Author: "Mian Wu" - Searchworks@Jio Institute Digital Library Search Results

447 results on '"Mian Wu"'

201. XIAP inhibits autophagy via XIAP-Mdm2-p53 signalling

Author: Xing Huang, Zhengsheng Wu, Yide Mei, and Mian Wu
Subjects: Have You Seen...?, Ubiquitin-Protein Ligases, Blotting, Western, X-Linked Inhibitor of Apoptosis Protein, Inhibitor of apoptosis, Article, General Biochemistry, Genetics and Molecular Biology, Mice, Ubiquitin, Downregulation and upregulation, Tumor Cells, Cultured, Autophagy, Immunoprecipitation, Animals, Humans, RNA, Small Interfering, Molecular Biology, PI3K/AKT/mTOR pathway, General Immunology and Microbiology, biology, General Neuroscience, Proto-Oncogene Proteins c-mdm2, HCT116 Cells, Immunohistochemistry, Cell biology, XIAP, Ubiquitin ligase, Microscopy, Electron, HEK293 Cells, Cell Transformation, Neoplastic, Starvation, biology.protein, Cancer research, Mdm2, RNA Interference, Tumor Suppressor Protein p53, Signal Transduction
Abstract: The primary role of autophagy is adaption to starvation. However, increasing evidence suggests that autophagy inhibition also plays an important role in tumorigenesis. Upregulation of X-linked inhibitor of apoptosis (XIAP) has been associated to a variety of human cancers, yet the underlying mechanisms remain obscure. Here, we report that XIAP suppresses autophagy by exerting a previously unidentified ubiquitin E3 ligase activity towards Mdm2, which is a negative regulator of p53. XIAP controls serum starvation-induced autophagy downstream of the PI3K/Akt pathway. In mouse models, inhibition of autophagy by XIAP promotes tumorigenecity of HCT116 cells. XIAP-mediated autophagy inhibition is also largely validated in clinical tumour samples. These findings reveal a novel XIAP-Mdm2-p53 pathway that mediates the inhibition of autophagy, by which XIAP may contribute to tumorigenesis.
Published: 2013

202. Preparation and Characteristics of a New Anion Exchange Resin from Agricultural by-Products, Cassava (Manihot esculenta) Stalk

Author: Chun Qiang Chen, Wei Ming Mo, Mian Wu Meng, Meng Lin Chen, Yu Long Lun, Wang Li, Min Jun Zhang, and Cai Yan Kang
Subjects: chemistry.chemical_compound, chemistry, Stalk, Pyridine, Chemical modification, Epichlorohydrin, General Medicine, Ion-exchange resin, Chemical synthesis, Dimethylamine, Nuclear chemistry, Catalysis
Abstract: A new type of anion exchange resin was prepared from cassava stalk (CS) after reaction with epichlorohydrin and dimethylamine in the presence of pyridine and N,N-dimethylformamide. In order to obtain the optimal conditions for the preparation of cassava stalk anion exchanger (CS-AE), the single influential factor experiments were carried out, with nitrate removal efficiency as indicator. Factors like dosage of CS and catalyst, experimental temperatures were examined. The results indicated that the optimal synthesis reaction parameters of dosages were CS: pyridine: dimethylamine = 2 g: 30 ml: 35 ml. The optimal experimental temperature was 100 °C; the catalytic temperature was a key factor in the preparation of CS-AE.
Published: 2013

203. Crystal structure and functional characterization of the human RBM25 PWI domain and its flanking basic region

Author: Zhenhua Shao, Fan Yang, Jihui Wu, Fudong Li, Dandan Qian, Minhao Wu, Yunyu Shi, Deshun Gong, and Mian Wu
Subjects: Models, Molecular, ssRNA, single-stranded RNA, RNA-binding protein, Biochemistry, Luc7AC, C-terminal region of Luc7A, Protein structure, GST, glutathione transferase, Protein Isoforms, GFP, green fluorescent protein, Genetics, dsDNA, double-stranded DNA, flanking basic region, RT, reverse transcription, Nuclear Proteins, RNA-Binding Proteins, NF, nucleic-acid-free, IPTG, isopropyl β-D-thiogalactopyranoside, RNA splicing, SR, serine- and arginine-rich, Research Article, Binding domain, SeMet, selenomethionine, RBM25, RNA-binding motif protein 25, rmsd, root mean square deviation, RNA Splicing, Molecular Sequence Data, bcl-X Protein, Luc7A, Computational biology, Biology, ss, splicing site, alternative splicing, HEK, human embryonic kidney, Splicing factor, FPA, fluorescence polarization assay, ssDNA, single-stranded DNA, Humans, Amino Acid Sequence, Binding site, Molecular Biology, Binding Sites, NP40, Nonidet P40, Alternative splicing, snRNP, small nuclear ribonucleoprotein, RNA, Bcl-x pre-mRNA, PWI domain, Cell Biology, RRM, RNA-recognition motif, WT, wild-type, Protein Structure, Tertiary, HEK293 Cells, RNA-binding protein motif 25 (RBM25), dsRNA, double-stranded RNA, SAD, single-wavelength anomalous dispersion, FAM, 6-carboxyfluorescein
Abstract: Human RBM25 (RNA-binding motif protein 25) is a novel splicing factor that contains a PWI domain, a newly identified RNA/DNA-binding domain, and regulates Bcl-x pre-mRNA alternative splicing. The flanking basic region has been suggested to serve as a co-operative partner of the PWI domain in the binding of nucleic acids, but the structure of this basic region is unknown. In the present paper, we report the crystal structure of the RBM25 PWI domain and its flanking basic region. The PWI domain is revealed to comprise a conserved four-helix bundle, and the flanking basic region forms two α-helices and associates with helix H4 of the PWI domain. These interactions promote directly the formation of an enlarged nucleic-acid-binding platform. Structure-guided mutagenesis reveals a positively charged nucleic-acid-binding surface in the RBM25 PWI domain that is entirely different from that in the SRm160 PWI domain. Furthermore, we show that the promotion of the pro-apoptotic Bcl-xS isoform expression by RBM25 is facilitated by the PWI domain in vivo. Thus the present study suggests that the PWI domain plays an important role in the regulation of Bcl-x pre-mRNA alternative splicing.
Published: 2013

204. Endoplasmic reticulum stress inhibits cell cycle progression via induction of p27 in melanoma cells

Author: Yide Mei, Chuanchun Han, Mian Wu, and Lei Jin
Subjects: Proteasome Endopeptidase Complex, Cell cycle checkpoint, Endoplasmic Reticulum, Antiviral Agents, chemistry.chemical_compound, Cell Line, Tumor, Humans, RNA, Small Interfering, Melanoma, S-Phase Kinase-Associated Proteins, biology, Tunicamycin, Endoplasmic reticulum, Ubiquitination, Cell Biology, Cell cycle, G1 Phase Cell Cycle Checkpoints, Ubiquitin ligase, Cell biology, chemistry, Cell culture, Unfolded Protein Response, biology.protein, Unfolded protein response, RNA Interference, G1 phase, Cyclin-Dependent Kinase Inhibitor p27
Abstract: The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the unfolded protein response (UPR), a stress signaling pathway. The UPR coordinates the induction of ER chaperones with decreased protein synthesis and growth arrest in G1 phase of the cell cycle. However, the molecular mechanism underlying UPR-induced G1 cell cycle arrest remains largely unknown. Here we report that activation of the UPR response by tunicamycin (TM), an ER stress inducer, leads to accumulation of p27 and G1 cell cycle arrest in melanoma cells. This accumulation of p27 is due to the inhibition on its polyubiquitination and subsequent degradation upon TM treatment. Correlated with p27 stabilization, the levels of Skp2, an E3 ligase for p27, are decreased in response to TM treatment. More importantly, knockdown of p27 greatly reduces TM-induced G1 cell cycle arrest. Taken together, these data implicate p27 as a critical mediator of ER stress-induced growth arrest.
Published: 2013

205. A new role of p53 in regulating lipid metabolism

Author: Xiaocheng Zhao, Xiang Gao, Xingwu Wang, Yide Mei, and Mian Wu
Subjects: Mice, Knockout, Mice, Genetics, Animals, Lipid metabolism, Cell Biology, General Medicine, Tumor Suppressor Protein p53, Pharmacology, Biology, Lipid Metabolism, Molecular Biology
Published: 2012

206. Study of ultrasonic cavitation during extraction of the peanut oil at varying frequencies

Author: Haile Ma, Mian Wu, Cunshan Zhou, Zhang Lei, Abu ElGasim A. Yagoub, Bei Wang, and Xiao Zhang
Subjects: Yield (engineering), Materials science, Acoustics and Ultrasonics, Acoustics, Organic Chemistry, Extraction (chemistry), 04 agricultural and veterinary sciences, 02 engineering and technology, 021001 nanoscience & nanotechnology, 040401 food science, Polyvinylidene fluoride, Inorganic Chemistry, chemistry.chemical_compound, 0404 agricultural biotechnology, Amplitude, chemistry, Cavitation, Chemical Engineering (miscellaneous), Environmental Chemistry, Waveform, Radiology, Nuclear Medicine and imaging, Ultrasonic sensor, 0210 nano-technology, Intensity (heat transfer)
Abstract: The ultrasonic extraction of oils is a typical physical processing technology. The extraction process was monitored from the standpoint of the oil quality and efficiency of oil extraction. In this study, the ultrasonic cavitation fields were measured by polyvinylidene fluoride (PVDF) sensor. Waveform of ultrasonic cavitation fields was gained and analyzed. The extraction yield and oxidation properties were compared. The relationship between the fields and cavitation oxidation was established. Numerical calculation of oscillation cycle was done for the cavitation bubbles. Results showed that the resonance frequency, fr, of the oil extraction was 40kHz. At fr, the voltage amplitude was the highest; the time was the shortest as reaching the amplitude of the waveform. Accordingly, the cavitation effect worked most rapidly, resulting in the strongest cavitation intensity. The extraction yield and oxidation properties were closely related to the cavitation effect. It controlled the cavitation oxidation effectively from the viewpoint of chemical and physical aspects.
Published: 2016

207. Speech perception of English as a foreign language by Mandarin Chinese speakers

Author: Mian Wu
Subjects: Communication, Speech perception, business.industry, language, English as a foreign language, business, Psychology, Mandarin Chinese, language.human_language, Linguistics
Published: 2016

208. Mastermind-like Transcriptional Coactivator 1 Overexpression Predicts Poor Prognosis in Human with Hepatocellular Carcinoma

Author: Jian, Wang, Sheng-Min, Zhang, Jia-Mian, Wu, Zhuo-Cai, Lu, Jian-Rong, Yang, Hong-Sheng, Wu, Hao, Chen, Bo, Lin, Rong-Hua, Xu, and Tian-Sheng, Cao
Subjects: Male, Carcinoma, Hepatocellular, Liver Neoplasms, Kaplan-Meier Estimate, Middle Aged, Prognosis, Immunohistochemistry, DNA-Binding Proteins, Liver, Humans, Female, Neoplasm Invasiveness, Proportional Hazards Models, Transcription Factors
Abstract: Mastermind-like transcriptional coactivator 1(MAML1) is a transcriptional coregulator of activators in various signaling pathways. High MAML1 was associated with tumorigenesis, progression, and aggressiveness in various tumors. The role of MAML in Hepatocellular Carcinoma (HCC), however, has not been directly addressed. The present study was to determine its association with clinicopathological characteristics and prognosis of HCC patients.MAML1 expression at protein level in human HCC and normal liver tissues was detected by immunohistochemistry analysis, which was further validated by high-throughput sequencing data TCGA dataset at mRNA level. Then, the association of MAML1 expression with clinicopathological features of HCC patients was statistically analyzed.Immunohistochemistry analysis found that MAML1 expression was significantly increased in HCC tissues compared with those in normal tissues (P=0.005). High MAML1 was dramatically associated with advanced clinical stage (P=0.019) and enhanced tumor invasion (P=0.019). The TCGA mRNA expression data showed that MAML1 was upregulated in HCC with young age (P=0.005). Kaplan-Meier survival curves revealed that HCC patients with high MAML1 levels had shorter survival (P=0.040). Furthermore, high MAML1 expression was an independent prognostic factor for HCC patients (HR 1.841, 95% CI 1.045-3.243; P=0.035).Our data suggests that MAML1 may play an important role in tumor progression of HCC. The increased expression of MAML1 may efficiently predict poor overall survival in HCC patients, and it may be a potential prognostic marker of this malignancy.
Published: 2016

209. Doping of three-dimensional porous carbon nanotube-graphene-ionic liquid composite into polyaniline for the headspace solid-phase microextraction and gas chromatography determination of alcohols

Author: Faqiong Zhao, Lulu Li, Baizhao Zeng, Mian Wu, and Yingying Feng
Subjects: Octanol, Chromatography, Gas, Analytical chemistry, Ionic Liquids, 02 engineering and technology, Carbon nanotube, Solid-phase microextraction, 01 natural sciences, Biochemistry, Analytical Chemistry, law.invention, chemistry.chemical_compound, law, Polyaniline, Spectroscopy, Fourier Transform Infrared, Environmental Chemistry, Spectroscopy, Solid Phase Microextraction, Undecanol, Aniline Compounds, Graphene, Nanotubes, Carbon, 010401 analytical chemistry, 021001 nanoscience & nanotechnology, 0104 chemical sciences, chemistry, Chemical engineering, Alcohols, Ionic liquid, Microscopy, Electron, Scanning, Dodecanol, Graphite, 0210 nano-technology
Abstract: In this work, ionic liquid (IL, i.e. 1-hydroxyethyl-3-methylimidazolium tetrafluoroborate), carboxyl multiwall carbon nanotubes (MWCNTs) and reduced graphene oxide (rGO) were used to prepare three-dimensional porous material (MWCNTs-rGO-IL) by one-step self-assembly, then it was co-electrodeposited with polyaniline (PANI) on stainless steel wires by cyclic voltammetry. The resulting coating (PANI-MWCNTs-rGO-IL) was characterized by using FT-IR and scanning electron microscopy etc, and it showed porous structure and had high thermal stability. Furthermore, it was found to be very suitable for the headspace solid-phase microextraction of alcohols (i.e. octanol, nonanol, geraniol, decanol, undecanol and dodecanol). By coupling with gas chromatography, wide linear ranges and low limits of detection (i.e. 2.2–28.3 ng L−1) were obtained for the alcohols. The coating also presented good repeatability and reproducibility; the relative standard deviations for intra-fiber and fiber-to-fiber were less than 5.6% (n = 5) and 7.0% (n = 5) respectively. In addition, the proposed method was successfully applied to the determination of alcohols in tea drinks, and the recoveries for standards added were 85.6–114%.
Published: 2016

210. A CK2-targeted Pt(IV) prodrug to disrupt DNA damage response

Author: Weiwei Hu, Xiaochao Huang, Shaohua Gou, Mian Wu, and Feihong Chen
Subjects: 0301 basic medicine, Male, Cancer Research, Time Factors, DNA Repair, Organoplatinum Compounds, Cell Cycle Proteins, Ataxia Telangiectasia Mutated Proteins, Rats, Sprague-Dawley, 0302 clinical medicine, Neoplasms, Prodrugs, Molecular Targeted Therapy, Phosphorylation, Cytotoxicity, Casein Kinase II, Genetics, Mice, Inbred BALB C, Chemistry, Nuclear Proteins, Hep G2 Cells, Prodrug, DNA-Binding Proteins, Drug Combinations, Oncology, 030220 oncology & carcinogenesis, embryonic structures, MCF-7 Cells, Female, medicine.drug, Signal Transduction, animal structures, DNA repair, DNA damage, Mice, Nude, Antineoplastic Agents, 03 medical and health sciences, Inhibitory Concentration 50, medicine, Animals, Humans, Protein Interaction Domains and Motifs, Naphthyridines, Protein Kinase Inhibitors, Adaptor Proteins, Signal Transducing, Aprataxin, Cisplatin, Dose-Response Relationship, Drug, fungi, HCT116 Cells, Xenograft Model Antitumor Assays, MDC1, 030104 developmental biology, Drug Design, Cancer cell, Cancer research, Trans-Activators, Phenazines, DNA Damage
Abstract: A Pt(IV) prodrug, Cx-platin, containing CX-4945 (a CK2 inhibitor) as an axial ligand was designed and prepared by targeting CK2 to disrupt DNA damage response. In vitro study indicated that Cx-platin had superior cytotoxicity to cisplatin against a number of cancer cell lines with distinct CK2-expressed levels, caused CK2-overexpressed cancer cells death via suppressing CK2-mediated DNA damage repair and reversed cisplatin resistance. Mechanistic investigation suggested that the potent antitumor activity of Cx-platin resulted from its major suppression of CK2-phosphorylated MDC1 to combine FHA domain of aprataxin to DNA double strand breaks (DSBs) caused by improved cellular uptakes of Pt and ATM deactivation. Further in vivo tests exhibited that Cx-platin displayed high tumor inhibition rates, increased weight gain, and hardly toxicity effects in contrast to cisplatin.
Published: 2016

