese Females: Evidence From Resting-State fMRI

Author

Zheng-Yu Zhang, Zhenghan Yang, Lixue Wang, Han Lv, Zhongtao Zhang, Mengyi Li, Kaixin Zhao, Zhenchang Wang, Jing Li, Wang Zheng, Ding Heyu, Peng Zhang, Feng-Xia Yu, Pengfei Zhao, and Yang Liu

Subjects
education.field_of_study, Fusiform gyrus, Resting state fMRI, Postcentral gyrus, Ventral striatum, Population, Biology, 030218 nuclear medicine & medical imaging, 03 medical and health sciences, Superior temporal gyrus, 0302 clinical medicine, medicine.anatomical_structure, medicine, Middle frontal gyrus, Radiology, Nuclear Medicine and imaging, Orbitofrontal cortex, education, Neuroscience
Abstract

BACKGROUND The reward-related regions have been considered a crucial component in the regulation of eating behavior. Furthermore, appetite-related regions associated with reward can influence eating behaviors through altered functional activity related to food in brain areas associated with emotion, memory, sensory processing, motor function, and cognitive control. PURPOSE To investigate the key nodes in obese females of reward-related regions and, based on key nodes, to evaluate the directionality of functional connectivity between key nodes and appetite-related regions. STUDY TYPE Prospective. POPULATION Twenty-eight obese and 28 normal-weight female controls of similar age. FIELD STRENGTH/SEQUENCE 3.0 T MRI and echo planar imaging (EPI) sequence, 3D BRAVO sequence. ASSESSMENT The fMRI data preprocessing was based on the Data Processing & Analysis of Brain Imaging and Statistical Parametric Mapping 12. Degree centrality calculation was based on the GRETNA toolkit and granger causality analysis were based on the DynamicBC toolbox. Statistical Tests: Independent two-sample t-tests were used to assess the differences in demographic and clinical data between two groups. Two-sample t-tests were conducted to test the difference in degree centrality and effective connectivity of key nodes between two groups. RESULTS Compared with normal-weight controls, obese females showed an increased degree centrality in the left ventral striatum/caudate (t = 2.96808, P < 0.05) and decreased degree centrality in right orbitofrontal cortex (OFC) (t = -3.3558, P < 0.05). The obese females showed directional effective connectivity between left ventral striatum/caudate and several regions (left inferior temporal gyrus, fusiform gyrus, postcentral gyrus, and right precentral gyrus) (P < 0.05). Directional effective connectivity was also observed between the right OFC and several regions (left middle temporal gyrus, cuneus, OFC, superior temporal gyrus, middle frontal gyrus, and right inferior parietal lobule) (P < 0.05). DATA CONCLUSION The left ventral striatum/caudate and right OFC are key nodes in reward-related regions. The key nodes with reward processing mainly enhance visual processing of information and further participate in cognitive, attention, and sensorimotor processing. LEVEL OF EVIDENCE 1. Technical Efficacy: Stage 4. J. Magn. Reson. Imaging 2019;50:541-551.

Published
2019

38. Chemical and biological study of aplysiatoxin derivatives showing inhibition of potassium channel Kv1.5

Author

Ting-Ting Fan, Jian Zhang, Gong Xiaoxia, Bing-Nan Han, Yang-Hua Tang, Hou-Wen Lin, Hui-Hui Zhang, Jing Wu, and Zheng-Yu Cao

Subjects
chemistry.chemical_classification, biology, Stereochemistry, General Chemical Engineering, Molecular Docking Analysis, 02 engineering and technology, General Chemistry, 010402 general chemistry, 021001 nanoscience & nanotechnology, Ring (chemistry), Lyngbya, biology.organism_classification, 01 natural sciences, Potassium channel, 0104 chemical sciences, chemistry.chemical_compound, chemistry, Aplysiatoxin, Ic50 values, 0210 nano-technology, Strong binding, Tricyclic
Abstract

Three new aplysiatoxins, neo-debromoaplysiatoxin D (1), oscillatoxin E (2) and oscillatoxin F (3), accompanied by four known analogues (4–7), were identified from the marine cyanobacterium Lyngbya sp. Structural frames differ amongst these metabolites, and therefore we classified compounds 1 and 4–6 as aplysiatoxins as they possess 6/12/6 and 6/10/6 tricyclic ring systems featuring a macrolactone ring, and compounds 2, 3 and 7 as oscillatoxins that feature a hexane-tetrahydropyran in a spirobicyclic system. Bioactivity experiments showed that compounds 1 and 4–6 presented significant expression of phosphor-PKCδ whereas compounds 2, 5 and 7 showed the most potent blocking activity against potassium channel Kv1.5 with IC50 values of 0.79 ± 0.032 μM, 1.28 ± 0.080 μM and 1.47 ± 0.138 μM, respectively. Molecular docking analysis supplementing the binding interaction of oscillatoxin E (2) and oscillatoxin F (3) with Kv1.5 showed oscillatoxin E (2) with a strong binding affinity of −37.645 kcal mol−1 and oscillatoxin F (3) with a weaker affinity of −32.217 kcal mol−1, further supporting the experimental data.

Published
2019

39. Avidity‐Based Selection of Tissue‐Specific CAR‐T Cells from a Combinatorial Cellular Library of CARs

Author

Richard A. Lerner, Ping Ren, Peixiang Ma, Zheng Yu, Jiaxing Tang, Chuyue Zhang, Kun Fan, Chenyu Min, Wei Sang, Guanglei Li, Xingxu Huang, Wei Zhu, Wenzhang Chen, Xuekai Zhu, and Guang Yang

Subjects
General Chemical Engineering, T cell, General Physics and Astronomy, Medicine (miscellaneous), 02 engineering and technology, CD38, Biology, 010402 general chemistry, 01 natural sciences, Biochemistry, Genetics and Molecular Biology (miscellaneous), Cell membrane, Antigen, In vivo, combinatorial antibody library, medicine, General Materials Science, Avidity, lcsh:Science, Full Paper, chimeric antigen receptor, General Engineering, Full Papers, 021001 nanoscience & nanotechnology, Chimeric antigen receptor, In vitro, 0104 chemical sciences, Cell biology, medicine.anatomical_structure, tumor‐associated antigen, lcsh:Q, 0210 nano-technology
Abstract

Using T‐cell chimeric antigen receptors (CAR‐T) to activate and redirect T cells to tumors expressing the cognate antigen represents a powerful approach in cancer therapy. However, normal tissues with low expression of tumor‐associated antigens (TAAs) can be mistargeted, resulting in severe side effects. An approach using a collection of T cells expressing a diverse, 106‐member combinatorial cellular library of CARs, in which members can be specifically enriched based on avidity for cell membrane antigens, is reported. Using CD38 as the target antigen, an efficient and effective selection of CARs specifically recognizing CD38+ tumor cells is demonstrated. These selected CAR‐T's produce cytokines known to be associated with T cell activation in a CD38 expression‐dependent manner. This avidity‐based selection endows the engineered T cells with minimal off‐tumor effects, while retaining robust antitumor efficacy both in vitro and in vivo. The described method may facilitate the application of CAR‐T therapy to TAAs previously considered undruggable., A novel polyclonal combinatorial cellular library of chimeric antigen receptors provides a comprehensive coverage of immune responses to specific antigens in vitro. An efficient and effective avidity‐based selection strategy takes advantage of paracrine signaling systems in cell–cell interactions, which endow the engineered T cells with robust antitumor efficacy both in vitro and in vivo with minimal on‐target off‐tumor effects.