211. Soybean Cyst Nematode Resistance Emerged via Artificial Selection of Duplicated Serine Hydroxymethyltransferase Genes

Author: Yun-Xia Chen, Li-Wei Liu, Yue-Yu Hang, Alexander E. Chu, Ping Wu, Mian Wu, Ying-Jie Zeng, Fang-Fang Ma, Cheng-Chen Liu, Jian-Qun Chen, Bin Wang, Xiao-Yi Wu, and Guang-Can Zhou
Subjects: 0106 biological sciences, 0301 basic medicine, Nonsynonymous substitution, Soybean cyst nematode, artificial selection, Plant Science, 01 natural sciences, 03 medical and health sciences, evolution, Gene duplication, Gene family, Allele, Gene, Original Research, Genetics, biology, fungi, Haplotype, gene duplication, food and beverages, biology.organism_classification, Null allele, 030104 developmental biology, Rhg4, SHMT, 010606 plant biology & botany
Abstract: A major soybean (Forrest cultivar) quantitative trait locus (QTL) gene, Rhg4, which controls resistance to soybean cyst nematodes (SCN), encodes the enzyme serine hydroxylmethyltransferase (SHMT). The resistant allele possesses two critical missense mutations (P130R and N358Y) compared to that of the sensitive allele, rhg4. To understand the evolutionary history of this gene, sequences of 117 SHMT family members from 18 representative plant species were used to reconstruct their phylogeny. According to this phylogeny, the plant SHMT gene family can be divided into two groups and four subgroups (Ia, Ib, IIa and IIb). Belonging to the Subgroup Ia lineage, the rhg4 gene evolved from a recent duplication event in Glycine spp. To further explore how the SCN-resistant allele emerged, both the rhg4 gene and its closest homolog, the rhg4h gene, were isolated from 33 cultivated and 68 wild soybean varieties. The results suggested that after gene duplication, the soybean rhg4 gene accumulated a higher number of nonsynonymous mutations than rhg4h did. Although a higher number of segregating sites and gene haplotypes were detected in wild soybeans than in cultivars, the SCN-resistant Rhg4 allele (represented by haplotype 4) was not found in wild varieties. Instead, a very similar allele, haplotype 3, was observed in wild soybeans at a frequency of 7.4%, although it lacked the two critical nonsynonymous substitutions. Taken together, these findings support that the SCN-resistant Rhg4 allele likely emerged via artificial selection during the soybean domestication process, based on a SCN-sensitive allele inherited from wild soybeans.
Published: 2016

212. P3‐354: Interventions for Dementia Caregivers in Chinese Populations: a Systematic Review

Author: Joanna Maselko, Truls Østbye, Jing Wang, Yuting Song, Kirsten Corazzini, Mian Wu, Bei Wu, Hanzhang Xu, Eleanor S. McConnell, and Jiakun Xu
Subjects: medicine.medical_specialty, Psychotherapist, Epidemiology, business.industry, Health Policy, Psychological intervention, medicine.disease, Psychiatry and Mental health, Cellular and Molecular Neuroscience, Developmental Neuroscience, Medicine, Dementia, Neurology (clinical), Geriatrics and Gerontology, business, Psychiatry
Published: 2016

213. Changes in T-lymphocytes in lung cancer patients after hyperthermic intraperitoneal chemotherapy or radiotherapy

Author: L Yan, G Y Shi, Li Wang, Hongwei Zhang, N Ba, and Mian Wu
Subjects: 0301 basic medicine, Hyperthermia, Adult, Male, medicine.medical_specialty, Lung Neoplasms, medicine.medical_treatment, T-Lymphocytes, Peripheral blood mononuclear cell, Gastroenterology, Metastasis, 03 medical and health sciences, 0302 clinical medicine, T-Lymphocyte Subsets, Internal medicine, Genetics, medicine, Humans, Lymphocyte Count, Lung cancer, Molecular Biology, Aged, Chemotherapy, business.industry, General Medicine, Hyperthermia, Induced, Middle Aged, medicine.disease, Flow Cytometry, Radiation therapy, 030104 developmental biology, 030220 oncology & carcinogenesis, Leukocytes, Mononuclear, Hyperthermic intraperitoneal chemotherapy, Female, business, Infiltration (medical)
Abstract: We investigated dynamic changes in T-lymphocyte subsets after hyperthermic intraperitoneal chemotherapy (HIPEC) or radiotherapy using flow cytometry. A total of 1423 lung cancer patients admitted to our hospital between October 2012 and July 2015 were enrolled, and age-matched healthy individuals served as controls. Peripheral blood mononuclear cells (PBMCs) were purified using standard Ficoll density gradient centrifugation, based on which CD3+, CD4+, and CD8+ T-cells were isolated. A surface marker was identified by flow cytometry. Immunohistochemical analysis determined the distribution of the cells in the tumor mass or adjacent tissues. A total of 957 patients (male: 555; female: 402; median age: 49.3 years) with lung cancer who had received only HIPEC or radiotherapy were enrolled. The patients were followed-up until death. No statistical difference was noticed between the patients who had received chemotherapy compared with the baseline levels. A remarkable elevation was noticed in the CD3+ T-cells in the patients three months after radiotherapy (78.71 ± 9.36 vs 68.15 ± 9.65, P < 0.05). The level of CD8+ in the patients who had received chemotherapy or radiotherapy was remarkably elevated in the post-treatment period (P < 0.05). The CD3+ and CD8+ T-cells were mainly expressed in the cytoplasm rather than in the adjacent tissues. The expression of CD3+ and CD4+ was correlated to tumor infiltration and metastasis. Remarkable elevation was noticed in the CD3+ T-cells in the patients three months after radiotherapy. The expression of CD3+ and CD4+ was negatively correlated to tumor infiltration and metastasis in non-small-cell lung cancer patients.
Published: 2016

214. Fine mapping of the Rsv1-h gene in the soybean cultivar Suweon 97 that confers resistance to two Chinese strains of the soybean mosaic virus

Author: Yun-Xia Chen, Zhu-Qing Shao, Fang-Fang Ma, Bin Wang, Xiao-Yi Wu, Ying-Na Liu, De-Xiao Li, Mian Wu, Jian-Qun Chen, Cheng-Chen Liu, Jia-Yin Yang, Ping Wu, and Wen-Ping Wu
Subjects: 0106 biological sciences, 0301 basic medicine, Genetic Markers, DNA, Plant, Potyvirus, Soybean mosaic virus, Locus (genetics), Genes, Plant, 01 natural sciences, Genome, 03 medical and health sciences, Genetics, Allele, Genotyping, Gene, Crosses, Genetic, Disease Resistance, Genes, Dominant, Plant Diseases, biology, food and beverages, General Medicine, biology.organism_classification, 030104 developmental biology, Phenotype, Genetic marker, Soybeans, Agronomy and Crop Science, 010606 plant biology & botany, Biotechnology, Microsatellite Repeats
Abstract: The Rsv1 - h gene in cultivar Suweon 97, which confers resistance to SMVs, was mapped to a 97.5-kb location (29,815,195–29,912,667 bp on chromosome 13) in the Rsv1 locus, thereby providing additional insights into the molecular nature underlying variations in resistance alleles in this particular locus. Soybean mosaic virus (SMV) is a well-known devastating pathogen of soybean (Glycine max (L.) Merrill.) causing significant yield losses and seed quality deterioration. A single dominant allele, Rsv1-h, which confers resistance to multiple SMV strains, was previously reported in the cultivar Suweon 97, but its exact location is unknown. In the present study, Suweon 97 was crossed with a SMV-sensitive cultivar, Williams 82. Inoculating 267 F 2 individuals with two Chinese SMV strains (SC6-N and SC7-N) demonstrated that one single dominant gene confers SMV resistance. Another 1,150 F 2 individuals were then screened for two simple sequence repeat (SSR) markers (BARCSOYSSR_13_1103 and BARCSOYSSR_13_1187) that flank the Rsv1 locus. Seventy-four recombinants were identified and 20 additional polymorphic SSR markers within the Rsv1 region were then employed in genotyping these recombinants. F 2:3 and F 3:4 recombinant lines were also inoculated with SC6-N and SC7-N to determine their phenotypes. The final data revealed that in Suweon 97, the Rsv1-h gene that confers resistance to SC6-N and SC7-N was flanked by BARCSOYSSR_13_1114 and BARCSOYSSR_13_1115, two markers that delimit a 97.5-kb region in the reference Williams 82 genome. In such region, eight genes were present, of which two, Glyma13g184800 and Glyma13g184900, encode the characteristic CC-NBS-LRR type of resistance gene and were considered potential candidates for Rsv1-h.
Published: 2016

215. Identification of Arbuscular Mycorrhiza (AM)-Responsive microRNAs in Tomato

Author: Yue Wu, Ping Wu, Jian-Qun Chen, Bin Wang, Xiao-Yi Wu, Cheng-Chen Liu, Yue-Yu Hang, Mian Wu, Li-Wei Liu, Fang-Fang Ma, and Zhu-Qing Shao
Subjects: 0301 basic medicine, Rhizophagus irregularis, Plant Science, lcsh:Plant culture, tomato, Genome, Deep sequencing, MiRBase, 03 medical and health sciences, Symbiosis, Arabidopsis, Botany, lcsh:SB1-1110, deep sequencing analysis, Original Research, Genetics, biology, fungi, food and beverages, arbuscular mycorrhiza symbiosis, biology.organism_classification, Medicago truncatula, MicroRNAs, 030104 developmental biology, Solanum
Abstract: A majority of land plants can form symbiosis with arbuscular mycorrhizal (AM) fungi. MicroRNAs (miRNAs) have been implicated to regulate this process in legumes, but their involvement in non-legume species is largely unknown. In this study, by performing deep sequencing of sRNA libraries in tomato roots and comparing with tomato genome, a total of 700 potential miRNAs were predicted, among them, 187 are known plant miRNAs that have been previously deposited in miRBase. Unlike the profiles in other plants such as rice and Arabidopsis, a large proportion of predicted tomato miRNAs was 24 nt in length. A similar pattern was observed in the potato genome but not in tobacco, indicating a Solanum genus-specific expansion of 24-nt miRNAs. About 40% identified tomato miRNAs showed significantly altered expressions upon Rhizophagus irregularis inoculation, suggesting the potential roles of these novel miRNAs in AM symbiosis. The differential expression of five known and six novel miRNAs were further validated using qPCR analysis. Interestingly, three up-regulated known tomato miRNAs belong to a known miR171 family, a member of which has been reported in Medicago truncatula to regulate AM symbiosis. Thus, the miR171 family likely regulates AM symbiosis conservatively across different plant lineages. More than 1000 genes targeted by potential AM-responsive miRNAs were provided and their roles in AM symbiosis are worth further exploring.
Published: 2016
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216. Erratum

Author: Sascha Martens, Masashi Narita, Rajkumar Cheluvappa, Kevin A. Roth, Ta Yuan Chang, Kartik Venkatachalam, Chang-Shen Lin, Sharon G. Adler, Flaminia Pavone, Dianwen Ju, Michelle A. Ozbun, Michael R. Duchen, Shu Feng Zhou, Wei-Guo Zhu, Aaron Di Antonio, Defeng Wu, Taixing Cui, Xu Guang Guo, Zhiping Xie, Lorena García Nannig, Eloy Bejarano, Stéphane D. Lemaire, Petro Starokadomskyy, Hyung Ryong Kim, Mario Pinar, Rebecca T. Marquez, Zvenyslava Husak, Anthony R. White, Joanna Poulton, Antonis S. Zervos, Shweta Sharma, Jochen Walter, Nicholas T. Ktistakis, Christopher H.K. Cheng, Sunhee Lee, Yuen Li Chung, Howard O. Fearnhead, Young J. Oh, Ivano Amelio, Guillermo A. Blanco, Jan Simak, Junfang Wu, Yingying Lu, Mary Kate McBrayer, Soo Han Bae, Ichizo Nishino, Hong-Ming Hu, Benjamin R. Underwood, Tomonori Kimura, Zexian Liu, Savithrama P. Dinesh-Kumar, Qian Yang, Andreas Kern, Hsing Jien Kung, Jan B. Parys, Cam Patterson, Celine Perier, Toshiro Okazaki, Daisuke Koya, Avinash Sonawane, Cédric Cleyrat, Robert I. Richards, Kai Y. Soo, Rodrigo Mora-Rodriguez, Gigi N.C. Chiu, Moon Moo Kim, Vladimir N. Uversky, Shengfang Ge, Matthew T. V. Chan, Irene Kyrmizi, Lara Gibellini, Ángela M. Valverde, Erik Norberg, Fan Zhang, Jan C. Koch, Alec C. Kimmelman, Jingfang Ju, Jie Bai, Lei Duan, Paulina Ordonez, Shuwen Liu, Wolfdieter Springer, Eric Deutsch, Elena Ortona, Jose M. Seguí-Simarro, Vinay Choubey, Leonidas Stefanis, Robert G. Hawley, Claudia Bincoletto, Xian-Hui He, Zhifen Yang, Thomas M. Durcan, Martine Biard-Piechaczyk, Kui Lin, Hongming Pan, Konstantinos Kambas, Cristina Muñoz-Pinedo, Marta Magariños, Yoshinori Takahashi, Adrienne M. Gorman, Philippe Gailly, Takahiko Akematsu, Justine D. Mintern, Liang Xu, Tetsuo Shioi, Luis M. Botana, Yule Liu, Yong Yeon Cho, Jinzhi Lei, Eung Kweon Kim, Alakananda Basu, Vikash Kumar Dubey, Candelaria Gomez-Manzano, Avital Eisenberg-Lerner, Chuan-Ming Xie, Wenjie Dai, Pedro Gonzalez-Alegre, Maria Condello, Zheng-Hong Qin, Zhi-Min Yuan, Catherine Andreadi, Anna Rita Migliaccio, Chong Liu, Michaël Boyer-Guittaut, Melanie Denizot, Esperanza Arias, Greet Van den Berghe, Guomei Tang, Timothy P. Devarenne, Xianyong Sheng, Louis R. Lapierre, J. Wade Harper, Zuzana Storchova, Aileen R. Ariosa, Sug Hyung Lee, Qi Zeng, Godefridus J. Peters, Daniela L. Papademetrio, Alexandre Arcaro, Zhiyuan Yao, Pablo Iribarren, Mario Chiariello, Maria Rosaria Torrisi, Parimal Karmakar, Yong Huang, Sebastiano Sciarretta, Nathalie Andrieu-Abadie, László Fésüs, Patricia Boya, Ruediger Rudolf, Leonor Miller-Fleming, Vasilis J. Promponas, Juan Segura-Aguilar, Paula Daza, Shiow Ju Lee, Songshu Meng, Paul K. Herman, Ludwig Eichinger, Ye-Guang Chen, Kay F. Macleod, Thomas Simmet, Cristina Corral-Ramos, Claudio Brancolini, Jun Ren, Ying Jiang, Benoît Derrien, Xiao Fang Yu, Qing Zhong, Zong Wan Mao, Xingcong Ren, Armando A. Genazzani, Marina Pierdominici, Sanbing Shen, Sandra Moreno, Hana Algül, Maurizio Renna, Ricardo Sánchez-Prieto, Ashok K. Saluja, Yasuo Uchiyama, Pope L. Moseley, Victor E. Dosenko, Chun-Feng Liu, Bakhos A. Tannous, Efthimios Sivridis, Baharia Mograbi, Michiko Shintani, Amanda S. Bess, Rodrigo Portes Ureshino, Avnika A. Ruparelia, Paul Hofman, Eric Chevet, Martha M. Monick, Hong Gang Wang, Daping Fan, Jorge Moscat, Giuseppe Matarese, Consiglia Pacelli, Young Seok Cho, Miriam Cnop, Stefan Böckler, Nikolai V. Gorbunov, Christina J. Sigurdson, Hang T.T. Nguyen, Aurélie François, Katarina Kågedal, Sam Gandy, Silvia Campello, Alain Bruhat, Filomena Fiorito, Hua Feng, Man Tian Mi, Gian Maria Fimia, Masaki Tanaka, Guofei Zhou, José L. Crespo, Heinz Jungbluth, Anna Chiara Nascimbeni, Arianne L. Theiss, Svetlana Dokudovskaya, Mar Lorente, Sergio Lavandero, Yu Xia Zhao, Fangming Lin, Yuchen Feng, Gad Galili, Silvia Cetrullo, Paula I. Moreira, Dhyan Chandra, Dimitrios J. Stravopodis, Roberta A. Gottlieb, Gregory A. Taylor, Longping Wen, Faqiang Li, Marco Sardiello, Umesh K. Jinwal, Francesca Belleudi, Lan Tan, Livia Di Renzo, Tamas Korcsmaros, Xinbing Sui, Douglas R. Green, Guillermo Mazzolini, Hervé Le Stunff, Kelly S. Doran, Mary E. Choi, Carlos S. Subauste, Natalia Rodriguez-Muela, Nicholas J. Talbot, Marta Palmieri, Sonia Hernández-Tiedra, Ligia C. Gomes, Irving M. Shapiro, Makoto Ubukata, Mario P. Tschan, Baris Bingol, Benjamin Loos, Terry Kwok, Luca M. Neri, Sreejayan Nair, Michele Wolfe Bianchi, Ralf Erdmann, Alexander Greenhough, Neeraj Vij, Jeong Hun Kim, Satoaki Matoba, Bo Liu, George R. Beck, Michael Moore, Vrajesh V. Parekh, Kyle A. Bauckman, Li-Lin Du, Mikihiro Fujiya, Yan G. 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Lee, Maria Xilouri, Qi Chen, Claudia Spies, Pengfei Ge, Natascia Ventura, Luca Galluzzi, Yau Hung Chen, Jing Pu Zhang, Diego Albani, Dingzhong Tang, Nikolai Engedal, Stefania Meschini, Maria Lyngaas Torgersen, Shibu M. Poulose, Jean-Paul Decuypere, Ziheng Xu, Jocelyn Laporte, Thierry Arnould, Albert Haas, Ida J. van der Klei, Agustín Hernández, Dong Wook Shin, Per E. Stromhaug, Valentín Ceña, Ugo Pagnini, Karolina Pakos-Zebrucka, Blagovesta Popova, Lisa M Lindqvist, Sangita C. Sinha, Yuguang Shi, Zvonimir Marelja, Robin Candau, Xin Wang, Evelina Gatti, Olatz Pampliega, Michael P. Lisanti, Elena Tamagno, Mei Lan Tan, Gary Warnes, Zdena Palková, Shigeomi Shimizu, Ingo Schmitz, Tino Kurz, Soledad Matus, Gopal Chakrabarti, Joseph J.Y. Sung, Beáta G. Vértessy, Giuliana Cassinelli, Giovanni Benard, Yin Chen, Emma Colucci-Guyon, Craig Blackstone, Lizhi Cao, Sebastian Schuck, Qingqiu Gong, Theocharis Panaretakis, Jayoung Choi, Sven R. 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Heinzen, Xiangmei Chen, Nihal Altan-Bonnet, Sung Sik Lee, Hai Jie Wang, Catherine Dargemont, Jie Du, Sofie Claerhout, Edmond Chan, Yi Sun, Xiangbo Wan, Paul Lingor, Shilpa Buch, Gerald M. McInerney, Zhenlong Wu, Guo Chang Zhang, Iain A. McNeish, Suresh Awale, Mark P. Mattson, Srinivasa Subramaniam, Wuhan Xiao, Katsuhiko Mikoshiba, Giancarlo Parenti, Bruno Miguel Neves, Benjamin Dehay, Fatima Teixeira-Clerc, Patricia Huebbe, Calvin K. Yip, Ryan J. Schulze, Pallabi Sarkar, Vladimir I. Titorenko, Johanna Laukkarinen, Martin E. Gleave, Veronika Stoka, Pascal Genschik, Karen Brown, Zhaoliang Su, Walter Malorni, Arlette Darfeuille-Michaud, Vincent C. O. Njar, Jeffrey E. Pessin, Thomas Wileman, Alexander J. Whitworth, Stefano Santaguida, Gustavo A. Nader, Gláucia Maria Machado-Santelli, Marie-Josée Hébert, Skye C. McIver, Scott A. Soleimanpour, Jia-Hong Lu, Fei Liu, Yu Wang, Elisa Motori, Chad A. 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Kumar, Deok Ryong Kim, Jianjie Ma, Sang Won Suh, Guido Kroemer, Klára Megyeri, Michael N. Sack, Heinrich Taegtmeyer, Gilles Pagès, Gabriella Marfe, Gregg L. Semenza, Karine G. Le Roch, Marisa Brini, Marina Bouché, Oliver Kepp, Vinay V. Eapen, J. David Beckham, Stephan T. Stern, Xudong Zhang, Marcello Pinti, Xiangnan Zhang, Jae Keun Lee, Ana Coto-Montes, Assaf Rudich, Laura D. Attardi, Debabrata Ghosh, Philip Rosenstiel, Sébastien Besteiro, Maria Rosa Sarrias, R. Andres Floto, Xiao Ming Yin, Nicholas W. Lukacs, Hermann Pavenstädt, Matias Simons, Hitoshi Nakatogawa, Sandro Alves, Krisztina Takács-Vellai, Masato Koike, Debasish Sinha, Shoji Notomi, Faraj Terro, Maria Carmela Roccheri, Santiago Ambrosio, K. Ulrich Bayer, Yumin Li, Terje Johansen, Christian Kuhn, Yee Shin Lin, David C. Rubinsztein, Ziwei Qu, Ronit Shiri-Sverdlov, Emmanuel T. Akporiaye, Galila Agam, Hui Ling Chiang, Seung-Jae Lee, Yu Xue, Francesca Giampieri, Markus Damme, Tassula Proikas-Cezanne, Tianwei Lin, Marc Kantorow, Guang-Chao Chen, Qiangrong Liang, Claudia Manzoni, Joan S. Steffan, Emilio Boada-Romero, Damien Freyssenet, Sepp D. Kohlwein, Maria D. Barrachina, Yulin Liao, Jiankang Chen, Erika Isono, Hugo Seca, Mei Wang, Taras Y. Nazarko, Yannick Bailly, Nadya V. Koshkina, Tapas K. Maiti, Bärbel Rohrer, Karin Nowikovsky, James H. Hurley, Gerald W. Dorn, Nils C. Gassen, Kazuhiro Nagata, Eiki Kominami, A. Ivana Scovassi, Ana Maria Cuervo, Adi Kimchi, Minghua Yang, Sylviane Muller, Life Sciences Institute and Department of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan [Ann Arbor], University of Michigan System-University of Michigan System, Defense in Plant-Pathogen Interactions [Nagoya, Japan], Nagoya University-Graduate School of Bioagricultural Sciences [Nagoya, Japan], Facultad de Quimica [Santiago], Pontificia Universidad Católica de Chile (UC), Institute of Cancer Sciences [Glasgow, UK] (CR-UK Beatson Institute), University of Glasgow, Cell Death Research & Therapy (CDRT) Lab, Université Catholique de Louvain, Harvard University Statistics Department, Harvard University [Cambridge], Centre épigénétique et destin cellulaire (EDC (UMR_7216)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Conway Institute of Biomolecular and Biomedical Research and School of Chemical and Bioprocess Engineering, University College Dublin [Dublin] (UCD), Immunobiologie des Cellules dendritiques, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Biochemistry and Molecular Biology, Thomas Jefferson University-Sidney Kimmel Cancer Center, Jefferson (Philadelphia University + Thomas Jefferson University)-Jefferson (Philadelphia University + Thomas Jefferson University), Centro de Estudios Farmacológicos y Botánicos [Buenos Aires] (CEFYBO), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Facultad de Medicina [Buenos Aires], Universidad de Buenos Aires [Buenos Aires] (UBA)-Universidad de Buenos Aires [Buenos Aires] (UBA), Thérapie génique, Génomique et Epigénomique (U 1169), Université Paris-Saclay-Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Sud - Paris 11 (UP11), Department of Experimental Medicine and Public Health, University of Camerino, MRC Toxicology Unit, University of Leicester, Génomique Fonctionnelle des Tumeurs Solides (U1162), Université Paris 13 (UP13)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Departamento de Bioquímica y Biología Molecular y Celular, University of Zaragoza - Universidad de Zaragoza [Zaragoza], Department of Pharmaco-Biology, Università della Calabria [Arcavacata di Rende] (Unical), Department of Molecular Genetics [Rehovot, Israël], Weizmann Institute of Science, Fondation Universitaire Notre Dame de la Paix (FUNDP), Facultés Universitaires Notre-Dame de la Paix, Département Advanced Research And Techniques For Multidimensional Imaging Systems (ARTEMIS), Institut Mines-Télécom [Paris] (IMT)-Télécom SudParis (TSP), USC Neuromuscular Center, Department of Neurology, University of Southern California (USC), Centre méditérannéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Giannina Gaslini Institute, Department of Molecular Pharmacology, Albert Einstein College of Medicine, Department of Cancer Biology, University of Massachusetts Medical School [Worcester] (UMASS), University of Massachusetts System (UMASS)-University of Massachusetts System (UMASS), Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Inner Mongolia Agricultural University (IMAU), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) (FEMTO-ST), Université de Franche-Comté (UFC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Technologie de Belfort-Montbeliard (UTBM), Indian Institute of Science [Bangalore] (IISc Bangalore), Politecnico di Milano [Milan] (POLIMI), Département des Sciences Biologiques [Montréal], Université du Québec à Montréal (UQAM), Laboratory of Molecular Biology, Scientific Institute E. Medea, Université Catholique de Louvain (UCL), Univ Ancona, Politecn Marche, University of Toronto, Munich Cluster for systems neurology [Munich] (SyNergy), Technische Universität München [München] (TUM)-Ludwig-Maximilians-Universität München (LMU), Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA), Department of Clinical and Molecular Medicine, Università degli Studi di Roma 'La Sapienza' [Rome]-Réseau International des Instituts Pasteur (RIIP)-Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP), Physiopathologie du système nerveux central - Institut François Magendie, Université Bordeaux Segalen - Bordeaux 2-IFR8-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Hémato-Cancérologie Expérimentale, CRP-Santé, Dpt of Neuroscience and Brain Technologies [Genova], NeuroEngineering & bio-arTificial Synergic SystemS Laboratory [Genova] (NetS3 Lab), Istituto Italiano di Tecnologia (IIT)-Istituto Italiano di Tecnologia (IIT), Center for Infection and Immunity Amsterdam (CINIMA), Laboratoire de biogenèse membranaire (LBM), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Centre de résonance magnétique biologique et médicale (CRMBM), Aix Marseille Université (AMU)-Assistance Publique - Hôpitaux de Marseille (APHM)-Centre National de la Recherche Scientifique (CNRS), Régulation de l'expression génétique (REG), Département de Biologie - ENS Paris, École normale supérieure - Paris (ENS Paris)-École normale supérieure - Paris (ENS Paris)-Centre National de la Recherche Scientifique (CNRS), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Department of Microbiology and Immunology, Stanford University School of Medicine [CA, USA], Institut de Myologie, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Association française contre les myopathies (AFM-Téléthon)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Department of Dermatology, Brigham and Women's Hospital [Boston], San Raffaele Scientific Institute, Milan, Italy, Laboratory of Molecular Neuroembryology, University of Rome 'Tor Vergeta'-Clinical and Behavioral Neurology - Neuroscienze e riabilitazione, IRCCS Fondazione Santa Lucia [Roma]-Dulbecco Telethon Institute, Department of Pharmacology, Universidade de Santiago de Compostela, Glycobiologie et signalisation cellulaire, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Complexo Hospitalario Universitario A Coruña, Mécanismes moléculaires de l'angiogénèse, Université Bordeaux Segalen - Bordeaux 2-Institut National de la Santé et de la Recherche Médicale (INSERM), University of Florida [Gainesville], Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer (JPArc - U1172 Inserm), Université Lille Nord de France (COMUE)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université Lille 2 - Faculté de Médecine, Centro de Investigaciones Biológicas (CSIC), Consejo Superior de Investigaciones Científicas [Spain] (CSIC), Interactions hôte-greffon-tumeur, ingénierie cellulaire et génique - UFC (UMR INSERM 1098) (HOTE GREFFON), Université de Franche-Comté (UFC)-Etablissement français du sang [Bourgogne-France-Comté] (EFS [Bourgogne-France-Comté])-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Infection bactérienne, inflammation, et carcinogenèse digestive, Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Institut National de la Recherche Agronomique (INRA)-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), Universita degli Studi di Padova, University of British Columbia (UBC), University of Edinburgh, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Australian Regenerative Medicine Institute, Monash University, Clayton, 3800, VIC, Australia, Faculty of Engineering and Natural Sciences, Sabanci University [Istanbul], Department of Biological Sciences [Stanford], Stanford University [Stanford], Université de Montréal (UdeM), Department of Human Genetics, Department of Psychiatry, University of Michigan System-University of Michigan System-Molecular and Behavioral Neuroscience Institute, Centre for Computational and Systems Biology (COSBI), Department of Computer Science [Tsukuba], Graduate School of Systems and Information Engineering [Tsukuba], University of Tsukuba-University of Tsukuba, Institut de biochimie et génétique cellulaires (IBGC), University of Western Ontario (UWO), Genetics, Dynamique Musculaire et Métabolisme (DMEM), Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM), Department of Biochemistry and Biophysics, University of Naples Federico II, Lund University [Lund], Institute of Molecular Biosciences, Karl-Franzens University Graz, (IMB), Karl-Franzens-Universität Graz, Polytechnic University of Marche, 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), Cell Biology, Physiology and Immunology, Research Unit on BioActive Molecules, Departamento de Química Orgánica Biológica, Instituto de Investigaciones Quimicas y Ambientales de Barcelona, Department of Experimental Oncology and Molecular Medicine, Fondazione IRCCS Istituto Nazionale dei Tumori, Physiopathologie et thérapie du muscle strié, Université Pierre et Marie Curie - Paris 6 (UPMC)-IFR14-Institut National de la Santé et de la Recherche Médicale (INSERM), The Buck Institute for Age Research, University of Pisa - Università di Pisa, Laboratorio di Genetica Molecolare, Istituto Gaslini, Universidad de Castilla-La Mancha (UCLM), Laboratoire de Biologie Moléculaire et Cellulaire du Cancer, Hôpital Kirchberg, University of Crete [Heraklion] (UOC), Division of Molecular and Cellular Pathology [Birmingham], Department of Medical Research, Taichung Veterans General Hospital, Modélisation et Simulation Numérique en Mécanique et Génie des Procédés (MSNMGP), Université de la Méditerranée - Aix-Marseille 2-Université Paul Cézanne - Aix-Marseille 3-Université de Provence - Aix-Marseille 1-Centre National de la Recherche Scientifique (CNRS), University of Queensland [Brisbane], Dept of Mathematics, Purdue University, Purdue University [West Lafayette], Virologie et Pathologie Humaine (VirPath), 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), Laboratoire de chimie de coordination (LCC), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Zhejiang University, Équipe Micro et nanosystèmes HyperFréquences Fluidiques (LAAS-MH2F), Laboratoire d'analyse et d'architecture des systèmes (LAAS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse 1 Capitole (UT1)-Université Toulouse - Jean Jaurès (UT2J)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse 1 Capitole (UT1)-Université Toulouse - Jean Jaurès (UT2J), King Abdullah University of Science and Technology (KAUST), Southern University of Science and Technology of China (SUSTech), OASE, National University of Tainan, Taiwan (OASE), National Taiwan University [Taiwan] (NTU), Weifang Bureau of Land Resources [Weifang], Department of cardiology [Guy's and St. Thomas ' hospitals] [London], Guy's and St Thomas' Hospital [London]-Guy's Hospital [London], University of Pennsylvania [Philadelphia], CRLCC Eugène Marquis (CRLCC), Emory University School of Medicine, Emory University [Atlanta, GA], Korea University, Cytokines et Immunologie des Tumeurs Humaines (U753), Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Pharmacology [Tartu, Estonie], Institute of Biomedicine and Translational Medicine [Tartu, Estonie], University of Tartu-University of Tartu, Max-Planck-Institut für Biophysikalische Chemie - Max Planck Institute for Biophysical Chemistry [Göttingen], Max-Planck-Gesellschaft, University of Pittsburgh (PITT), Pennsylvania Commonwealth System of Higher Education (PCSHE), University of Cincinnati (UC), Réponses immunes : régulation et développement, Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Experimental Medicine, Oxford University, University of Oxford [Oxford], Division of regenerative Medicine, San Raffaele Scientific Institute, The University of New Mexico [Albuquerque], Université Libre de Bruxelles [Bruxelles] (ULB), Macrophages et Développement de l'Immunité, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health [Baltimore], Johns Hopkins University (JHU)-Johns Hopkins University (JHU), Institut du Cerveau et de la Moëlle Epinière = Brain and Spine Institute (ICM), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [APHP]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Dipartimento di Scienze Biomediche, Università degli Studi di Modena e Reggio Emilia (UNIMORE), Department of Experimental Medicine and Oncology, University of Turin, Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), CNV, University of Valparaiso, Institut Gustave Roussy (IGR), Universidad Autonoma de Madrid (UAM), Cell Signalling & Proteomics Group [Londres, Royayme-Uni], Barts Cancer Institute [Londres, Royayme-Uni], Queen Mary University of London (QMUL)-Queen Mary University of London (QMUL), Department of General, Visceral and Vascular Surgery [Jena], Friedrich-Schiller-Universität Jena, Department of Biomedical Engineering, The University of Texas at Austin, University of Texas at Austin, Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte - Clermont Auvergne (M2iSH), Institut National de la Recherche Agronomique (INRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Clermont Auvergne (UCA)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne), Fondazione Santa Lucia (IRCCS), Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Jacques Monod (IJM (UMR_7592)), Institute of Biological, Environmental and Rural Sciences (IBERS), Aberystwyth University, Department of Biology, Johns Hopkins University (JHU), Neurogenetics Group, Instituto de Investigación en Recursos Cinegéticos (IREC), Laboratório de Ultraestrutura Celular Hertha Meyer (IBCCF), Universidade Federal do Rio de Janeiro [Rio de Janeiro] (UFRJ), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology in Zürich [Zürich] (ETH Zürich), Molecular and Cellular Biology, Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), National University of Ireland [Galway] (NUI Galway), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Freiburg Institute for Advanced Studies-LifeNet, Albert-Ludwigs-Universität Freiburg, Groupe de Recherche en Immunopathologies et maladies infectueuses (GRI), Université de La Réunion (UR)-Centre hospitalier Félix-Guyon [Saint-Denis, La Réunion], Brunel University London [Uxbridge], Unité Propre de Recherche 2357, Institution de Biologie Moléculaire des Plantes, Radiothérapie moléculaire (UMR 1030), Department of Chemistry, University of Kentucky, Universidad de Córdoba [Cordoba], Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], Facultad de Ciencias Químicas y Farmacéuticas, Centro de Estudios Moleculares de la Célula, Biochemistry and Molecular Biology, Goethe-University Frankfurt am Main, Department of Biological and Environmental Sciences and Technologies (DiSTeBA), Università del Salento, Institut Bergonié - Département de médecine, Université Bordeaux Segalen - Bordeaux 2-Centre régional de lutte contre le cancer [CRLCC], Institut National Polytechnique de Lorraine (INPL), Récepteurs nucléaires, maladies cardiovasculaires et diabète (EGID), Université de Lille, Droit et Santé-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Unité de Recherche sur les Maladies Cardiovasculaires, du Métabolisme et de la Nutrition = Institute of cardiometabolism and nutrition (ICAN), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [APHP]-Sorbonne Université (SU), Institut de recherches sur la catalyse et l'environnement de Lyon (IRCELYON), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Laboratoire de signalisation moléculaire et neurodégénerescence, Université Louis Pasteur - Strasbourg I-IFR37-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Européen de Chimie et Biologie (IECB), Centre National de la Recherche Scientifique (CNRS)-Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM), Trafic membranaire et Division cellulaire, Landesbetrieb Hessisches Landeslabor, Hematology-Oncology Division, Perelman School of Medicine, University of Pennsylvania [Philadelphia]-University of Pennsylvania [Philadelphia], University of Pavia, Instituto de Investigaciones Biotecnológicas [San Martín] (IIB-INTECH), Universidad Nacional de San Martin (UNSAM)-Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET), University of Helsinki, School of Physics and Astronomy [Exeter], University of Exeter, Department of Biomedicinal Chemistry (CSIC), Institut de Química Avançada de Catalunya, Laboratory of Vascular Pathology (IDI-IRCCS), Istituto Dermopatico dell'Immacolata, Peking University [Beijing], MRC Centre for Developmental Neurobiology, University of Brescia, Immunobiologie fondamentale et clinique, Université de Lyon-Université de Lyon-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), CIC régional épidémiologie clinique/essais cliniques - Ile de la Réunion (CIC-EC), University of Rome 'Tor Vergeta', Universidad de Oviedo [Oviedo], Laboratoire des signaux et systèmes (L2S), Université Paris-Sud - Paris 11 (UP11)-CentraleSupélec-Centre National de la Recherche Scientifique (CNRS), Dulbecco Telethon Institute/Department of Biology, Istituto Nazionale di Malattie Infettive 'Lazzaro Spallanzani' (INMI), Rockefeller University [New York], The Babraham Institute, Kansas State University, McGill University, Service d'Anatomie et Cytologie Pathologique [Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Laboratoire Interuniversitaire de Biologie de la Motricité (LIBM ), Université de Lyon-Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Department of Medicine [New York], Icahn School of Medicine at Mount Sinai [New York] (MSSM), ATOS Origin, Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences-Tohoku University [Sendai], Goethe-University, Goethe-Universität Frankfurt am Main, Institute of physiological chemistry, Hannover Medical School [Hannover] (MHH), Department of Physiology, Department of Plant and Environmental Sciences, Apoptose, cancer et immunité (U848), Laboratoire de Biologie du Développement (LBD), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-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), Departments of Neurology and Psychiatry, Alzheimer's Disease Research Center, Institute of Experimental Immunology - IEI [Zürich, Switzerland], Université de Zurich [Switzerland], Digital Enterprise Research Institute (DERI-NUIG), Spanish National Research Council (CSIC), Cell Death Research and Therapy Unit [Leuven, Belgium] ( Department of Cellular and Molecular Medicine), Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Signaling in Oncogenesis, Angiogenesis and Permeability - SOAP (CRCINA - Département ONCO - Equipe 15), Centre de recherche de Cancérologie et d'Immunologie / Nantes - Angers (CRCINA), Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN), Department of Medicine [San Francisco], University of California [San Francisco] (UCSF), University of California-University of California, Fondazione Santa Lucia [IRCCS], Clinical and Behavioral Neurology [IRCCS Santa Lucia], Institut de biologie moléculaire des plantes (IBMP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), Institut de Recherche pour le Développement (IRD)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR48, INSB-INSB-Centre National de la Recherche Scientifique (CNRS), Department of Anatomy, Histology, Forensic Medicine and Orthopedic, N.A., Division of Pharmacology and Chemotherapy, Department of Internal Medicine, Pathogénie Microbienne Moléculaire, University of Chile [Santiago], Université de Montpellier (UM), Faculdade de Ciências Farmacêuticas de Ribeirão Preto [São Paulo], Universidade de São Paulo (USP), Centro de Investigación Biomédica en Red en Enfermedades Neurodegenerativas (CIBERNED), Institut de recherche en cancérologie de Montpellier (IRCM - U896 Inserm - UM1), CRLCC Val d'Aurelle - Paul Lamarque-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1), Catalan Institute of Oncology, Department of Cell Biology, National Institute for Basic Biology [Okazaki], Instituto de Bioquímica Vegetal y Fotosíntesis (IBVF), Universidad de Sevilla-Centro de Investigaciones Científicas Isla de la Cartuja, The Adams Super Center for Brain Studies, Tel Aviv University [Tel Aviv], Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS), Department of Pharmacology and biochemistry, Virginia Commonwealth University (VCU), Department of Immunology, St Jude Children's Research Hospital, Department of Biology and Biotechnologies 'Charles Darwin', Lettres, Idées, Savoir (LIS), Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Institute of Biological Chemistry and Nutrition, University of Hohenheim, China Seismological Bureau, Massachusetts Institute of Technology (MIT), Rosenstiel Basic Medical Sciences Research Center [Waltham], Brandeis University, Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA), Meakins-Christie Laboratories, Sanford Burnham Medical Research Institute, La Jolla, National Institute of Advanced Industrial Science and Technology (AIST), ORIENT ET MÉDITERRANÉE : Textes, Archéologie, Histoire (OM), Université Panthéon-Sorbonne (UP1)-École pratique des hautes études (EPHE)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), David Geffen School of Medicine [Los Angeles], University of California [Los Angeles] (UCLA), Ludwig Institute for Cancer Research, Royal Melbourne Hospital, Centro de Investigacion y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV), Biochemistry and Molecular Biology I, Department of Immunology and Infectious Diseases, Harvard School of Public Health, aDepartment of Plant Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences (SLU), Philipps University of Marburg, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Renal Division, University Medical Center Freiburg, Freiburg, Germany, Rural Health Academic Centre, University of Melbourne-Rural Clinical School, Department of Pathology, University of Veterinary and Animal Sciences, Dipartimento di Scienze della Vita [Modena, Italy], Stress Cellulaire, Université de la Méditerranée - Aix-Marseille 2-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Pathology, Anatomy & Cell Biology [Philadelphia, Pennsylvania, USA], Thomas Jefferson University, Department of Molecular Neuroscience, Departamento de Bioquimica Clinica, Facultad de Ciencias Quimicas, Centro de Investigación en Bioquímica Clínica e Inmunología (CONICET), Universidad Nacional de Córdoba, Córdoba, Argentina, Neuroinflammation Unit, Biotech Research and Innovation Centre-University of Copenhagen = Københavns