Published
2021

40. Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

Author

Long-Jiang Yu, Koudai Okazaki, Zheng-Yu Wang-Otomo, Tomoaki Kawakami, Yukihiro Kimura, Tai Liang, and Michael T. Madigan

Subjects
Iron-Sulfur Proteins, Models, Molecular, 0301 basic medicine, Photosynthetic reaction centre, Cytochrome, Protein Conformation, Science, Photosynthetic Reaction Center Complex Proteins, Light-Harvesting Protein Complexes, General Physics and Astronomy, Electron donor, Heme, Bioenergetics, Chromatiaceae, Article, General Biochemistry, Genetics and Molecular Biology, Electron Transport, 03 medical and health sciences, Electron transfer, chemistry.chemical_compound, Protein structure, Bacterial Proteins, Biophysical chemistry, Photosynthesis, Integral membrane protein, X-ray crystallography, Binding Sites, Multidisciplinary, 030102 biochemistry & molecular biology, biology, Chemistry, General Chemistry, Electron transport chain, 030104 developmental biology, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, biology.protein, Biophysics, Cytochromes, Crystallization
Abstract

Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems., The high potential iron-sulfur (HiPIP) proteins are direct electron donors to the light-harvesting-reaction center complexes (LH1-RC) in photosynthetic β- and γ-Proteobacteria. Here, the authors present the 2.9 Å crystal structure of the HiPIP-bound LH1-RC complex from the thermophilic purple sulfur bacterium Thermochromatium tepidum and discuss mechanistic implications for the electron transfer pathway.