Universitet (KU), Mathematics and Computing in Automatic Control and Optimization for the User (MIAOU), Inria Sophia Antipolis - Méditerranée (CRISAM), Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria), Centre de Recherche des Cordeliers (CRC), Université Paris Diderot - Paris 7 (UPD7)-École pratique des hautes études (EPHE)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Danish Cancer Society, Institute of Cancer Biology, UCL-Institute of Child Health (ICH), Institute of Child Health-Great Ormond Street Hospital for Children [London] (GOSH), Division of Renal Diseases and Hypertension, University of Colorado [Boulder], Institut de biologie et chimie des protéines [Lyon] (IBCP), Joslin Diabetes Center, Universität Ulm - Ulm University [Ulm, Allemagne], Qingdao Institute of Marine Geology, China Geological Survey, Qingdao 266071, China, Université Paris Diderot - Paris 7 (UPD7), Institute of Software, Chinese Academy of Sciences [Beijing] (CAS), Metabolic Engineering Group, Departamento de Microbiologia y Genetica, Edificio Departamental, Campus Miguel de Unamuno, Universidad de Salamanca, University of Minnesota [Twin Cities], University of Minnesota System, Department of Cellular and Molecular Physiology, Yale University School of Medicine, The Arctic University of Norway, Department of Biological Sciences, The Open University [Milton Keynes] (OU), Summit Analytical, CALRG, Institute of Educational Technology, Institute for Neurologic Disabilities Research, Faculty of Health Sciences-University of Pretoria [South Africa], Department of Paediatric Neurology, Guy's and St Thomas' Hospital [London]-Evelina Children's Hospital, Physiologie des Adaptations Nutritionnelles [UMR_A1280] (PhAN), Institut National de la Recherche Agronomique (INRA)-Université de Nantes (UN), Dana-Farber Cancer Institute and the Department of Cell Biology, Harward Medical School, Translational Health Science and Technology Institute [Faridabad] (THSTI), Department of Biomedical Sciences of Cells and Systems, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands, School of Reliability and Systems Engineering [Beijing], Beihang University, Oxford Centre for Integrative Systems Biology, Center for Membrane and Cell Physiology [Charlottesville, VA, USA] (School of Medicine), University of Virginia [Charlottesville], Apoptose, cancer et immunité (Equipe labellisée Ligue contre le cancer - CRC - Inserm U1138), Institut Gustave Roussy (IGR)-Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), St James's University Hospital, Leeds Teaching Hospitals NHS Trust, Karlsruher Institut für Technologie (KIT), Faculty of Pharmaceutical Sciences, Hokkaido University, École normale supérieure - Paris (ENS Paris), School of Electrical Engineering [Seoul] (Korea University), Department of Mathematics and Statistics [Guelph], University of Guelph, Department of Molecular Genetics, Department of Genetics [Stanford, CA, États-Unis], Institute of Immunology, University Hospital Schleswig-Holstein, Arizona Respiratory Center, Okazaki Institute for Integrative Bioscience, ToxAlim (ToxAlim), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA), Newcastle University [Newcastle], JRC Institute for Transuranium Elements [Karlsruhe] (ITU ), European Commission - Joint Research Centre [Karlsruhe] (JRC), Department of Neuroscience, University of Texas Southwestern Medical Center [Dallas], Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Laboratory of Functional Neurogenomics [Tuebingen, Germany], University of Tuebingen-Center of Neurology and Hertie-Institute for Clinical Brain Research [Tuebingen, Germany], Indian Institute of Technology Bombay (IIT Bombay), European Organization for Nuclear Research (CERN), Harvard Medical School [Boston] (HMS), Indian School of Mines, Department of Computer Science [UIUC] (UIUC), University of Illinois at Urbana-Champaign [Urbana], University of Illinois System-University of Illinois System, Centre for Cancer Biology, Hanson Institute, Adelaide, University of California [San Diego] (UC San Diego), University of California, Centre d’Infection et d’Immunité de Lille (CIIL) - U1019 - 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 National de la Recherche Scientifique (CNRS), Department of Biochemistry, University of Bristol, Organisation Nucléaire et Oncogenèse, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), FONDAP Center CEMC Estudios Moleculares de la Célula, Unité de Biologie Fonctionnelle et Adaptative (BFA (UMR_8251 / U1133)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), Centre d'infectiologie Necker-Pasteur [CHU Necker], CHU Necker - Enfants Malades [AP-HP], Chungnam National Univesity School of Medicine, Taejon, Korea, Chungnam National Univesity School of Medicine, Micro & Nanobiotechnologies, Institut des Sciences Analytiques (ISA), Centre National de la Recherche Scientifique (CNRS)-Université de Lyon-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-École normale supérieure - Lyon (ENS Lyon)-Centre National de la Recherche Scientifique (CNRS)-Université de Lyon-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-École normale supérieure - Lyon (ENS Lyon), Centre de Recherche en Cancérologie de Lyon (CRCL), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de génétique moléculaire (CGM), Université Paris-Sud - Paris 11 (UP11)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Center for Applied Mathematics, Tsinghua University [Beijing], University of Connecticut School of Medicine, University of Connecticut (UCONN), Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes (LBMCE), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Microenvironnement et Physiopathologie de la Differenciation, Division of Nephrology and Hypertension, Mayo Clinic, Beatson Institute for Cancer Research, Beatson institute for cancer research, Howard Hughes Medical Institute, Howard Hugues Medical Institute, 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), Institute of Computing Technology [Beijing] (ICT), Chinese Academy of Sciences [Changchun Branch] (CAS), School of Electronics and Computer Science (ECS), University of Southampton, Third Hospital, Department of Anesthesiology, Cognitive Interaction Technology [Bielefeld] (CITEC), Universität Bielefeld = Bielefeld University, Procédés, Matériaux et Energie Solaire (PROMES), Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS), Faculty of Pharmacy- University of Coimbra, National Neuroscience Institute, Key Laboratory of Molecular Virology & Immunology (LMVI), Institut Pasteur de Shanghai, Académie des Sciences de Chine - Chinese Academy of Sciences (IPS-CAS), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Coll Life Sci, Beijing Normal University, Delft University of Technology (TU Delft), Christian-Albrechts-Universität zu Kiel (CAU), Department of Molecular Pathology and Microbiology, Center for Applied Proteomics and Molecular Medicine-George Mason University [Fairfax], Sidney Kimmel Cancer Center, Jefferson (Philadelphia University + Thomas Jefferson University), Institut des Sciences Chimiques de Rennes (ISCR), Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Rennes-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES), Department of Chemistry, University of Pittsburgh, University of Pittsburg, Tianjin University of Science and Technology (TUST), Hunan University of Science and Technology [Xiangtan], Laboratoire de Génie Civil et Génie Mécanique (LGCGM), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), China Agricultural University (CAU), Acad Disaster Reduct and Emergency Management, Minist Civil Affairs, Minist Educ, Beijing, Peoples R China, affiliation inconnue, Département Technologie des Polymères et Composites & Ingénierie Mécanique (TPCIM), École des Mines de Douai (Mines Douai EMD), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Ministère de l'Economie, des Finances et de l'Industrie, MOE Key Laboratory of Bioinformatics, Centre for Plant Biology, School of Life Sciences, Laboratoire d'Informatique Gaspard-Monge (ligm), Université Paris-Est Marne-la-Vallée (UPEM)-École des Ponts ParisTech (ENPC)-ESIEE Paris-Fédération de Recherche Bézout-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biochimie Moléculaire et Cellulaire (LBMC), Université de Bourgogne (UB), Center for International Blood and Marrow Transplant Research (CIBMTR), Emory University [Atlanta, GA]-Medical College of Wisconsin, Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Illman Cancer Center, Pennsylvania Commonwealth System of Higher Education (PCSHE)-Pennsylvania Commonwealth System of Higher Education (PCSHE), Ingénierie des Matériaux Polymères (IMP), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Jean Monnet [Saint-Étienne] (UJM)-Centre National de la Recherche Scientifique (CNRS), Université Côte d'Azur (UCA), Department of Medical Microbiology and Immunology, University of California [Davis] (UC Davis), School of Health Sciences, University of Minho [Braga], Équipe Calcul Distribué et Asynchronisme (LAAS-CDA), University of California [Riverside] (UCR), Ohio State University [Columbus] (OSU), Laboratory of Systems Biology, Van Andel Institute [Grand Rapids], Division of Genetics and Cell Biology, National Center for Gender-Specific Medicine, Istituto Superiore di Sanità, Oregon Health and Science University [Portland] (OHSU), Dendrite Differenciation Group [DZNE - Bonn], German Research Center for Neurodegenerative Diseases - Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Equipe 12, Génétique moléculaire, signalisation et cancer (GMSC), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre de Recherche en Cancérologie de Lyon (CRCL), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), University Medical Center [Utrecht], Institut d'Investigacions Biomèdiques August Pi I Sunyer [Barcelona, Spain] (Hospital Clinic ), Department of Genetics, Trinity College Dublin, Fisiopatologia de los procesos inflamatorios, Vall d'Hebron Research Institute, Institució Catalana de Recerca i Estudis Avançats (ICREA), Department of Human Genetics, Nagasaki University, Transduction du signal et oncogénèse, Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Curie, Center for Experimental and Molecular Medicine, Academic Medical Center - Academisch Medisch Centrum [Amsterdam] (AMC), University of Amsterdam [Amsterdam] (UvA)-University of Amsterdam [Amsterdam] (UvA), Department of medical Biochemistry, University of Amsterdam [Amsterdam] (UvA), IDI-IRCCS Biochemistry Laboratory, Università degli Studi di Roma Tor Vergata [Roma], Program Against Cancer Therapeutic Resistance/Metabolism & Cancer Group [Catalonia, Spain] (ProCURE), Catalan Institute of Oncology-Girona (ICO-Girona), Instituto de Tecnologia Química e Biológica António Xavier (ITQB), Universidade Nova de Lisboa (NOVA), Medical Genetics Unit, IRCCS Casa Sollievo della Sofferenza Hospital, CNR, Consiglio Nazionale delle Ricerche (CNR), Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Laboratory for Developmental Neurobiology, RIKEN Brain Science Institute, The Hospital for sick children [Toronto] (SickKids), Universidad de Sevilla, Immunité muqueuse et vaccination, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR50-Université Nice Sophia Antipolis (... - 2019) (UNS), DIMS, University of Trento [Trento], Laboratoire de Biologie Moléculaire de la Cellule (LBMC), Department of Cellular and Molecular Medicine [Madrid, Spain], Laboratory of Cell Death and Cancer Therapy [Madrid, Spain], Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC) -Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth PL1 3HD, UK, Centre d'Immunologie et de Maladies Infectieuses (CIMI), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Dpt. of Cancer & Cell Biology, Interactions Bactéries-Cellules (UIBC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur [Paris]-Institut National de la Recherche Agronomique (INRA), Max planck Institute for Biology of Ageing [Cologne], Euromov (EuroMov), Wellcome Trust Centre for Molecular Parasitology [Glasgow, UK], University of Glasgow- Institute of Infection, Immunity and Inflammation [Glasgow, UK], Immunologie et chimie thérapeutiques (ICT), Cancéropôle du Grand Est-Centre National de la Recherche Scientifique (CNRS), UMR 1599, Centre National de la Recherche Scientifique (CNRS), EA 4100, Histoire culturelle et sociale de l'art (HiCSA), Université Panthéon-Sorbonne (UP1)-Université Panthéon-Sorbonne (UP1), Centre for Astrophysics and Supercomputing (Centre for Astrophysics and Supercomputing), Swinburne University of Technology [Melbourne], Department of Cellular and Physiological Sciences [Vancouver, BC, Canada] (Life Sciences Institute), University of British Columbia (UBC)-Life Sciences Institute [Vancouver, BC, Canada], School of Pharmacy, Department of Experimental Medicine, Dept. Neurosciences, Department of Internal Medicine, Radboud University Medical Center [Nijmegen], Institute of Medical Genetics and Applied Genomics, Radiation Physics, School of Life Science, Department of Basic Biology, The Graduate University for Advanced Studies, CIBER de Enfermedades Neurodegenerativas (CIBERNED), Doshisha University, National Cancer Research Center [Tokyo, Japan], University of Washington [Seattle], Department of Experimental Neurodegeneration [Göttingen, Germany], University Medical Center Göttingen (UMG), Cibles moléculaires et thérapeutiques de la maladie d'Alzheimer (CIMoTHeMA), Université de Poitiers, Laboratoire de Probabilités et Modèles Aléatoires (LPMA), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), BioCeV-Institute of Microbiology, Médecine Personnalisée, Pharmacogénomique, Optimisation Thérapeutique (MEPPOT - U1147), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Istituto di chimica biologica, Università degli Studi di Verona, Département Image et Traitement Information (ITI), Institut Mines-Télécom [Paris] (IMT)-Université européenne de Bretagne - European University of Brittany (UEB)-Télécom Bretagne, Department of Cell Biology and Biophysics, Università degli Studi di Firenze [Firenze], Cell Immunity in Cancer, Inflammation and infection Group [Zaragoza, Spain] (Biomedical Research Center), Nanoscience Institute of Aragon - INA [Zaragoza, Spain]-Fundación Agencia Aragonesa para la Investigación y el Desarrollo - ARAID [Zaragoza, Spain]-University of Zaragoza - Universidad de Zaragoza [Zaragoza], Department of Pediatrics, Università degli studi di Napoli Federico II, Transfert de Genes a Visee Therapeutique Dans les Cellules Souches, Developpement Normal et Pathologique du Système Immunitaire, Signalisation et physiopathologie des cellules épithéliales, Facultad de Medicina, Universidad de Santiago de Chile [Santiago] (USACH), Departamento de Farmacobiología, Cinvestav-Sede Sur, Centre de recherche Croissance et signalisation (UMR_S 845), College of Life Sciences, Central China Normal University, Institute of Molecular Biotechnology, Austrian Academy of Sciences (OeAW), Laboratory of Cardiac Surgical Research, Monash University [Clayton], Universidade do Minho, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Neurodegenerative Diseases Research Group (CIBERNED), Vall d'Hebron Research Institute-Center for Networked Biomedical Research on Neurodegenerative Diseases, Barcelona, Department of medicine, Syracuse, NY, USA, State University of New York (SUNY), National University of Singapore (NUS)-Yong Loo Lin School of Medicine-Graduate School for Integrative Sciences and Engineering, McGill University Health Center [Montreal] (MUHC), National Institute for Infectious Diseases, Transporteurs en Imagerie et Radiothérapie en Oncologie (TIRO - UMR E4320), Service Hospitalier Frédéric Joliot (SHFJ), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-UMR E4320 (TIRO-MATOs), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Nice Sophia Antipolis (... - 2019) (UNS), Institut Gustave Roussy (IGR)-Centre de Recherche des Cordeliers (CRC), Université Paris Diderot - Paris 7 (UPD7)-École pratique des hautes études (EPHE)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Diderot - Paris 7 (UPD7)-École pratique des hautes études (EPHE)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Biomedical Sciences, Department of Genetics of Eukaryotic Microorganisms, Georg-August-University [Göttingen]-Institute of Microbiology and Genetics, Sterol metabolism and therapeutic innovations in oncology, Institut Claudius Regaud, CRLCC Institut Claudius Regaud-CRLCC Institut Claudius Regaud-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Department of Molecular, Cellular and Developmental Biology, Señalización Celular 4, Institute of integrative biology (Liverpool), University of Liverpool, Department of Human Biology, University of Cape Town, National Institute of Diabetes and Digestive and Kidney Diseases [Bethesda], Department of Molecular Biology, Eberhard Karls Universität Tübingen, Technical University of Munich (TUM), Biophysics and Bioinformatics Laboratory, Department of Cell Biology and Morphology, Université de Lausanne (UNIL), Shenyang Institute of Automation, the Chinese Academy of Sciences (SIA), Key Laboratory of Thermo-Fluid Science and Engineering of Ministry of Education, Xi'an Jiaotong University (Xjtu), Dipartimento di Biologia, Mechanics laboratory , UniversityAmar Telidji, 3000 Laghouat, Algéria., Mechanics laboratory , University Amar Telidji, sans affiliation, Service d'hépatologie [Hôpital Beaujon], Assistance publique - Hôpitaux de Paris (AP-HP) (APHP), University of Waterloo, Waterloo, ON, Canada, Institute of Cell Biology and Immunology, University of Stuttgart, Chaperones Research Group, Institute of Biosciences and Technology [Houston, TX, États-Unis] (IBT), Texas A&M Health Science Center [Houston, TX, États-Unis] (TAMHSC), Texas A&M University Health Science Center-Texas A&M University Health Science Center, Aquatic and Crop Resource Development, National Research Council of Canada (NRC), Cibles thérapeutiques, formulation et expertise pré-clinique du médicament (CITHEFOR), Université de Lorraine (UL), Dipartimento di Scienze Cliniche e Molecolari, Università Politecnica delle Marche [Ancona] (UNIVPM), Department of Biochemistry and Molecular Biology [Indianapolis, IN, USA], Indiana University School of Medicine, Indiana University System-Indiana University System, Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, iMed.UL, Faculty of Pharmacy, University of Lisbon, CESAM & Biology Department, Universidade de Aveiro, Celullar and Molecular Medicine, Università degli Studi di Perugia (UNIPG), Institute of Clinical Molecular Biology, Kiel University, Apoptose et Système Immunitaire (ASI), Vieillissement Cellulaire Intégré et Inflammation (VCII), Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Department of Mathematical Sciences [Aalborg], Aalborg University [Denmark] (AAU), Cambridge Institute for Medical Research (CIMR), University of Cambridge [UK] (CAM), Biozentrum, University of Basel (Unibas), Structural and Computational Biology Unit, European Molecular Biology Laboratory [Grenoble] (EMBL), Rutgers New Jersey Medical School (NJMS), Rutgers University System (Rutgers), Université de Perpignan Via Domitia (UPVD), Universidad Pablo de Olavide [Sevilla] (UPO), Department of Neurosciences, Agronomes et Vétérinaires Sans Frontières (AVSF), AVSF, Department of Mathematics [Gakushuin], Gakushuin University, Department of Internal Medicine [Münster, Germany], University of Münster, Neurogenetics laboratory, University Medicine Goettingen, Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Université d'Uruguay, Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération (LBCMCP), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Institute for Conservation & Improvement of Valentian Agrodiversity (COMAV), Universitat Politecnica de Valencia (UPV), ICBM, University of Chile [Santiago]-Faculty of Medicine, Nutrition, Métabolisme, Aquaculture (NuMéA), Institut National de la Recherche Agronomique (INRA)-Université de Pau et des Pays de l'Adour (UPPA), Department of Cell Biology, Baltimore, Johns Hopkins University School of Medicine, Baylor College of Medicine (BCM), Baylor University, University of Minnesota Medical School, Beijing Candid soft Technology Co. Ltd, Nanjing University of Information Science and Technology, Department of Hepatobiliary and Pancreatic Surgery [Maebashi, Japan], Gunma University Graduate Schoolof Medicine [Maebashi, Japan], Department of Molecular Genetics [Maastricht, The Netherlands], Maastricht University [The Netherlands], Institute of Cell Biology and Genetic Engineering, National Academy of Sciences of Ukraine (NASU), Institute of Pharmacology of Natural Products and Clinical Pharmacology, Institute of Pharmacology, University of Bern, Imagine - Institut des maladies génétiques (IMAGINE - U1163), Wilmer Eye Institute, Mayo Clinic and Mayo College of Medicine, Rochester, Institute of Biochemistry and Biophysics, Polska Akademia Nauk (PAN)-Sciences, Department of Electrical and Computer Engineering [Waterloo] (ECE), University of Waterloo [Waterloo], Department of Chemistry and Toxicology, Norwegian Veterinary Institute, Department of Gynecologic Oncology, The University of Texas M.D. Anderson Cancer Center [Houston], University of Minho, Friedrich Miescher Laboratory (FML), Charité - Universitätsmedizin Berlin / Charite - University Medicine Berlin, Department of Biomedical Sciences and Biotechnologies, Brescia University, Department of Physiological Chemistry [Bochum], Ruhr-Universität Bochum [Bochum], University of Oslo (UiO), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Facultés Universitaires Notre Dame de la Paix (FUNDP), 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), École pratique des hautes études (EPHE)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226, Université du Québec à Montréal = University of Québec in Montréal (UQAM), 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 Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-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), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Association française contre les myopathies (AFM-Téléthon)-Sorbonne Université (SU), Université Lille 2 - Faculté de Médecine -Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang [Bourgogne-France-Comté] (EFS [Bourgogne-France-Comté])-Université de Franche-Comté (UFC), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM), 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), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon), Institut de Chimie de Toulouse (ICT-FR 2599), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Université Toulouse 1 Capitole (UT1)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse 1 Capitole (UT1)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Université Fédérale Toulouse Midi-Pyrénées, Université libre de Bruxelles (ULB), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Universidade Federal do Rio de Janeiro (UFRJ), Institut Bergonié [Bordeaux], UNICANCER, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Trafic membranaire et Division cellulaire - Membrane Traffic and Cell Division, Centre National de la Recherche Scientifique (CNRS)-CentraleSupélec-Université Paris-Sud - Paris 11 (UP11), McGill University = Université McGill [Montréal, Canada], Service d'Anatomie et Cytologie Pathologique [CHU Rouen], Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Signaling in Oncogenesis, Angiogenesis and Permeability (CRCINA-ÉQUIPE 15), Centre de Recherche en Cancérologie et Immunologie Nantes-Angers (CRCINA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Centre National de la Recherche Scientifique (CNRS)-Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Centre National de la Recherche Scientifique (CNRS)-Université d'Angers (UA), Universidad de Chile = University of Chile [Santiago] (UCHILE), Centro de Investigacion Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Instituto de Salud Carlos III (ISC), Université Montpellier 1 (UM1)-CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Aix Marseille Université (AMU)-Collège de France (CdF (institution))-Centre National de la Recherche Scientifique (CNRS), Université Panthéon-Sorbonne (UP1)-École pratique des hautes études (EPHE)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Collège de France (CdF (institution)), Université Pierre et Marie Curie - Paris 6 (UPMC)-École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Great Ormond Street Hospital for Children [London] (GOSH)-Institute of Child Health, Hokkaido University [Sapporo, Japan], Université Paris sciences et lettres (PSL), Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université de Lyon-Université de Lyon, Centre d’Infection et d’Immunité de Lille (CIIL) - INSERM U1019 - UMR 9017 (CIIL), 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), Organisation Nucléaire et Oncogenèse - Nuclear Organization and Oncogenesis, Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche en Cancérologie de Lyon (UNICANCER/CRCL), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon], Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU), The Beatson Institute for Cancer Research, Beijing Normal University (BNU), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Fédération de Recherche Bézout-ESIEE Paris-École des Ponts ParisTech (ENPC)-Université Paris-Est Marne-la-Vallée (UPEM), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA), Université de Lyon-Université de Lyon-Centre de Recherche en Cancérologie de Lyon (UNICANCER/CRCL), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre Léon Bérard [Lyon], Vall d’Hebron Research Institute (VHIR), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Universidade Nova de Lisboa = NOVA University of Lisboa (NOVA), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), 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)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Doshisha University [Kyoto], Université européenne de Bretagne - European University of Brittany (UEB)-Télécom Bretagne-Institut Mines-Télécom [Paris] (IMT), Università degli Studi di Firenze = University of Florence [Firenze], University of Zaragoza - Universidad de Zaragoza [Zaragoza]-Nanoscience Institute of Aragon - INA [Zaragoza, Spain]-Fundación Agencia Aragonesa para la Investigación y el Desarrollo - ARAID [Zaragoza, Spain], Central China Normal University [Wuhan, China], Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-UMR E4320 (TIRO-MATOs), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Université Pierre et Marie Curie - Paris 6 (UPMC)-École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut Claudius Regaud, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Institut de biologie structurale [1992-2019] (IBS - UMR 5075 [1992-2019]), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), 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)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Nanjing University of Information Science and Technology (NUIST), Facultad de Medicina [Buenos Aires], Universidad de Buenos Aires [Buenos Aires] (UBA)-Universidad de Buenos Aires [Buenos Aires] (UBA)-Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Clermont Auvergne (UCA)-Institut National de la Recherche Agronomique (INRA), 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, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Universidad Nacional de San Martin (UNSAM), Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-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), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, George Mason University [Fairfax]-Center for Applied Proteomics and Molecular Medicine, Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), 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), Institute of Infection, Immunity and Inflammation [Glasgow, UK]-University of Glasgow, Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-CHU Rouen, Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Gustave Roussy (IGR)-Université Paris-Sud - Paris 11 (UP11), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur [Paris], Centre Léon Bérard [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 Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), 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), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), and Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: 0301 basic medicine, Settore BIO/06, biology, Cell Biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, biology.organism_classification, Cell biology, Interpretation (model theory), 03 medical and health sciences, Arama, 030104 developmental biology, Molecular Biology, Humanities, ComputingMilieux_MISCELLANEOUS
Abstract: Author(s): Klionsky, DJ; Abdelmohsen, K; Abe, A; Abedin, MJ; Abeliovich, H; Arozena, AA; Adachi, H; Adams, CM; Adams, PD; Adeli, K; Adhihetty, PJ; Adler, SG; Agam, G; Agarwal, R; Aghi, MK; Agnello, M; Agostinis, P; Aguilar, PV; Aguirre-Ghiso, J; Airoldi, EM; Ait-Si-Ali, S; Akematsu, T; Akporiaye, ET; Al-Rubeai, M; Albaiceta, GM; Albanese, C; Albani, D; Albert, ML; Aldudo, J; Algul, H; Alirezaei, M; Alloza, I; Almasan, A; Almonte-Beceril, M; Alnemri, ES; Alonso, C; Altan-Bonnet, N; Altieri, DC; Alvarez, S; Alvarez-Erviti, L; Alves, S; Amadoro, G; Amano, A; Amantini, C; Ambrosio, S; Amelio, I; Amer, AO; Amessou, M; Amon, A; An, Z; Anania, FA; Andersen, SU; Andley, UP; Andreadi, CK; Andrieu-Abadie, N; Anel, A; Ann, DK; Anoopkumar-Dukie, S; Antonioli, M; Aoki, H; Apostolova, N; Aquila, S; Aquilano, K; Araki, K; Arama, E; Aranda, A; Araya, J; Arcaro, A; Arias, E; Arimoto, H; Ariosa, AR; Armstrong, JL; Arnould, T; Arsov, I; Asanuma, K; Askanas, V; Asselin, E; Atarashi, R; Atherton, SS; Atkin, JD; Attardi, LD; Auberger, P; Auburger, G; Aurelian, L; Autelli, R
Published: 2016

217. Ionic liquid polymer functionalized carbon nanotubes-doped poly(3,4-ethylenedioxythiophene) for highly-efficient solid-phase microextraction of carbamate pesticides

Author: Liying Wang, Baizhao Zeng, Faqiong Zhao, and Mian Wu
Subjects: Chromatography, Gas, Polymers, Ionic Liquids, Carbon nanotube, engineering.material, 010402 general chemistry, Solid-phase microextraction, 01 natural sciences, Biochemistry, Analytical Chemistry, law.invention, chemistry.chemical_compound, Coating, law, Nafion, Pesticides, Solid Phase Microextraction, Detection limit, Flame Ionization, Chromatography, Nanotubes, Carbon, 010401 analytical chemistry, Organic Chemistry, Extraction (chemistry), General Medicine, Bridged Bicyclo Compounds, Heterocyclic, 0104 chemical sciences, chemistry, Ionic liquid, engineering, Carbamates, Poly(3,4-ethylenedioxythiophene), Food Analysis
Abstract: A poly(3,4-ethylenedioxythiophene)-ionic liquid polymer functionalized multiwalled carbon nanotubes (PEDOT-PIL/MWCNTs) composite solid-phase microextraction (SPME) coating was fabricated by electrodeposition. After being dipped in Nafion solution, a Nafion-modified coating was obtained. The outer layer Nafion played a crucial role in enhancing the durability and stability of the coating, thus it was robust enough for replicated extraction for at least 150 times without decrease of extraction performance. The Nafion-modified coating exhibited much higher sensitivity than commercial coatings for the direct extraction of carbamate pesticides in aqueous solutions, due to its strong hydrophobic effect and π-π affinity based enrichment. When it was used for the determination of carbamate pesticides in combination with gas chromatography-flame ionization detection, good linearity (correlation coefficients higher than 0.9981), low limits of detection (15.2-27.2 ng/L) and satisfactory precision (relative standard deviation
Published: 2016