Published
2021

41. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Author

Klionsky, Daniel, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis, Adeli, Khosrow, Adolph, Timon, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed, Agrotis, Alexander, Aguilar, Patricia, Ahmad, S Tariq, Ahmed, Zubair, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo, Altan-Bonnet, Nihal, Altieri, Dario, Álvarez, Élida, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal, Ammanathan, Veena, An, Zhenyi, Andersen, Stig, Andrabi, Shaida, Andrade-Silva, Magaiver, Andres, Allen, Angelini, Sabrina, Ann, David, Anozie, Uche, Ansari, Mohammad, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas, Au, Alicia, Auberger, Patrick, Auner, Holger, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, Azzopardi, Maria, Baba, Misuzu, Backer, Jonathan, Backues, Steven, Bae, Dong-Hun, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric, Baek, Ahruem, Baek, Seung-Hoon, Baek, Sung Hee, Bagetta, Giacinto, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xiyuan, Bai, Yidong, Bairagi, Nandadulal, Baksi, Shounak, Balbi, Teresa, Baldari, Cosima, Balduini, Walter, Ballabio, Andrea, Ballester, Maria, Balazadeh, Salma, Balzan, Rena, Bandopadhyay, Rina, Banerjee, Sreeparna, Banerjee, Sulagna, Bánréti, Ágnes, Bao, Yan, Baptista, Mauricio, Baracca, Alessandra, Barbati, Cristiana, Bargiela, Ariadna, Barilà, Daniela, Barlow, Peter, Barmada, Sami, Barreiro, Esther, Barreto, George, Bartek, Jiri, Bartel, Bonnie, Bartolome, Alberto, Barve, Gaurav, Basagoudanavar, Suresh, Bassham, Diane, Bast, Robert, Basu, Alakananda, Batoko, Henri, Batten, Isabella, Baulieu, Etienne, Baumgarner, Bradley, Bayry, Jagadeesh, Beale, Rupert, Beau, Isabelle, Beaumatin, Florian, Bechara, Luiz, Beck, George, Beers, Michael, Begun, Jakob, Behrends, Christian, Behrens, Georg, Bei, Roberto, Bejarano, Eloy, Bel, Shai, Behl, Christian, Belaid, Amine, Belgareh-Touzé, Naïma, Bellarosa, Cristina, Belleudi, Francesca, Belló Pérez, Melissa, Bello-Morales, Raquel, Beltran, Jackeline Soares de Oliveira, Beltran, Sebastián, Benbrook, Doris Mangiaracina, Bendorius, Mykolas, Benitez, Bruno, Benito-Cuesta, Irene, Bensalem, Julien, Berchtold, Martin, Berezowska, Sabina, Bergamaschi, Daniele, Bergami, Matteo, Bergmann, Andreas, Berliocchi, Laura, Berlioz-Torrent, Clarisse, Bernard, Amélie, Berthoux, Lionel, Besirli, Cagri, Besteiro, Sebastien, Betin, Virginie, Beyaert, Rudi, Bezbradica, Jelena, Bhaskar, Kiran, Bhatia-Kissova, Ingrid, Bhattacharya, Resham, Bhattacharya, Sujoy, Bhattacharyya, Shalmoli, Bhuiyan, Md Shenuarin, Bhutia, Sujit Kumar, Bi, Lanrong, Bi, Xiaolin, Biden, Trevor, Bijian, Krikor, Billes, Viktor, Binart, Nadine, Bincoletto, Claudia, Birgisdottir, Asa, Bjorkoy, Geir, Blanco, Gonzalo, Blas-Garcia, Ana, Blasiak, Janusz, Blomgran, Robert, Blomgren, Klas, Blum, Janice, Boada-Romero, Emilio, Boban, Mirta, Boesze-Battaglia, Kathleen, Boeuf, Philippe, Boland, Barry, Bomont, Pascale, Bonaldo, Paolo, Bonam, Srinivasa Reddy, Bonfili, Laura, Bonifacino, Juan, Boone, Brian, Bootman, Martin, Bordi, Matteo, Borner, Christoph, Bornhauser, Beat, Borthakur, Gautam, Bosch, Jürgen, Bose, Santanu, botana, luis, Botas, Juan, Boulanger, Chantal, Boulton, Michael, Bourdenx, Mathieu, Bourgeois, Benjamin, Bourke, Nollaig, Bousquet, Guilhem, Boya, Patricia, Bozhkov, Peter, Bozi, Luiz, Bozkurt, Tolga, Brackney, Doug, Brandts, Christian, Braun, Ralf, Braus, Gerhard, Bravo-Sagua, Roberto, Bravo-San Pedro, José, Brest, Patrick, Bringer, Marie-Agnès, Briones-Herrera, Alfredo, Broaddus, V Courtney, Brodersen, Peter, Brodsky, Jeffrey, Brody, Steven, Bronson, Paola, Bronstein, Jeff, Brown, Carolyn, Brown, Rhoderick, Brum, Patricia, Brumell, John, Brunetti-Pierri, Nicola, Bruno, Daniele, Bryson-Richardson, Robert, Bucci, Cecilia, Buchrieser, Carmen, Bueno, Marta, Buitrago-Molina, Laura Elisa, Buraschi, Simone, Buch, Shilpa, Buchan, J Ross, Buckingham, Erin, Budak, Hikmet, Budini, Mauricio, Bultynck, Geert, Burada, Florin, Burgoyne, Joseph, Burón, M Isabel, Bustos, Victor, Büttner, Sabrina, Butturini, Elena, Byrd, Aaron, Cabas, Isabel, Cabrera-Benitez, Sandra, Cadwell, Ken, Cai, Jingjing, Cai, Lu, Cai, Qian, Cairó, Montserrat, Calbet, Jose, Caldwell, Guy, Caldwell, Kim, Call, Jarrod, Calvani, Riccardo, Calvo, Ana, Calvo-Rubio Barrera, Miguel, Camara, Niels OS, Camonis, Jacques, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Edward, Campbell-Valois, François-Xavier, Campello, Silvia, Campesi, Ilaria, Campos, Juliane, Camuzard, Olivier, Cancino, Jorge, Candido de Almeida, Danilo, Canesi, Laura, Caniggia, Isabella, Canonico, Barbara, Cantí, Carles, Cao, Bin, Caraglia, Michele, Caramés, Beatriz, Carchman, Evie, Cardenal-Muñoz, Elena, Cardenas, Cesar, Cardenas, Luis, Cardoso, Sandra, Carew, Jennifer, Carle, Georges, Carleton, Gillian, Carloni, Silvia, Carmona-Gutierrez, Didac, Carneiro, Leticia, Carnevali, Oliana, Carosi, Julian, Carra, Serena, Carrier, Alice, Carrier, Lucie, Carroll, Bernadette, Carter, A Brent, Carvalho, Andreia Neves, Casanova, Magali, Casas, Caty, Casas, Josefina, Cassioli, Chiara, Castillo, Eliseo, Castillo, Karen, Castillo-Lluva, Sonia, Castoldi, Francesca, Castori, Marco, Castro, Ariel, Castro-Caldas, Margarida, Castro-Hernandez, Javier, Castro-Obregon, Susana, Catz, Sergio, Cavadas, Claudia, Cavaliere, Federica, Cavallini, Gabriella, Cavinato, Maria, Cayuela, Maria, Cebollada Rica, Paula, Cecarini, Valentina, Cecconi, Francesco, Cechowska-Pasko, Marzanna, Cenci, Simone, Ceperuelo-Mallafré, Victòria, Cerqueira, João, Cerutti, Janete, Cervia, Davide, Cetintas, Vildan Bozok, Cetrullo, Silvia, Chae, Han-Jung, Chagin, Andrei, Chai, Chee-Yin, Chakrabarti, Gopal, Chakrabarti, Oishee, Chakraborty, Tapas, Chakraborty, Trinad, Chami, mounia, Chamilos, Georgios, Chan, David, Chan, Edmond, Chan, Edward, Chan, H.Y. Edwin, Chan, Helen, Chan, Hung, Chan, Matthew, Chan, Yau Sang, Chandra, Partha, Chang, Chih-Peng, Chang, Chunmei, Chang, Hao-Chun, Chang, Kai, Chao, Jie, Chapman, Tracey, Charlet-Berguerand, Nicolas, Chatterjee, Samrat, Chaube, Shail, Chaudhary, Anu, Chauhan, Santosh, Chaum, Edward, Checler, Frédéric, Cheetham, Michael, Chen, Chang-Shi, Chen, Guang-Chao, Chen, Jian-Fu, Chen, Liam, Chen, Leilei, Chen, Lin, Chen, Mingliang, Chen, Mu-Kuan, Chen, Ning, Chen, Quan, Chen, Ruey-Hwa, Chen, Shi, Chen, Wei, Chen, Weiqiang, Chen, Xin-Ming, Chen, Xiong-Wen, Chen, Xu, Chen, Yan, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Yue-Qin, Chen, Zhefan Stephen, Chen, Zhi, Chen, Zhi-Hua, Chen, Zhijian, Chen, Zhixiang, Cheng, Hanhua, Cheng, Jun, Cheng, Shi-Yuan, Cheng, Wei, Cheng, Xiaodong, Cheng, Xiu-Tang, Cheng, Yiyun, Cheng, Zhiyong, Chen, Zhong, Cheong, Heesun, Cheong, Jit Kong, Chernyak, Boris, Cherry, Sara, Cheung, Chi Fai Randy, Cheung, Chun Hei Antonio, Cheung, King-Ho, Chevet, Eric, Chi, Richard, Chiang, Alan Kwok Shing, Chiaradonna, Ferdinando, Chiarelli, Roberto, Chiariello, Mario, Chica, Nathalia, Chiocca, Susanna, Chiong, Mario, Chiou, Shih-Hwa, Chiramel, Abhilash, Chiurchiù, Valerio, Cho, Dong-Hyung, Choe, Seong-Kyu, Choi, Augustine, Choi, Mary, Choudhury, Kamalika Roy, Chow, Norman, Chu, Charleen, Chua, Jason, Chua, John Jia En, Chung, Hyewon, Chung, Kin Pan, Chung, Seockhoon, Chung, So-Hyang, Chung, Yuen-Li, Cianfanelli, Valentina, Ciechomska, Iwona, Cifuentes, Mariana, Cinque, Laura, Cirak, Sebahattin, Cirone, Mara, Clague, Michael, Clarke, Robert, Clementi, Emilio, Coccia, Eliana, Codogno, Patrice, Cohen, Ehud, Cohen, Mickael, Colasanti, Tania, Colasuonno, Fiorella, Colbert, Robert, Colell, Anna, Čolić, Miodrag, Coll, Nuria, Collins, Mark, Colombo, María, Colón-Ramos, Daniel, Combaret, Lydie, Comincini, Sergio, Cominetti, Márcia, Consiglio, Antonella, Conte, Andrea, Conti, Fabrizio, Contu, Viorica Raluca, Cookson, Mark, Coombs, Kevin, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corkery, Dale, Cordes, Nils, Cortese, Katia, Costa, Maria do Carmo, Costantino, Sarah, Costelli, Paola, Coto-Montes, Ana, Crack, Peter, Crespo, Jose, Criollo, Alfredo, Crippa, Valeria, Cristofani, Riccardo, Csizmadia, Tamas, Cuadrado, Antonio, Cui, Bing, Cui, Jun, Cui, Yixian, Cui, Yong, Culetto, Emmanuel, Cumino, Andrea, Cybulsky, Andrey, Czaja, Mark, Czuczwar, Stanislaw, D'Adamo, Stefania, D'Amelio, Marcello, D'Arcangelo, Daniela, D'Lugos, Andrew, D'Orazi, Gabriella, da Silva, James, Dafsari, Hormos Salimi, Dagda, Ruben, Dagdas, Yasin, Daglia, Maria, Dai, Xiaoxia, Dai, Yun, Dai, Yuyuan, Dal Col, Jessica, Dalhaimer, Paul, Dalla Valle, Luisa, Dallenga, Tobias, Dalmasso, Guillaume, Damme, Markus, Dando, Ilaria, Dantuma, Nico, Darling, April, Das, Hiranmoy, Dasarathy, Srinivasan, Dasari, Santosh, Dash, Srikanta, Daumke, Oliver, Dauphinee, Adrian, Davies, Jeffrey, Dávila, Valeria, Davis, Roger, Davis, Tanja, Dayalan Naidu, Sharadha, De Amicis, Francesca, De Bosscher, Karolien, De Felice, Francesca, De Franceschi, Lucia, De Leonibus, Chiara, de Mattos Barbosa, Mayara, De Meyer, Guido, De Milito, Angelo, De Nunzio, Cosimo, De Palma, Clara, De Santi, Mauro, De Virgilio, Claudio, De Zio, Daniela, Debnath, Jayanta, DeBosch, Brian, Decuypere, Jean-Paul, Deehan, Mark, Deflorian, Gianluca, DeGregori, James, Dehay, Benjamin, Del Rio, Gabriel, Delaney, Joe, Delbridge, Lea, Delorme-Axford, Elizabeth, Delpino, M