218. Noncoding RNAs Regulating p53 and c-Myc Signaling

Author: Yide Mei and Mian Wu
Subjects: 0301 basic medicine, Cell signaling, Effector, Gene regulatory network, Biology, Non-coding RNA, Cell biology, law.invention, 03 medical and health sciences, 030104 developmental biology, law, microRNA, Suppressor, Proto-Oncogene Proteins c-myc, Signal transduction
Abstract: p53 is one of the most important tumor suppressors and is known to play critical roles in the process of tumor development. Similarly, as an important proto-oncogenes, c-Myc is activated in over half of human cancers. Both p53 and c-Myc participate in almost every crucial decision of almost every cell. Therefore, it is utmost important to gain a better understanding of how they affect multiple cellular processes. The physiological and pathologic patterns of p53 and c-Myc regulations are modulated by a large number of cis-elements and transfactors (RNAs and proteins). These elements and factors are composed of a complicated network of intracellular and extracellular pathways. How the noncoding RNAs are involved in their regulations has not been comprehensively reviewed. In this chapter, we will list and describe recently published important noncoding RNAs including microRNAs and long noncoding RNAs, which act as effectors and regulators for both p53 and c-Myc regulation. The purpose of this chapter is to provide a recent progress of noncoding RNA in the regulation of p53 and c-Myc on network of cellular signaling and its potential implications in both basic science and clinical application.
Published: 2016

219. Dimensionality Reduction Method of Training Sample Set for SVDD Based on Statistical Information

Author: Bin Chen, Xiao Bin Cheng, Zhao Li Yan, Bao Cheng Gao, and Mian Wu
Subjects: business.industry, Dimensionality reduction, Pattern recognition, Scale (descriptive set theory), Sample (statistics), General Medicine, computer.software_genre, Support vector machine, Set (abstract data type), Kernel (linear algebra), Position (vector), Data mining, Artificial intelligence, business, Time complexity, computer, Mathematics
Abstract: In order to solve problem of high time complexity of support vector data description (SVDD) in training process, a low complexity SVDD algorithm is proposed by introducing statistical information grid (STING).The algorithm applies STING division to sample set space using support vector distribution characteristics and kernel distances between samples and sphere’s centre. Based on position information of sample points, it rejects non-support vectors and obtained simplified sample set. The results show that proposed method can reduce training scale and time without decreasing classification accuracy.
Published: 2012

220. p53-Facilitated miR-199a-3p Regulates Somatic Cell Reprogramming

Author: Yide Mei, Chuanchun Han, Hao Gu, Qun Li, Lei Jin, Mian Wu, Qianqian He, and Jiaxu Wang
Subjects: Induced stem cells, Somatic cell, Cell growth, Induced Pluripotent Stem Cells, Cell Biology, Biology, Cellular Reprogramming, Cell Line, Cell biology, Mice, MicroRNAs, Cell culture, Animals, Humans, Molecular Medicine, Ectopic expression, Tumor Suppressor Protein p53, Induced pluripotent stem cell, Reprogramming, G1 phase, Cells, Cultured, Cell Proliferation, Developmental Biology
Abstract: Somatic cells can be reprogrammed to induced pluripotent stem cells (iPSCs) by ectopic expression of defined transcriptional factors. The efficiency of this process, however, is extremely low. Although inactivation of p53 has been recently shown to greatly enhance reprogramming efficiency, the underlying molecular mechanisms still remain largely unknown. Here, we report that miR-199a-3p is upregulated by p53 at the post-transcriptional level. Induction of miR-199a-3p significantly decreases reprogramming efficiency, whereas miR-199a-3p inhibition greatly enhances it. Mechanistically, miR-199a-3p overexpression inhibits cell proliferation by imposing G1 cell cycle arrest. Conversely, miR-199a-3p inhibition results in a pronounced increase in cell proliferation. Furthermore, the enhancement in reprogramming of p53 knockdown cells is almost completely reversed with replacement of miR-199a-3p. Also, miR-199a-3p inhibition partially rescues iPS generation impaired by p53. These findings suggest miR-199a-3p as a novel p53 target that negatively regulates somatic cell reprogramming.
Published: 2012

221. Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription

Author: Jihui Wu, Mian Wu, Jiahai Zhang, Fudong Li, Yide Mei, Lei Liu, Chuanchun Han, Yu Qiu, Chen Zhao, Yunyu Shi, Guohong Li, and Yan Wang
Subjects: Models, Molecular, Transcription, Genetic, Molecular Sequence Data, SAP30, Arginine, Models, Biological, Histones, Histone H3, Genetics, Humans, Amino Acid Sequence, Promoter Regions, Genetic, Histone Acetyltransferases, Homeodomain Proteins, Regulation of gene expression, biology, Lysine, Acetylation, Histone acetyltransferase, Molecular biology, Protein Structure, Tertiary, Cell biology, Protein Transport, Histone, Gene Expression Regulation, PHD finger, biology.protein, Chromatin immunoprecipitation, Protein Binding, Research Paper, Developmental Biology
Abstract: Histone acetylation is a hallmark for gene transcription. As a histone acetyltransferase, MOZ (monocytic leukemia zinc finger protein) is important for HOX gene expression as well as embryo and postnatal development. In vivo, MOZ forms a tetrameric complex with other subunits, including several chromatin-binding modules with regulatory functions. Here we report the solution structure of the tandem PHD (plant homeodomain) finger (PHD12) of human MOZ in a free state and the 1.47 Acrystal structure in complex with H3K14ac peptide, which reveals the structural basis for the recognition of unmodified R2 and acetylated K14 on histone H3. Moreover, the results of chromatin immunoprecipitation (ChIP) and RT-PCR assays indicate that PHD12 facilitates the localization of MOZ onto the promoter locus of the HOXA9 gene, thereby promoting the H3 acetylation around the promoter region and further up-regulating the HOXA9 mRNA level. Taken together, our findings suggest that the combinatorial readout of the H3R2/K14ac by PHD12 might represent an important epigenetic regulatory mechanism that governs transcription and also provide a clue of cross-talk between the MOZ complex and histone H3 modifications. (Keywords: histone acetyltransferase; MOZ; PHD finger; H3R2me0; H3K14ac; HOXA9) Supplemental material is available for this article.
Published: 2012

222. Novel single nucleotide polymorphisms of the bovine methyltransferase 3b gene and their association with meat quality traits in beef cattle

Author: Ying Yu, Y. Zhang, W.H. Shi, Chao Qin, Chuanyue Wang, X.Y. Guo, Qingwang Li, Y.C. Wang, Xuejun Liu, Mian Wu, L. Liu, P.P. Ma, X.Z. Xu, F.J. Geng, and Xiang Zhang
Subjects: Meat, Genotype, Molecular Sequence Data, Population, Single-nucleotide polymorphism, Breeding, Beef cattle, Biology, Polymorphism, Single Nucleotide, Quantitative Trait, Heritable, Animal science, Gene Frequency, Genetics, Animals, DNA (Cytosine-5-)-Methyltransferases, Allele, education, Molecular Biology, Genotyping, Genetic Association Studies, Genetic association, education.field_of_study, Base Sequence, General Medicine, Breed, Cattle
Abstract: DNA methylation is essential for adipose deposition in mammals. We screened SNPs of the bovine DNA methyltransferase 3b (DNMT3b) gene in Snow Dragon beef, a commercial beef cattle population in China. Nine SNPs were found in the population and three of six novel SNPs were chosen for genotyping and analyzing a possible association with 16 meat quality traits. The frequencies of the alleles and genotypes of the three SNPs in Snow Dragon beef were similar to those in their terminal-paternal breed, Wagyu. Association analysis disclosed that SNP1 was not associated with any of the traits; SNP2 was significantly associated with lean meat color score and chuck short rib score, and SNP3 had a significant effect on dressing percentage and back-fat thickness in the beef population. The individuals with genotype GG for SNP2 had a 25.7% increase in lean meat color score and a 146% increase in chuck short rib score, compared with genotype AA. The cattle with genotype AG for SNP3 had 35.7 and 24% increases in dressing percentage and 28.8 and 29.2% increases in back-fat thickness, compared with genotypes GG and AA, respectively. Genotypic combination analysis revealed significant interactions between SNP1 and SNP2 and between SNP2 and SNP3 for the traits rib-eye area and live weight. We conclude that there is considerable evidence that DNMT3b is a determiner of beef quality traits.
Published: 2012

223. Effects of Filament Pre-Tension to the Characteristics of Solo-Sirofil Composite Yarn

Author: Wei Mian Wu, Wei Dong Gao, Yu Qin Wan, Shan Yuan Wang, Rui Hua Yang, Chun Ping Xie, and Hong Bo Wang
Subjects: Materials science, Pre tension, business.industry, Composite number, General Medicine, Structural engineering, Yarn, Breaking strength, Protein filament, visual_art, visual_art.visual_art_medium, Standard test, Species evenness, business, Spinning
Abstract: Pre-tension of filament is critical to the characteristics of solo-sirofil composite yarn. In this paper, solo-sirofil yarns under filament pre-tension of 5-25cN were produced by modified EJM-128K ring spinning frame. The hairiness, breaking strength, breaking work and yarn evenness were tested under standard test conditions. It’s explored that when the pre-tension of filament is 15cN, perform of solo-sirofil achieve the best level with lower hairiness, higher breaking strength and breaking work, and better yarn evenness.
Published: 2011

224. Recognition of Unmodified Histone H3 by the First PHD Finger of Bromodomain-PHD Finger Protein 2 Provides Insights into the Regulation of Histone Acetyltransferases Monocytic Leukemic Zinc-finger Protein (MOZ) and MOZ-related factor (MORF)

Author: Jiahai Zhang, Lei Liu, Mian Wu, Peng Ji, Jihui Wu, Yunyu Shi, Lei Jin, and Su Qin
Subjects: Nuclear Proteins, Cell Biology, SAP30, Biology, Biochemistry, Protein Structure, Secondary, Protein Structure, Tertiary, DNA-Binding Proteins, Histones, Histone H3, Histone H1, PHD finger, Protein Structure and Folding, Histone H2A, Animals, Humans, Histone code, Cattle, Histone octamer, Molecular Biology, Adaptor Proteins, Signal Transducing, Histone Acetyltransferases, Protein Binding, Histone binding
Abstract: MOZ (monocytic leukemic zinc-finger protein) and MORF (MOZ-related factor) are histone acetyltransferases important for HOX gene expression as well as embryo and postnatal development. They form complexes with other regulatory subunits through the scaffold proteins BRPF1/2/3 (bromodomain-PHD (plant homeodomain) finger proteins 1, 2, or 3). BRPF proteins have multiple domains, including two PHD fingers, for potential interactions with histones. Here we show that the first PHD finger of BRPF2 specifically recognizes the N-terminal tail of unmodified histone H3 (unH3) and report the solution structures of this PHD finger both free and in complex with the unH3 peptide. Structural analysis revealed that the unH3 peptide forms a third antiparallel β-strand that pairs with the PHD1 two-stranded antiparallel β-sheet. The binding specificity was determined primarily through the recognition of arginine 2 and lysine 4 of the unH3 by conserved aspartic acids of PHD1 and of threonine 6 of the unH3 by a conserved asparagine. Isothermal titration calorimetry and NMR assays showed that post-translational modifications such as H3R2me2as, H3T3ph, H3K4me, H3K4ac, and H3T6ph antagonized the interaction between histone H3 and PHD1. Furthermore, histone binding by PHD1 was important for BRPF2 to localize to the HOXA9 locus in vivo. PHD1 is highly conserved in yeast NuA3 and other histone acetyltransferase complexes, so the results reported here also shed light on the function and regulation of these complexes.
Published: 2011

225. An online intelligent system for teaching design technologies to engineering students

Author: Mian Wu, Amal Oraifige, Barry Mills, and Ilias Oraifige
Subjects: Engineering, Knowledge management, Higher education, business.industry, Process (engineering), media_common.quotation_subject, Education, Engineering management, Work (electrical), New product development, Quality (business), business, Engineering design process, Engineering (miscellaneous), media_common, Diversity (politics)
Abstract: Engineering design is a knowledge intensive process which encompasses detailed conceptual analysis and evaluation, involving various areas of knowledge and experience. The sharing between these tasks is critical if the capacity for new product development is to be increased whilst its quality is maintained. Design technologies describe the use of a wide range of computer-based tools designed to assist engineers in their activities. The rapid growth of such technologies in engineering design industry is considerable and it is important that education moves into this area of work without delay. As the industry evolves, students in higher education seek to learn technologies that can best serve their future careers. Teaching design technologies in the traditional way may involve presenting in front of an audience and explaining instructions step-by-step. One of the main tasks of competent teaching is to provide a wide diversity of problems and supporting activities. This paper presents the design, de...
Published: 2011

226. E2F1 inhibits MDM2 expression in a p53-dependent manner

Author: Youjun Chen, Wanglai Hu, Mian Wu, and Xu Tian
Subjects: endocrine system, DNA damage, Molecular Sequence Data, Apoptosis, Stimulation, Gene Knockout Techniques, RNA interference, Cell Line, Tumor, Humans, E2F1, Binding site, Promoter Regions, Genetic, neoplasms, Gene knockdown, Binding Sites, Base Sequence, Chemistry, Proto-Oncogene Proteins c-mdm2, Cell Biology, Molecular biology, Up-Regulation, enzymes and coenzymes (carbohydrates), Cell culture, RNA Interference, Tumor Suppressor Protein p53, biological phenomena, cell phenomena, and immunity, E2F1 Transcription Factor, DNA Damage
Abstract: MDM2 expression is down-regulated upon E2F1 over-expression, but the mechanism is not well defined. In the current study, we found that E2F1 inhibits MDM2 expression by suppressing its promoter activity. Although E2F1 binds to the MDM2 promoter, the inhibitory effect of E2F1 on the MDM2 promoter does not require the direct binding. We demonstrate that E2F1 inhibits MDM2 promoter activity in a p53-dependent manner. Knockdown of p53 in U2OS cells impairs the inhibitory effect of E2F1 on the MDM2 promoter. Consistent with this observation, E2F1 does not inhibit MDM2 promoter activity in p53-deficient H1299 cells, and the inhibition is restored when p53 is expressed exogenously. Both E2F1 and p53 are up-regulated after DNA damage stimulation. We show that such stimulation induces E2F1 to inhibit MDM2 promoter activity and promote p53 accumulation. Furthermore, inhibition of MDM2 by E2F1 promotes E2F1 induced apoptosis. These data suggest that E2F1 regulates the MDM2-p53 pathway by inhibiting p53 induced up-regulation of MDM2.
Published: 2011

227. Miktoarm star copolymers via combination of RAFT arm-first technique and aldehyde-aminooxy click reaction

Author: Wen-Li Deng, Jiang Lu, Zhao-Mian Wu, and Hui Liang
Subjects: Polymers and Plastics, Chemistry, Organic Chemistry, Radical polymerization, Chain transfer, Raft, End-group, chemistry.chemical_compound, Polymer chemistry, Materials Chemistry, Copolymer, Click chemistry, Living polymerization, Ethylene glycol
Abstract: A facile synthetic pathway to miktoarm star copolymers with multiple arms has been developed by combining reversible addition–fragmentation chain transfer (RAFT) arm-first technique and aldehyde–aminooxy “click” coupling reaction. Star polystyrene (PS) with aldehyde functionalized core was initially prepared by RAFT arm-first technique via crosslinking of the preformed linear macro-RAFT agents using a newly designed aldehyde-containing divinyl compound 6,6′-(ethane-1,2-diylbis(oxy))bis(3-vinylbenzaldehyde) (EVBA). It was then used as a multifunctional coupling agent for the subsequent formation of the second generation poly(ethylene glycol) (PEG) arms via the click coupling reaction between its aldehyde groups and aminooxy-terminated PEGs. The possible formation of PS-PEG miktoarm star copolymer with Janus-like segregated structure in cyclohexanone was also investigated. © 2010 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 48: 3323–3330, 2010
Published: 2010

228. Nucleophosmin/B23 Inhibits Eg5-mediated Microtubule Depolymerization by Inactivating Its ATPase Activity

Author: Zhan Yao, Qinghua Shi, Yun Huang, Guoxing Wang, Mian Wu, and Xiang Gao
Subjects: Swine, ATPase, Down-Regulation, Kinesins, Microtubules, Biochemistry, Microtubule polymerization, Cytosol, Microtubule, Two-Hybrid System Techniques, Animals, Humans, RNA, Small Interfering, Molecular Biology, Adenosine Triphosphatases, Nucleophosmin, biology, Nuclear Proteins, RNA, Cell Biology, Cell biology, Gene Expression Regulation, Neoplastic, biology.protein, Kinesin, HeLa Cells, Subcellular Fractions, Binding domain
Abstract: Nucleophosmin/B23, an abundant nucleolar protein, plays multiple roles in cell growth and proliferation, and yet, little has been studied about its function in regulating dynamics of microtubules. Here, we report that B23 directly interacts with Eg5, a member of the kinesin family, in the cytosol. The DNA/RNA binding domain of B23 and the motor domain of Eg5 were found to be involved in their interaction. Both in vivo and in vitro evidences showed that B23 acts as an upstream regulator of Eg5 in promoting microtubule polymerization. Moreover, we further demonstrated that B23 regulates microtubule dynamics by directly inhibiting Eg5 ATPase activity.
Published: 2010

229. Synthesis of Poly(N-isopropylacrylamide)−Poly(ethylene glycol) Miktoarm Star Copolymers via RAFT Polymerization and Aldehyde−Aminooxy Click Reaction and Their Thermoinduced Micellization

Author: Zhao-Mian Wu, Jiang Lu, and Hui Liang
Subjects: Polymers and Plastics, Chemistry, Organic Chemistry, Radical polymerization, Chain transfer, Inorganic Chemistry, chemistry.chemical_compound, Polymerization, Polymer chemistry, Materials Chemistry, Poly(N-isopropylacrylamide), Click chemistry, Copolymer, Reversible addition−fragmentation chain-transfer polymerization, Ethylene glycol
Abstract: A facile synthetic pathway to poly(N-isopropylacrylamide) (PNIPAM)−poly(ethylene glycol) (PEG) miktoarm star copolymers with multiple arms has been developed by combining reversible addition−fragmentation chain transfer (RAFT) polymerization and aldehyde−aminooxy “click” coupling reaction. Star PNIPAM with aldehyde functionalized core was initially prepared by the RAFT arm-first technique via cross-linking of the preformed linear macro-RAFT agents using a newly designed aldehyde-containing divinyl compound 6,6′-(ethane-1,2-diylbis(oxy))bis(3-vinylbenzaldehyde) (EVBA). It was then used as a multifunctional coupling agent for the subsequent formation of the second-generation PEG arms via the click coupling reaction between its aldehyde groups and aminooxy-terminated PEGs. The thermoresponsive micellization behavior of PNIPAM−PEG miktoarm star copolymer with different PEG arm numbers in water was also investigated. Opportunities are open for thermoinduced intermolecular or intramolecular micellization of PNI...
Published: 2010

230. B23 acts as a nucleolar stress sensor and promotes cell survival through its dynamic interaction with hnRNPU and hnRNPA1

Author: Zhan Yao, Shanshan Duan, Mian Wu, Yuan Liu, Longping Wen, Dezhi Hou, Guanghui Wang, and Wenchao Wang
Subjects: Untranslated region, Cancer Research, Transcription, Genetic, Cell Survival, Nucleolus, Heterogeneous Nuclear Ribonucleoprotein A1, bcl-X Protein, Ribosome biogenesis, Apoptosis, RNA polymerase II, Heterogeneous-Nuclear Ribonucleoproteins, Heterogeneous-Nuclear Ribonucleoprotein Group A-B, Genetics, RNA polymerase I, Humans, RNA, Messenger, 3' Untranslated Regions, Molecular Biology, Ribonucleoprotein, Messenger RNA, biology, Cell Cycle, Nuclear Proteins, RNA, Ribonuclease, Pancreatic, DNA Polymerase I, Molecular biology, Cell biology, Protein Transport, biology.protein, Nucleophosmin, Ribosomes, Cell Nucleolus, HeLa Cells
Abstract: The nucleolus is one of the functional nuclear compartments in which the ribosome biogenesis takes place. Proteomic analysis revealed a large number of nucleolar proteins that are involved in diverse cellular processes, including biogenesis of ribonucleoprotein particles, stress responses, cell proliferation and cell cycle progression. Here, we report that in response to transcription repression-induced nucleolar segregation, B23, a nucleolar protein required for rRNA processing, is localized to the cytoplasm and forms a complex with the mRNA-binding proteins hnRNPU and hnRNPA1 in a sequential manner. In addition, RNA Polymerase I, but not RNA Polymerase II inhibition, was found to account for the translocation-dependent assembly of B23/hnRNPU/hnRNPA1. We also showed that interactions among these proteins are regulated by hnRNPU-bound mRNAs such as the 3'-untranslated region (UTR) of Bcl-xL mRNA. Ectopically expressed 3'-UTR of Bcl-xL mRNA, which disrupted the interactions among B23, hnRNPU and hnRNPA1, led to enhanced cell apoptosis induced by either actinomycin D treatment or mitotic arrest. Overall, these data highlight a novel function of B23 as a stress sensor in the assembly of B23/hnRNPU/hnRNPA1 complex to promote cell survival.
Published: 2010

231. The Pirh2–keratin 8/18 interaction modulates the cellular distribution of mitochondria and UV-induced apoptosis

Author: Dezhi Hou, Mian Wu, Longping Wen, Guanghui Wang, Y Zhu, Zhan Yao, and Shanshan Duan
Subjects: Programmed cell death, Ultraviolet Rays, Ubiquitin-Protein Ligases, Intermediate Filaments, Apoptosis, macromolecular substances, Mitochondrion, Keratin 18, Cell Line, Tumor, Protein Interaction Mapping, Keratin, Humans, Intermediate filament, Molecular Biology, chemistry.chemical_classification, Keratin-18, biology, Keratin-8, Cell Biology, Mitochondria, Ubiquitin ligase, Cell biology, chemistry, Cytoplasm, Gene Knockdown Techniques, biology.protein, Keratin 8, RNA Interference
Abstract: Intermediate filaments (IFs) provide crucial structural support in higher eukaryotic cells. Accumulating evidences show that IFs also participate in various cellular activities including stress responses, cell growth, cell death and cell migration through dynamic interactions with various non-structure proteins. Here we report the identification of Pirh2, a RING-H2-type ubiquitin E3 ligase, as a novel binding partner of the cytoplasmic IF proteins keratin 8/18 (K8/18). Phosphorylation of either Pirh2 or K8/18 affects their association. Although Pirh2 was not found to influence the stability of K8/18, it displayed an unexpected role in regulating the organization of the network of K8/18 keratin filaments. Disruption of Pirh2-K8/K18 interaction by either UV irradiation or knockdown with Pirh2 or K18 led to the aggregation of K8/18 keratin filaments. It further induced mitochondrial redistribution, and this process is likely through a microtubule-mediated pathway. The abnormal localization of mitochondria in Pirh2-knockdown cells may partially account for its increased cell sensitivity to UV-induced apoptosis, probably through enhancing the release of pro-apoptotic proteins, such as cytochrome c and Smac/DIABLO to the cytosol. Overall, our data reveal the novel role of the Pirh2-K8/18 complex in governing the distribution of mitochondria.
Published: 2009

232. E2F1 represses β‐catenin/TCF activity by direct up‐regulation of Siah1

Author: Mian Wu, Wei Xie, Yide Mei, and Lei Jin
Subjects: Chromatin Immunoprecipitation, endocrine system, Ubiquitin-Protein Ligases, Biology, TCF/LEF family, Transcription (biology), Cell Line, Tumor, Transcriptional regulation, Humans, E2F1, E2F, Psychological repression, beta Catenin, DNA Primers, Base Sequence, Nuclear Proteins, Articles, Cell Biology, Molecular biology, Up-Regulation, Molecular Medicine, Ectopic expression, biological phenomena, cell phenomena, and immunity, TCF Transcription Factors, Chromatin immunoprecipitation, E2F1 Transcription Factor
Abstract: Transcription factor E2F1 is a key regulator of cell proliferation and apoptosis. Its activity is strictly controlled by the pRB/E2F pathway. In the majority of cancer cells, however, this pathway is frequently found deregulated, and the underlying mechanism involving transcriptional control by E2F1 has not yet been fully elucidated. Here we report the identification of two putative E2F1-binding sites located upstream from Siah1 transcription start site (+1). Chromatin immunoprecipitation assay reveals that transcription factor E2F1 is capable of binding to the putative sites, and luciferase reporter assay shows that E2F1 can activate transcription from the Siah1 promoter. Ectopic expression of E2F1 elevates the Siah1 level, hence suppressing the beta-catenin/TCF activity. Consistently, knock-down of endogenous E2F1 by a shRNA strategy results in reduced expression of Siah1. Moreover, repression of beta-catenin/TCF activity by E2F1 can be attenuated by shRNA-based repression of endogenous Siah1, implying that Siah1 is a bona fide E2F1 target gene, which at least partly, mediates the suppression of beta-catenin/TCF signalling pathway.
Published: 2008

233. Tumor Suppressor ARF Promotes Non-classic Proteasome-independent Polyubiquitination of COMMD1

Author: Mian Wu, Hoi-Yeung Li, and Yafen Huang
Subjects: Proteasome Endopeptidase Complex, Nucleolus, Proteolysis, Mutant, Endogeny, macromolecular substances, Models, Biological, environment and public health, Biochemistry, Ubiquitin, Cell Line, Tumor, medicine, Humans, Fluorescent Antibody Technique, Indirect, Molecular Biology, Cyclin-Dependent Kinase Inhibitor p16, Adaptor Proteins, Signal Transducing, Nucleoplasm, biology, medicine.diagnostic_test, Chemistry, Lysine, Cell Biology, Protein Structure, Tertiary, Cell biology, Gene Expression Regulation, Neoplastic, Tumor Suppressor ARF, Proteasome, Dactinomycin, biology.protein, Tumor Suppressor Protein p53, Carrier Proteins, Gene Deletion, DNA Damage
Abstract: Although the tumor suppressor ARF is generally accepted for its essential role in activating the p53 pathway, its p53-independent function has also been proposed. Here, we report that ARF associates with COMMD1 and promotes Lys(63)-mediated polyubiquitination of COMMD1 in a p53-independent manner. We found that ARF interacts with COMMD1 in vivo. Deletion analysis of ARF suggested that the N-terminal amino acids 15-45 are important for its interaction with COMMD1. In addition, we found that endogenous ARF redistributes from the nucleolus to the nucleoplasm and interacts with COMMD1 when DNA is damaged by actinomycin D. Interestingly, we found that ARF promotes the polyubiquitination of COMMD1 through Lys(63) of ubiquitin but not the polyubiquitination of Lys(48), which does not target COMMD1 for proteasome-dependent proteolysis. Moreover, ARF mutants lacking the domain interacting with COMMD1 did not promote COMMD1 polyubiquitination, indicating that physical association is a prerequisite condition for the polyubiquitination process. Together, these data suggest that the ability to promote Lys(63)-mediated polyubiquitination of COMMD1 is a novel property of ARF independent of p53.
Published: 2008