Victoria, Demarchi, Francesca, Dembitz, Vilma, Demers, Nicholas, Deng, Hongbin, Deng, Zhiqiang, Dengjel, Joern, Dent, Paul, Denton, Donna, DePamphilis, Melvin, Der, Channing, Deretic, Vojo, Descoteaux, Albert, Devis, Laura, Devkota, Sushil, Devuyst, Olivier, Dewson, Grant, Dharmasivam, Mahendiran, Dhiman, Rohan, di Bernardo, Diego, Di Cristina, Manlio, Di Domenico, Fabio, Di Fazio, Pietro, Di Fonzo, Alessio, Di Guardo, Giovanni, Di Guglielmo, Gianni, Di Leo, Luca, Di Malta, Chiara, Di Nardo, Alessia, Di Rienzo, Martina, Di Sano, 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Eissa, N Tony, Eissa, Sanaa, Ejarque, Miriam, El Andaloussi, Abdeljabar, El-Hage, Nazira, El-Naggar, Shahenda, Eleuteri, Anna Maria, El-Shafey, Eman, Elgendy, Mohamed, Eliopoulos, Aristides, Elizalde, María, Elks, Philip, Elsasser, Hans-Peter, Elsherbiny, Eslam, Emerling, Brooke, Emre, N., Eng, Christina, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelsen, Agnete, Enserink, Jorrit, Escalante, Ricardo, Esclatine, Audrey, Escobar-Henriques, Mafalda, Eskelinen, Eeva-Liisa, Espert, Lucile, Eusebio, Makandjou-Ola, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Facchiano, Francesco, Fadeel, Bengt, Fader, Claudio, Faesen, Alex, Fairlie, W Douglas, Falcó, Alberto, Falkenburger, Bjorn, Fan, Daping, Fan, Jie, Fan, Yanbo, Fang, Evandro, Fang, Yanshan, Fang, Yognqi, Fanto, Manolis, Farfel-Becker, Tamar, Faure, Mathias, Fazeli, Gholamreza, Fedele, Anthony, Feldman, Arthur, Feng, Du, Feng, Jiachun, Feng, Lifeng, Feng, Yibin, Feng, Yuchen, Feng, Wei, Fenz Araujo, Thais, Ferguson, Thomas, Fernández, Álvaro, Fernandez-Checa, Jose, Fernández-Veledo, Sonia, Fernie, Alisdair, Ferrante, Anthony, Ferraresi, Alessandra, Ferrari, Merari, Ferreira, Julio, Ferro-Novick, Susan, Figueras, Antonio, Filadi, Riccardo, Filigheddu, Nicoletta, Filippi-Chiela, Eduardo, Filomeni, Giuseppe, Fimia, Gian Maria, Fineschi, Vittorio, Finetti, Francesca, Finkbeiner, Steven, Fisher, Edward, Fisher, Paul, Flamigni, Flavio, Fliesler, Steven, Flo, Trude, Florance, Ida, Florey, Oliver, Florio, Tullio, Fodor, Erika, Follo, Carlo, Fon, Edward, Forlino, Antonella, Fornai, Francesco, Fortini, Paola, Fracassi, Anna, Fraldi, Alessandro, Franco, Brunella, Franco, Rodrigo, Franconi, Flavia, Frankel, Lisa, Friedman, Scott, Fröhlich, Leopold, Frühbeck, Gema, Fuentes, Jose, Fujiki, Yukio, Fujita, Naonobu, Fujiwara, Yuuki, Fukuda, Mitsunori, Fulda, Simone, Furic, Luc, Furuya, Norihiko, Fusco, Carmela, Gack, Michaela, Gaffke, Lidia, Galadari, Sehamuddin, Galasso, Alessia, Galindo, Maria, Gallolu Kankanamalage, Sachith, Galluzzi, Lorenzo, Galy, Vincent, Gammoh, Noor, Gan, Boyi, Ganley, Ian, Gao, Feng, Gao, Hui, Gao, Minghui, Gao, Ping, Gao, Shou-Jiang, Gao, Wentao, Gao, Xiaobo, Garcera, Ana, Garcia, Maria Noé, Garcia, Verónica, García-del Portillo, Francisco, Garcia-Escudero, Vega, Garcia-Garcia, Aracely, Garcia-Macia, Marina, García-Moreno, Diana, Garcia-Ruiz, Carmen, García-Sanz, Patricia, Garg, Abhishek, Gargini, Ricardo, Garofalo, Tina, Garry, Robert, Gassen, Nils, Gatica, Damian, Ge, Liang, Ge, Wanzhong, Geiss-Friedlander, Ruth, Gelfi, Cecilia, Genschik, Pascal, Gentle, Ian, Gerbino, Valeria, Gerhardt, Christoph, Germain, Kyla, Germain, Marc, Gewirtz, David, Ghasemipour Afshar, Elham, Ghavami, Saeid, Ghigo, Alessandra, Ghosh, Manosij, Giamas, Georgios, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibson, Gary, Gibson, Spencer, Ginet, Vanessa, Giniger, Edward, Giorgi, Carlotta, Girao, Henrique, Girardin, Stephen, Giridharan, Mridhula, Giuliano, Sandy, Giulivi, Cecilia, Giuriato, Sylvie, Giustiniani, Julien, Gluschko, Alexander, Goder, Veit, Goginashvili, Alexander, Golab, Jakub, Goldstone, David, Golebiewska, Anna, Gomes, Luciana, Gomez, Rodrigo, Gómez-Sánchez, Rubén, Gomez-Puerto, Maria Catalina, Gomez-Sintes, Raquel, Gong, Qingqiu, Goni, Felix, González-Gallego, Javier, Gonzalez-Hernandez, Tomas, Gonzalez-Polo, Rosa, Gonzalez-Reyes, Jose, González-Rodríguez, Patricia, Goping, Ing Swie, Gorbatyuk, Marina, Gorbunov, Nikolai, Görgülü, Kıvanç, Gorojod, Roxana, Gorski, Sharon, Goruppi, Sandro, Gotor, Cecilia, Gottlieb, Roberta, Gozes, Illana, Gozuacik, Devrim, Graef, Martin, Gräler, Markus, Granatiero, Veronica, Grasso, Daniel, Gray, Joshua, Green, Douglas, Greenhough, Alexander, Gregory, Stephen, Griffin, Edward, Grinstaff, Mark, Gros, Frederic, Grose, Charles, Gross, Angelina, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Gu, Xueyan, Guan, Jun-Lin, Guardia, Carlos, Guda, Kishore, Guerra, Flora, Guerri, Consuelo, Guha, Prasun, Guillén, Carlos, Gujar, Shashi, 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Elena, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm, Ułamek-Kozioł, Marzena, Ulasov, Ilya, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir, Vaccari, Thomas, Vaccaro, Maria, Vahsen, Björn, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria, Valko, Ayelén, Vallee, Richard, Valverde, Angela, Van Den Berghe, Greet, van der Veen, Stijn, Van Kaer, Luc, van Loosdregt, Jorg, van Wijk, Sjoerd, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios, Vega-Naredo, Ignacio, Vega-Rubin-de-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre, Victor, Victor, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia, Vierstra, Richard, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David, Voitsekhovskaja, Olga, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick, Wakatsuki, Shuji, Walker, David, Walker, Mark, Walker, Simon, Walter, Jochen, Wandosell, Francisco, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, PengWei, Wang, PeiPei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, wang, yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy, Wegrzyn, Grzegorz, Wehman, Ann, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver, Weihl, Conrad, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally, Whitton, J Lindsay, Whitworth, Alexander, Wiktorska, Katarzyna, Wildenberg, Manon, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin, Williams, Roger, Williamson, Peter, Wilson, Richard, Winner, Beate, Winsor, Nathaniel, Witkin, Steven, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, Jinrong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin, Yiu, Stephanie Pei Tung, Yoo, Young, Yoshida, Kiyotsugu, Yoshii, Saori, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond, Zacks, David, Zaffagnini, Gabriele, Zambelli, Vanessa, Zanella, Isabella, Zang, Qun, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott, Zeng, Jialiu, Zeng, Ju-deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin, Zhang, Leshuai, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, ZHOU, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith, Stallings, Christina, Tong, Chun-Kit, Ahmad, S. Tariq, Alim Al-Bari, M. Abdul, Bechara, Luiz R.G., Behrens, Georg M.N., Bhuiyan, Md. Shenuarin, Broaddus, V. Courtney, Buchan, J. Ross, Burón, M. Isabel, Carter, A. Brent, Chan, Matthew T.V., Choi, Augustine M.K., D’Adamo, Stefania, D’Amelio, Marcello, D’Arcangelo, Daniela, D’Lugos, Andrew, D’Orazi, Gabriella, De Meyer, Guido R.Y., Delpino, M. Victoria, Distler, Jörg H.W., Dixon, Ian M.C., Dobson, Renwick C.J., 2nd Dorn, Gerald, Eissa, N. Tony, Engelsen, Agnete S.T., Fairlie, W. Douglas, Ferreira, Julio C.B., H.B., Ranjitha, Hanson, Phyllis I., Hejtmancik, J. Fielding, Ho, Idy H.T., Hobbs, G. Aaron, Hoet, Peter H.M., Huang, Michael L.H., Iyer, Anand Krishnan V., Johnson, Gail V.W., Joosten, Leo A.B., Karim, Md. Razaul, Kaufmann, Stefan H.E., Ko, Ben C.B., Leck, Lionel Y.W., Lima, Thania R.R., Livingston, J. Andrew, Martin, Alexandre P.J., Montes, L. Ruth, Murphy, J. Patrick, Ng, Charlene C.W., Nicolao, M. Celeste, O’Donovan, Tracey, O’Leary, Seónadh, O’Rourke, Eyleen, O’Sullivan, Mary, O’Sullivan, Timothy, Omary, M. Bishr, Pereira, Gustavo J.S., Ratnayaka, J. Arjuna, Riazuddin, S. Amer, Rouschop, Kasper M.A., Sanderson, J. Thomas, Scaglione, K. Matthew, Schapira, Anthony H.V., Scovassi, A. Ivana, St. Clair, Daret, Sunahara, Karen K.S., Symons, J. David, Triola, Gemma, van Wijk, Sjoerd J.L., Vanrell, M. Cristina, Vasconcelos, M. Helena, Whitton, J. Lindsay, Williams, Robin S.B., Wong, W. Wei-Lynn, Wu, William K.K., Yakhine-Diop, Sokhna M.S., Yu, W. Haung, Zhang, Kalin Y.B., Dong, X. Charlie, Ain Shams University [ASU], Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University [JGU], Medical University Graz, Centre de Recherche des Cordeliers [CRC (UMR_S_1138 / U1138)], Institut Pasteur d'Iran, Leibniz Institute of Plant Biochemistry [IPB], The University of Texas M.D. Anderson Cancer Center [Houston], Institut de pharmacologie moléculaire et cellulaire [IPMC], Lipides - Nutrition - Cancer [Dijon - U1231] [LNC], Centre méditerranéen de médecine moléculaire [C3M], Institut de Biologie Valrose [IBV], Petites Molécules de neuroprotection, neurorégénération et remyélinisation, Signalisation Hormonale, Physiopathologie Endocrinienne et Métabolique, Institut Cochin [IC UM3 (UMR 8104 / U1016)], Institut NeuroMyoGène [INMG], Paris-Centre de Recherche Cardiovasculaire [PARCC (UMR_S 970/ U970)], Marqueurs cardiovasculaires en situation de stress [MASCOT (UMR_S_942 / U942)], Institut de Recherche sur le Cancer et le Vieillissement [IRCAN], Centre de Recherche en Cancérologie de Marseille [CRCM], Centre for Integrative Biology - CBI [Inserm U964 - CNRS UMR7104 - IGBMC], Oncogenesis, Stress, Signaling [OSS], Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)], Institut de Biologie Intégrative de la Cellule [I2BC], Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH], Centre de Recherches en Cancérologie de Toulouse [CRCT], Physiopathologie et traitement des maladies du foie, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Institut de Génétique et de Biologie Moléculaire et Cellulaire [IGBMC], Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] [BIO-PEROXIL], Centre de recherche sur l'Inflammation [CRI (UMR_S_1149 / ERL_8252 / U1149)], Unité de génétique et biologie des cancers [U830], Laboratoire d'Optique et Biosciences [LOB], Institut des Maladies Métaboliques et Casdiovasculaires [UPS/Inserm U1297 - I2MC], Différenciation et communication neuronale et neuroendocrine [DC2N], Institut de Recherche en Cancérologie de Montpellier [IRCM - U1194 Inserm - UM], Centre d'Immunologie de Marseille - Luminy [CIML], Physiopathologie et imagerie des troubles neurologiques [PhIND], Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée [LBFA], Imagine - Institut des maladies génétiques (IHU) [Imagine - U1163], Institut Mondor de Recherche Biomédicale [IMRB], Franco-czech Laboratory for clinical research on obesity, University of Michigan [Ann Arbor], University of Michigan System, Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Université Côte d'Azur (UCA), Lipides - Nutrition - Cancer [Dijon - U1231] (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), 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)-Université Côte d'Azur (UCA), Institut de Biologie Valrose (IBV), 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)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Nutrition, Métabolisme, Aquaculture (NuMéA), Université de Pau et des Pays de l'Adour (UPPA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), 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), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de Recherche en Cancérologie de Marseille (CRCM), 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), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institute of genetics and molecular and cellular biology-Centre National de la Recherche Scientifique (CNRS), Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie et Génomique des Poissons (LPGP), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de génétique et biologie des cancers (U830), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et imagerie des troubles neurologiques (PhIND), Université de Caen Normandie (UNICAEN), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epithelial biology and disease - Liliane Bettencourt Chair of Developmental Biology (Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Biomécanique cellulaire et respiratoire (BCR), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Charles University [Prague]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by the National Institute of General Medical Sciences [GM131919]., Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Département Plateforme (PF I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO), Chinese Academy of Medical Sciences [Suzhou, Chine] (CAMS), Karolinska Institutet [Stockholm], Karolinska University Hospital [Stockholm], Department of Women's and Children's Health [Stockholm, Sweden], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-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), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-École polytechnique (X), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, FHU OncoAge - Pathologies liées à l’âge [CHU Nice] (OncoAge), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)-Institut de Pharmacologie Moléculaire et Cellulaire [UNIV Côte d'Azur] (UPMC), Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM), Life Sciences Institute [Ann Arbor, MI, USA], University of Michigan System-University of Michigan System, European Institute of Oncology IRCCS [Milan, Italy] (EIO), Ain Shams University (ASU), Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Réseau International des Instituts Pasteur (RIIP), Leibniz Institute of Plant Biochemistry (IPB), Hebrew University of Jerusalem, Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), 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)-Université Côte d'Azur (UCA), 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), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord, 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), Oncogenesis, Stress, Signaling (OSS), Institut des Maladies Métaboliques et Casdiovasculaires (UPS/Inserm U1297 - I2MC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Charles University [Prague] (CU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Klionsky, D. 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G., Puertollano, R., Puglielli, L., Pulinilkunnil, T., Puri, D., Puri, R., Puyal, J., Qi, X., Qi, Y., Qian, W., Qiang, L., Qiu, Y., Quadrilatero, J., Quarleri, J., Raben, N., Rabinowich, H., Ragona, D., Ragusa, M. J., Rahimi, N., Rahmati, M., Raia, V., Raimundo, N., Rajasekaran, N. -S., Ramachandra Rao, S., Rami, A., Ramirez-Pardo, I., Ramsden, D. B., Randow, F., Rangarajan, P. N., Ranieri, D., Rao, H., Rao, L., Rao, R., Rathore, S., Ratnayaka, J. A., Ratovitski, E. A., Ravanan, P., Ravegnini, G., Ray, S. K., Razani, B., Rebecca, V., Reggiori, F., Regnier-Vigouroux, A., Reichert, A. S., Reigada, D., Reiling, J. H., Rein, T., Reipert, S., Rekha, R. S., Ren, H., Ren, J., Ren, W., Renault, T., Renga, G., Reue, K., Rewitz, K., Ribeiro de Andrade Ramos, B., Riazuddin, S. A., Ribeiro-Rodrigues, T. M., Ricci, J. -E., Ricci, R., Riccio, V., Richardson, D. R., Rikihisa, Y., Risbud, M. V., Risueno, R. M., Ritis, K., Rizza, S., Rizzuto, R., Roberts, H. C., Roberts, L. D., Robinson, K. J., Roccheri, M. C., Rocchi, S., Rodney, G. G., Rodrigues, T., Rodrigues Silva, V. R., Rodriguez, A., Rodriguez-Barrueco, R., Rodriguez-Henche, N., Rodriguez-Rocha, H., Roelofs, J., Rogers, R. S., Rogov, V. V., Rojo, A. I., Rolka, K., Romanello, V., Romani, L., Romano, A., Romano, P. S., Romeo-Guitart, D., Romero, L. C., Romero, M., Roney, J. C., Rongo, C., Roperto, S., Rosenfeldt, M. T., Rosenstiel, P., Rosenwald, A. G., Roth, K. A., Roth, L., Roth, S., Rouschop, K. M. A., Roussel, B. D., Roux, S., Rovere-Querini, P., Roy, A., Rozieres, A., Ruano, D., Rubinsztein, D. C., Rubtsova, M. P., Ruckdeschel, K., Ruckenstuhl, C., Rudolf, E., Rudolf, R., Ruggieri, A., Ruparelia, A. A., Rusmini, P., Russell, R. R., Russo, G. L., Russo, M., Russo, R., Ryabaya, O. O., Ryan, K. M., Ryu, K. -Y., Sabater-Arcis, M., Sachdev, U., Sacher, M., Sachse, C., Sadhu, A., Sadoshima, J., Safren, N., Saftig, P., Sagona, A. 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P., Whitton, J. L., Whitworth, A. J., Wiktorska, K., Wildenberg, M. E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R. S. B., Williams, R. L., Williamson, P. R., Wilson, R. A., Winner, B., Winsor, N. J., Witkin, S. S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J. H., Wong, R. W., Wong, V. K. W., Wong, W. W. -L., Wu, A. -G., Wu, C., Wu, J., Wu, K. K., Wu, M., Wu, S. -Y., Wu, S., Wu, W. K. K., Wu, X., Wu, Y. -W., Wu, Y., Xavier, R. J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H. -T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C. -M., Xie, M., Xie, Y., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, L., Xu, W. W., Xu, X., Xue, Y., Yakhine-Diop, S. M. 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D., Zhang, H., Zhang, H. -L., Zhang, J., Zhang, J. -P., Zhang, K. Y. B., Zhang, L. W., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X. -W., Zhang, X. D., Zhang, Y., Zhang, Y. -D., Zhang, Y. -Y., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X. -F., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X. -L., Zheng, Y., Zheng, Z. -G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, J., Zhou, K., Zhou, R., Zhou, X. -J., Zhou, Y., Zhou, Z. -Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G. -Q., Zhu, H., Zhu, W. -G., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C. M., Ziviani, E., Zoladek, T., Zong, W. -X., Zorov, D. B., Zorzano, A., Zou, W., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X. C., Kenchappa, C. S., Lin, Y., Oshima, S., Rong, Y., Sluimer, J. C., Stallings, C. L., Tong, C. -K., and Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Programmed cell death, Settore BIO/06, Autophagosome, Autolysosome, [SDV]Life Sciences [q-bio], lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Autophagy-Related Proteins, Review, Computational biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Settore MED/04, 03 medical and health sciences, stress, Chaperone-mediated autophagy, ddc:570, Autophagy, LC3, Animals, Humans, cancer, Settore BIO/10, flux, lysosome, macroautophagy, neurodegeneration, phagophore, vacuole, Set (psychology), Molecular Biology, 030102 biochemistry & molecular biology, business.industry, Interpretation (philosophy), Autophagosomes, Cell Biology, Multicellular organism, 030104 developmental biology, Knowledge base, Biological Assay, Lysosomes, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.

Published
2021

42. Expression, purification and properties of the enzymes involved in lanthanide-dependent alcohol oxidation: XoxF4, XoxF5, ExaF/PedH, and XoxG4

Author

Zheng Yu, Yue Zheng, Jing Huang, Ludmila Chistoserdova, and Joseph Groom

Subjects
chemistry.chemical_classification, 0303 health sciences, Cytochrome, biology, 030303 biophysics, Substrate (chemistry), Alcohol, Electron acceptor, biology.organism_classification, Catalysis, 03 medical and health sciences, chemistry.chemical_compound, Enzyme, chemistry, Biochemistry, Alcohol oxidation, Gammaproteobacteria, biology.protein
Abstract

In this chapter we describe logistics, protocols and conditions for expression, purification and characterization of Ln3 +-dependent alcohol dehydrogenases representing three distinct phylogenetic clades of these enzymes, classified as XoxF4, XoxF5 and ExaF/PedH. We present data on the biochemical properties of a dozen enzymes, all generated by our group, in a comparative fashion. These enzymes display a range of properties in terms of substrate and metal specificities, pH and ammonium requirement, as well as catalytic constants. In addition, we describe a single novel cytochrome, XoxG4, that likely serves as a natural electron acceptor from XoxF5 in methanotrophs of the Gammaproteobacteria class.

Published
2021

43. Pig kidney xenotransplantation: Progress toward clinical trials

Author

Devin E. Eckhoff, Douglas J. Anderson, Jayme E. Locke, Huy Q Nguyen, Zheng-Yu Wang, Hayato Iwase, Jeremy B. Foote, Abhijit Jagdale, Wayne Paris, David Ayares, Takayuki Yamamoto, Vineeta Kumar, David K. C. Cooper, Mohamed H Bikhet, and Hidetaka Hara

Subjects
Graft Rejection, Swine, Transgene, Xenotransplantation, medicine.medical_treatment, Transplantation, Heterologous, 030230 surgery, Kidney, Animals, Genetically Modified, 03 medical and health sciences, 0302 clinical medicine, medicine, Animals, Humans, CD154, Transplantation, biology, business.industry, Graft Survival, Acquired immune system, Kidney Transplantation, Blockade, medicine.anatomical_structure, Immunology, biology.protein, Heterografts, 030211 gastroenterology & hepatology, Antibody, business
Abstract

Pig organ xenotransplantation offers a solution to the shortage of deceased human organs for transplantation. The pathobiological response to a pig xenograft is complex, involving antibody, complement, coagulation, inflammatory, and cellular responses. To overcome these barriers, genetic manipulation of the organ-source pigs has largely been directed to two major aims-(a) deletion of expression of the known carbohydrate xenoantigens against which humans have natural (preformed) antibodies, and (b) transgenic expression of human protective proteins, for example, complement- and coagulation-regulatory proteins. Conventional (FDA-approved) immunosuppressive therapy is unsuccessful in preventing an adaptive immune response to pig cells, but blockade of the CD40:CD154 costimulation pathway is successful. Survival of genetically engineered pig kidneys in immunosuppressed nonhuman primates can now be measured in months. Non-immunological aspects, for example, pig renal function, a hypovolemia syndrome, and rapid growth of the pig kidney after transplantation, are briefly discussed. We suggest that patients on the wait-list for a deceased human kidney graft who are unlikely to receive one due to long waiting times are those for whom kidney xenotransplantation might first be considered. The potential risk of infection, public attitudes to xenotransplantation, and ethical, regulatory, and financial aspects are briefly addressed.

Published
2020

44. Metagenomic Insight into Environmentally Challenged Methane-Fed Microbial Communities

Author

Ludmila Chistoserdova, Yue Zheng, Fauzi Haroon, Zheng Yu, Huan Wang, and Maria E. Hernandez

Subjects
Microbiology (medical), methanotrophic communities, media_common.quotation_subject, Zoology, Methylophilaceae, Microbiology, Methylococcaceae, Competition (biology), Methane, Article, 03 medical and health sciences, chemistry.chemical_compound, Virology, lcsh:QH301-705.5, Burkholderiales, 030304 developmental biology, media_common, 0303 health sciences, metagenomics, microcosm incubation, metatranscriptomics, biology, Bacteriovorax, 030306 microbiology, Bacteroidetes, biology.organism_classification, chemistry, lcsh:Biology (General), Metagenomics, Lacunisphaera, Microcosm
Abstract

In this study, we aimed to investigate, through high-resolution metagenomics and metatranscriptomics, the composition and the trajectories of microbial communities originating from a natural sample, fed exclusively with methane, over 14 weeks of laboratory incubation. This study builds on our prior data, suggesting that multiple functional guilds feed on methane, likely through guild-to-guild carbon transfer, and potentially through intraguild and intraspecies interactions. We observed that, under two simulated dioxygen partial pressures&mdash, low versus high&mdash, community trajectories were different, with considerable variability among the replicates. In all microcosms, four major functional guilds were prominently present, representing Methylococcaceae (the true methanotrophs), Methylophilaceae (the nonmethanotrophic methylotrophs), Burkholderiales, and Bacteroidetes. Additional functional guilds were detected in multiple samples, such as members of Opitutae, as well as the predatory species, suggesting additional complexity for methane-oxidizing communities. Metatranscriptomic analysis suggested simultaneous expression of the two alternative types of methanol dehydrogenases in both Methylococcaceae and Methylophilaceae, while high expression of the oxidative/nitrosative stress response genes suggested competition for dioxygen among the community members. The transcriptomic analysis further suggested that Burkholderiales likely feed on acetate that is produced by Methylococcaceae under hypoxic conditions, while Bacteroidetes likely feed on biopolymers produced by both Methylococcaceae and Methylophilaceae.

Published
2020

45. The laterodorsal tegmentum-ventral tegmental area circuit controls depression-like behaviors by activating ErbB4 in DA neurons

Author

Wanpeng Cui, Lin Mei, Zheng Yu, Fang Liu, Hongsheng Zhang, Guanglin Xing, Zhi-Peng Liu, Nannan Gao, Wen Cheng Xiong, Kai Zhao, Zhaoqi Dong, Bin Luo, Wen-Jun Zou, Heath L. Robinson, Xiao Ren, Hongsheng Wang, and Wenbing Chen

Subjects
biology, Chemistry, Receptor tyrosine kinase, Laterodorsal tegmentum, Social defeat, Ventral tegmental area, Cellular and Molecular Neuroscience, Psychiatry and Mental health, medicine.anatomical_structure, nervous system, Dopamine, mental disorders, medicine, biology.protein, Neuron, Kinase activity, Molecular Biology, Neuroscience, ERBB4, medicine.drug
Abstract

Dopamine (DA) neurons in the ventral tegmental area (VTA) are critical to coping with stress. However, molecular mechanisms regulating their activity and stress-induced depression were not well understood. We found that the receptor tyrosine kinase ErbB4 in VTA was activated in stress-susceptible mice. Deleting ErbB4 in VTA or in DA neurons, or chemical genetic inhibition of ErbB4 kinase activity in VTA suppressed the development of chronic social defeat stress (CSDS)-induced depression-like behaviors. ErbB4 activation required the expression of NRG1 in the laterodorsal tegmentum (LDTg); LDTg-specific deletion of NRG1 inhibited depression-like behaviors. NRG1 and ErbB4 suppressed potassium currents of VTA DA neurons and increased their firing activity. Finally, we showed that acute inhibition of ErbB4 after stress attenuated DA neuron hyperactivity and expression of depression-like behaviors. Together, these observations demonstrate a critical role of NRG1-ErbB4 signaling in regulating depression-like behaviors and identify an unexpected mechanism by which the LDTg-VTA circuit regulates the activity of DA neurons.

Published
2020

46. Design and Application of a Rotatory Device for Detecting Transient Ca 2+ Signals in Response to Mechanical Stimulation Using an Aequorin‐Based Ca 2+ Imaging System

Author

Zhou Jinrun, Zheng Yu, Keke Shang-Guan, Yan Liang, Peng Yingtong, and Wang Huiquan

Subjects
biology, Chemistry, Detector, Aequorin, biology.protein, Biophysics, Context (language use), Stimulation, General Medicine, Transient (oscillation), Luminescence, Calcium Measurement, Ca2 imaging
Abstract

Elevation of the cytosolic free calcium ion (Ca2+ ) concentration ([Ca2+ ]cyt ) is one of the earliest responses to biotic and abiotic stress in plant cells. Among the various Ca2+ detection systems available, aequorin-based luminescence Ca2+ imaging systems provide a relatively amenable and robust method that facilitates large-scale genetic-mutant screening based on [Ca2+ ]cyt responses. Compared to that mediated by chemical elicitors, mechanical stimulation-induced elevation of [Ca2+ ]cyt is considerably more rapid, occurring within 10 s following stimulation. Therefore, its assessment using aequorin-based Ca2+ imaging systems represents a notable challenge, given that a time interval of ≥1 min is required to reduce the background light before operating the photon imaging detector. In this context, we designed a device that can rotate automatically within the confines of an enclosed dark box, and using this, we can record [Ca2+ ]cyt dynamics immediately after plants had been rotated to induce mechanical stimulation. This tool can facilitate the study of perception and early signal transduction in response to mechanical stimulation on a large scale based on [Ca2+ ]cyt responses. © 2020 Wiley Periodicals LLC. Basic Protocol 1: Detection of background luminance signals in aequorin-transformed Arabidopsis seedlings using a photon imaging detector Basic Protocol 2: Construction of the rotatory device Basic Protocol 3: Calcium measurement in Arabidopsis seedlings after rotatory stimulation Basic Protocol 4: Data analysis and processing.

Published
2020

47. Human anti‐α‐fucose antibodies are xenoreactive toward GGTA1/CMAH knockout pigs

Author

A. Joseph Tector, Christopher Burlak, Zheng-Yu Wang, and R. Travis Taylor

Subjects
0301 basic medicine, Glycan, Swine, Xenotransplantation, medicine.medical_treatment, Transplantation, Heterologous, Immunology, Dot blot, 030230 surgery, Fucose, Epitope, Mixed Function Oxygenases, Animals, Genetically Modified, Gene Knockout Techniques, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Affinity chromatography, Antigens, Heterophile, medicine, Animals, Humans, Transplantation, biology, Lectin, Galactosyltransferases, Molecular biology, 030104 developmental biology, chemistry, Leukocytes, Mononuclear, biology.protein, Antibody
Abstract

Progress has been made in overcoming antibody-mediated rejection of porcine xenografts by deleting pig genes that produce unique carbohydrate epitopes. Pigs deficient in galactose α-1,3 galactose (gene modified: GGTA1) and neu5Gc (gene modified: CMAH) have reduced levels of human antibody binding. Previously we identified α-fucose as a glycan that was expressed in high levels on cells of GGTA1/CMAH KO pigs. To validate the α-fucose phenotype observed previously we compared lectin affinity toward human and pig serum glycoproteins by dot blot analysis and confocal microscopy. Human anti-fucose antibody isolated by affinity chromatography was tested for specificity to L-fucose by custom macroarray. The affinity and cytotoxicity of the isolated human anti-fucose antibody toward human and GGTA1/CMAH KO pig PBMCs was determined by flow cytometry. Dot blot and confocal analysis support out previous findings that α-fucose is more highly expressed in pigs than humans. Pig kidney glomeruli and tubules contain abundant α-fucose and may represent focal sites for anti-α-fucose antibody binding. The Isolated human anti-fucose IgA, IgG and IgM bound to GGTA1/CMAH KO pig PBMC and were cytotoxic. Interestingly, the isolated human IgG cross reacted with the methyl pentose, L-rhamnose. Human anti-fucose antibody bound and was cytotoxic to GGTA1/CMAH KO pig peripheral blood monocytes. We have shown that α-fucose is an abundant target for cytotoxic human antibody in the organs of genetically modified pigs important to xenotransplantation.

Published
2020

48. The final obstacle to successful pre‐clinical xenotransplantation?

Author

Jeremy B. Foote, David Ayares, Takayuki Yamamoto, Mohamed H Bikhet, Zheng-Yu Wang, Douglas J. Anderson, Hayato Iwase, Abhijit Jagdale, Hidetaka Hara, Yehua Cui, Huy Q Nguyen, Mahmoud Morsi, Henk-Jan Schuurman, Devin E. Eckhoff, and David K. C. Cooper

Subjects
Graft Rejection, medicine.medical_specialty, Swine, Transgene, Xenotransplantation, medicine.medical_treatment, Transplantation, Heterologous, Immunology, Biology, Organ transplantation, Animals, Genetically Modified, Immune system, Antigens, Heterophile, biology.animal, medicine, Animals, Humans, Transplantation, Genetically engineered, Clinical trial, biology.protein, Heterografts, Antibody, Papio, Baboon
Abstract

Genetically engineered pigs are now available for xenotransplantation in which all three known carbohydrate xenoantigens, against which humans have natural antibodies, have been deleted (triple-knockout [TKO] pigs). Furthermore, multiple human transgenes have been expressed in the TKO pigs, all of which are aimed at protecting the cells from the human immune response. Many human sera demonstrate no or minimal antibody binding to, and little or no cytotoxicity of, cells from these pigs, and this is associated with a relatively low T-cell proliferative response. Unfortunately, baboons and other Old World NHPs have antibodies against TKO pig cells, apparently directed to a fourth xenoantigen that appears to be exposed after TKO. In our experience, most, if not all, humans do not have natural antibodies against this fourth xenoantigen. This discrepancy between NHPs and humans is providing a hurdle to successful translation of pig organ transplantation into the clinic, and making it difficult to provide pre-clinical data that support initiation of a clinical trial. The potential methods by which this obstacle might be overcome are discussed. We conclude that, whatever currently available genetically engineered pig is selected for the final pre-clinical studies, this may not be the optimal pig for clinical trials.

Published
2020

49. The human T cell proliferative response to triple-knockout pig cells in mixed lymphocyte reaction

Author

Mahmoud Morsi, KaLia Burnette, David K. C. Cooper, David Ayares, Huy Q Nguyen, Zheng-Yu Wang, Mohamed H Bikhet, and Hidetaka Hara

Subjects
Transplantation, business.industry, Swine, T cell, Immunology, Transplantation, Heterologous, Heterologous, Biology, Mixed lymphocyte reaction, Lymphocyte Activation, T-Lymphocytes, Regulatory, Proliferative response, Article, Genetically modified organism, Animals, Genetically Modified, medicine.anatomical_structure, Text mining, Cancer research, medicine, Lymphocyte activation, Animals, Humans, Lymphocyte Culture Test, Mixed, business
Published
2020

50. Lycopene-Family Carotenoids Confer Thermostability on Photocomplexes from a New Thermophilic Purple Bacterium

Author

Toshiyuki Kurihara, Michael T. Madigan, Rikako Kishi, Zheng-Yu Wang-Otomo, Yukihiro Kimura, Shinichi Takaichi, Mai Honda, Ryuta Seto, Yusuke Tsukatani, and Shinji Takenaka

Subjects
Photosynthetic reaction centre, food.ingredient, Light-Harvesting Protein Complexes, Biochemistry, chemistry.chemical_compound, food, Lycopene, Bacterial Proteins, Amino Acid Sequence, Carotenoid, Thermostability, chemistry.chemical_classification, Hyphomicrobiaceae, biology, Photosystem I Protein Complex, Protein Stability, Thermophile, Diphenylamine, Temperature, Blastochloris, biology.organism_classification, Light intensity, chemistry, Bacteriochlorophyll, Sequence Alignment, Bacteria
Abstract

Blastochloris tepida is a newly described thermophilic purple bacterium containing bacteriochlorophyll b. Using purified light-harvesting 1 reaction center (LH1-RC) core complexes from Blc. tepida,...

Published
2020

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