234. Biocompatible, Luminescent Silver@Phenol Formaldehyde Resin Core/Shell Nanospheres: Large-Scale Synthesis and Application for In Vivo Bioimaging

Author: Shu-Hong Yu, Shirui Guo, Peng Jiang, Yang Lu, Jun-Yan Gong, and Mian Wu
Subjects: chemistry.chemical_classification, Materials science, Dispersity, food and beverages, Nanoparticle, Nanotechnology, Condensed Matter Physics, Biocompatible material, Hydrothermal circulation, Electronic, Optical and Magnetic Materials, Biomaterials, Polymerization, chemistry, In vivo, Phenol formaldehyde resin, Electrochemistry, Luminescence
Abstract: Biocompatible and green luminescent monodisperse silver/phenol formaldehyde resin core/shell spheres with controllable sizes, in the range of 180 to 1000 nm, and interesting architectures (centric, eccentric, and coenocytic core/shell spheres) have been synthesized by a facile one-step hydrothermal approach. These spheres can be used as bioimaging labels for human lung cancer H1299 cells. The results demonstrate that the nanoparticles can be internalized into cells and exhibit no cytotoxic effects, showing that such novel biocompatible core/shell structures can potentially be used as in vivo bioimaging labels. This facile one-pot polymerization and encapsulation technique may provide a useful tool to synthesize other core/shell particles that have potential application in biotechnology.
Published: 2008

235. Sumoylation is critical for DJ-1 to repress p53 transcriptional activity

Author: Mian Wu, Peng Jiang, Jun Fan, Zheng Ying, Guanghui Wang, Haigang Ren, Erkang Fei, and Nali Jia
Subjects: DJ-1, Programmed cell death, Transcription, Genetic, Protein Deglycase DJ-1, Mutant, Active Transport, Cell Nucleus, Biophysics, SUMO protein, Apoptosis, Biology, medicine.disease_cause, Biochemistry, Cell Line, Mice, Bcl-2-associated X protein, Structural Biology, Transcription (biology), Genetics, medicine, Animals, Humans, Promoter Regions, Genetic, Molecular Biology, bcl-2-Associated X Protein, Cell Nucleus, Oncogene Proteins, Mutation, Intracellular Signaling Peptides and Proteins, Sumoylation, Cell Biology, p53 transcriptional activity, Molecular biology, Cell nucleus, medicine.anatomical_structure, Bax, Cytoplasm, Parkinson’s disease, Small Ubiquitin-Related Modifier Proteins, biology.protein, Tumor Suppressor Protein p53, Protein Processing, Post-Translational
Abstract: Sumoylation is an important post-translational modification, which is also involved in the pathogenesis of many neurodegenerative diseases. We previously reported that DJ-1 decreases Bcl-2 associated X protein expression through repressing p53 transcriptional activity. Here we show that DJ-1(K130R), the non-sumoylatable mutant form of DJ-1, shifts from nucleus to cytoplasm, fails to repress p53 transcriptional activity and loses its protective function against ultraviolet induced cell death. Our findings suggest that sumoylation is critical for DJ-1 to repress p53 transcriptional activity.
Published: 2008

236. DJ-1 Decreases Bax Expression through Repressing p53 Transcriptional Activity

Author: Nali Jia, Tian Zhou, Guanghui Wang, Haigang Ren, Mian Wu, Erkang Fei, Peng Jiang, and Jun Fan
Subjects: Programmed cell death, Transcription, Genetic, Ultraviolet Rays, Protein Deglycase DJ-1, Apoptosis, Biology, medicine.disease_cause, Biochemistry, Cell Line, Transcriptional regulation, medicine, Humans, Immunoprecipitation, Molecular Biology, DNA Primers, bcl-2-Associated X Protein, Oncogene Proteins, Gene knockdown, Base Sequence, Oncogene, Intracellular Signaling Peptides and Proteins, Hydrogen Peroxide, Cell Biology, Cytoprotection, Cell biology, Caspases, Cancer research, Tumor Suppressor Protein p53, Oxidative stress
Abstract: DJ-1, originally identified as an oncogene product, is a protein with various functions in cellular transformation, oxidative stress response, and transcriptional regulation. Although previous studies suggest that DJ-1 is cytoprotective, the mechanism by which DJ-1 exerts its survival functions remains largely unknown. Here we show that DJ-1 exerts its cytoprotection through inhibiting p53-Bax-caspase pathway. DJ-1 interacts with p53 in vitro and in vivo. Overexpression of DJ-1 decreases the expression of Bax and inhibits caspase activation, whereas knockdown of DJ-1 increases Bax protein levels and accelerates caspase-3 activation and cell death induced by UV exposure. Our data provide evidence that the protective effects of DJ-1 on apoptosis are associated with its ability of decreasing Bax level through inhibiting p53 transcriptional activity.
Published: 2008

237. Influencing Factors Analysis and Mathematical Model for the Formaldehyde Emission from Plywood

Author: Meng, Mian-Wu, primary, Hong, Wei, additional, Qi, Cong-Liang, additional, Liu, Qing-Ye, additional, Zhou, Zhen-Ming, additional, Chen, Chun-Qiang, additional, Huang, Cai-Yan Kang, additional, and Si-yu, Dr, additional
Published: 2017
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238. Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain

Author: Naseruddin Höti, Yide Mei, Shanshan Feng, De-e Zhu, Li Ma, Mark Castanares, Yonghui Yang, and Mian Wu
Subjects: Inhibitor of apoptosis domain, Caspase 8, MAP kinase kinase kinase, biology, Caspase-Independent Apoptosis, Cyclin-dependent kinase 2, NF-kappa B, Apoptosis, Cell Biology, Mitogen-activated protein kinase kinase, Cell Line, MAP2K7, Cell biology, Caspases, Catalytic Domain, Receptor-Interacting Protein Serine-Threonine Kinases, biology.protein, Animals, Humans, ASK1, Kinase activity, Signal Transduction
Abstract: RIP3 (Receptor Interacting Protein 3), a member of the Ser/Thr kinase family, is able to induce apoptosis and activate NF-kappaB in various cell types. However, the detailed mechanism of RIP3-induced apoptosis is largely unknown. In this study, we show that RIP3 is cleaved at Asp328 by caspase-8 under apoptotic stimuli, which is blocked by pan-caspase inhibitor Z-VAD-FMK. In addition, full-length RIP3 induces both caspase-dependent and-independent apoptosis, as well as activates NF-kappaB. However, after cleavage, the C-terminus of RIP3 (aa 329-518) that lacks the kinase domain can form punctuate or filaments-like structures in cytoplasm, which induces only caspase-dependent apoptosis and exhibits a markedly higher NF-kappaB-activating activity than full-length RIP3. More importantly, the cleaved product of RIP3 (aa 329-518) displays better stability than wild type RIP3. Additionally, RIP3(K50A), a kinase-dead RIP3 mutant, also induces only caspase-dependent apoptosis along with an increased NF-kappaB-activating activity compared to RIP3, which further demonstrates that kinase activity of RIP3 is essential for its caspase-independent apoptotic activity. These results will help us to understand the mechanism underlying RIP3-induced apoptosis and the different roles of kinase domain and unique domain of RIP3.
Published: 2007

239. Siah-1S, a novel splice variant of Siah-1 (seven in absentia homolog), counteracts Siah-1-mediated downregulation of β-catenin

Author: Chongwei Xie, Wei Xie, Zhengsheng Wu, Yide Mei, and Mian Wu
Subjects: Proteasome Endopeptidase Complex, Cancer Research, Beta-catenin, Ubiquitin-Protein Ligases, Molecular Sequence Data, Down-Regulation, Apoptosis, Plasma protein binding, Cell Line, Exon, Ubiquitin, Downregulation and upregulation, Genes, Reporter, Skp1, Genetics, Humans, Protein Isoforms, Amino Acid Sequence, Molecular Biology, beta Catenin, Etoposide, Sequence Homology, Amino Acid, biology, Calcium-Binding Proteins, Alternative splicing, Intron, Nuclear Proteins, Molecular biology, Up-Regulation, Alternative Splicing, biology.protein, Dimerization, Sequence Alignment, Protein Binding
Abstract: Siah-1 (seven in absentia homolog) is known to cause indirect degradation of beta-catenin through formation of a complex with Siah-interacting protein (SIP), Skp1 and Ebi. Here, we report the characterization of a novel splice variant of human Siah-1, designated Siah-1S, which is produced by an alternative splicing mechanism. The novel intron/exon junctions used to generate Siah-1S follow a non-conventional CT-AC rule. Siah-1S exhibits an even shorter half-life than Siah-1 and is able to catalyse self-ubiquitination that results in its subsequent degradation by proteasome. Siah-1S is shown to upregulate beta-catenin-dependent Tcf/Lef transcriptional activation and antagonize Siah-1's potentiation effect on the apoptosis induced by etoposide in MCF-7 cells. Additionally, Siah-1S is found to interact with Siah-1 to form heterodimer or with itself to form homodimer. Unlike homodimer Siah-1*Siah-1, neither Siah-1*Siah-1S nor Siah-1S*Siah-1S is able to bind to Siah-1-interacting protein, which may explain the underlying mechanism for Siah-1S's dominant negative effect on Siah-1. Importantly, results from in vitro soft agar assay demonstrated that Siah-1S displays a promotion effect on cells tumorigenicity.
Published: 2007

240. Increased urinary Smad3 is significantly correlated with glomerular hyperfiltration and a reduced glomerular filtration rate and is a new urinary biomarker for diabetic nephropathy

Author: Lei Zhang, Mingliang Zhang, Haoyong Yu, Jing-xin Kou, Weiping Jia, Yuqian Bao, Haibing Chen, Junxi Lu, Mian Wu, and Kaifeng Guo
Subjects: Blood Glucose, Male, medicine.medical_specialty, Urinary system, Renal function, Blood Pressure, Diabetic nephropathy, Type 2 diabetes, Nephropathy, Diabetes mellitus, Internal medicine, medicine, Humans, Insulin, Diabetic Nephropathies, Smad3 Protein, Aged, Glycated Hemoglobin, Proteinuria, C-Peptide, business.industry, Age Factors, Middle Aged, medicine.disease, Endocrinology, Diabetes Mellitus, Type 2, Glomerular hyperfiltration, Nephrology, Case-Control Studies, Female, medicine.symptom, business, Biomarkers, Glomerular Filtration Rate, Research Article, Smad3
Abstract: Background Diabetic nephropathy is one of the major microvascular complications of diabetes. We investigated the association between urinary Smad3 (usmad3) levels, glomerular hyperfiltration, and the development of nephropathy in patients with type 2 diabetes mellitus (T2DM). Methods The usmad3 level was determined by enzyme-linked immunosorbent assay in 245 well-characterised patients with T2DM and 82 healthy control subjects. The associations of the usmad3 level with glomerular hyperfiltration, glucose and lipid profiles, and renal function were evaluated. Results The usmad3 level was significantly higher in patients with diabetes than in the control group. The level in the hyperfiltration group was higher than that in the normofiltering group, regardless of whether patients were in the normoalbuminuric or the proteinuria groups. Pearson’s correlation analysis suggested that the usmad3 level was significantly correlated with age, systolic blood pressure, fasting plasma glucose, insulin, C-peptide, glycated haemoglobin, and estimated glomerular filtration rate (eGFR). A multiple linear stepwise regression analysis revealed that usmad3 levels in patients with T2DM and an eGFR ≥90 ml/min/1.73 m2 were independently and positively correlated with eGFR, whereas in patients with T2DM and eGFR
Published: 2015

241. Highly selective and effective solid phase microextraction of benzoic acid esters using ionic liquid functionalized multiwalled carbon nanotubes-doped polyaniline coating

Author: Youhong Ai, Baizhao Zeng, Lulu Li, Mian Wu, and Faqiong Zhao
Subjects: Chromatography, Gas, Inorganic chemistry, Ionic Liquids, 02 engineering and technology, Methyl benzoate, Solid-phase microextraction, 01 natural sciences, Biochemistry, Ethyl benzoate, Analytical Chemistry, chemistry.chemical_compound, Aniline, Limit of Detection, Polyaniline, Propyl benzoate, Solid Phase Microextraction, Benzoic acid, Chromatography, Aniline Compounds, Nanotubes, Carbon, 010401 analytical chemistry, Organic Chemistry, Esters, General Medicine, Benzoic Acid, 021001 nanoscience & nanotechnology, 0104 chemical sciences, chemistry, Ionic liquid, 0210 nano-technology, Water Pollutants, Chemical
Abstract: The present work reports the electrochemical fabrication of an ionic liquid functionalized multiwalled carbon nanotubes-polyaniline (MWCNT@IL/PANI) nanocomposite coating and its application in the headspace-solid phase microextraction (HS-SPME) and gas chromatography (GC) determination of benzoic acid esters (i.e., methyl benzoate, ethyl benzoate, propyl benzoate and butyl benzoate). The MWCNTs was firstly functionalized with amine-terminated IL (MWCNT@IL) through chemical reduction, and then was doped in PANI during the electropolymerization of aniline. The resulting coating was characterized by infrared spectroscopy, field emission scanning electron microscopy and thermo gravimetry. It showed net-like structure and had high thermal stability (up to 330°C). Furthermore, it presented high selectivity for the four benzoic acid esters and thus suited for their HS-SPME-GC determination. Results showed that under optimized extraction conditions, the detection limits were less than 6.1ngL(-1) (S/N=3) and the linear detection ranges were 0.012-50μgL(-1) (R≥0.9957) for these analytes. The relative standard deviations (RSDs) were lower than 6.4% for five successive measurements with one fiber, and the RSDs for fiber-to-fiber were 4.4-9.6% (n=5). The developed method was successfully applied to the determination of these benzoic acid esters in perfume samples.
Published: 2015

242. The Chronic Kidney Disease Epidemiology Collaboration equation improves the detection of hyperfiltration in Chinese diabetic patients

Author: Fangya, Zhao, Lei, Zhang, Junxi, Lu, Kaifeng, Guo, Mian, Wu, Haoyong, Yu, Mingliang, Zhang, Yuqian, Bao, Haibing, Chen, and Weiping, Jia
Subjects: Original Article, urologic and male genital diseases
Abstract: Objective: Hyperfiltration confers an increased risk of diabetic nephropathy. Early detection can ensure timely intervention and improved treatment outcomes. Because GFR is known to be affected by hyperglycemia, the aim of this study was to compare the influence of hyperglycemia on GFR estimations calculated by the CKD-EPI equation, the CG equation, and the MDRD equations in estimating hyperfiltration in Chinese diabetic patients. Materials and methods: The performance of the equations, compared with the measured 99mTc-DTPA glomerular filtration rate was analyzed in 3492 diabetic patients. Bias, precision, and accuracies were compared with respect to HbA1c status. The Bland-Altman method was used to evaluate the agreement among the equations with respect to the mGFR, and the receiver-operating characteristic curve method was used to evaluate diagnostic value of the three equations with respect to the detection of moderate renal failure and hyperfiltration. Results: The mean absolute bias was the smallest for the CKD-EPI equation in the HbA1c < 7.2% cohort, and the highest accuracy within ± 15% and ± 30% was also reached with the CKD-EPI equation in both cohorts. For the detection of hyperfiltration, the CKD-EPI equation exhibited the best performance with the greatest combination of sensitivity and specificity. The biases of the three equations were significantly higher in the HbA1c ≥ 10.5% subgroup compared with the HbA1c < 7.2% cohort. Conclusion: The CKD-EPI equation can be used as a screening tool for hyperfiltration and appears to be a more generalizable and accurate equation for estimating GFR in Chinese diabetic patients.
Published: 2015

243. Facile fabrication of ionic liquid doped polycarbazole coating for the headspace solid-phase microextraction of some environmental pollutants

Author: Mian Wu, Faqiong Zhao, Baizhao Zeng, and Yuanyuan Feng
Subjects: Carbazoles, Ionic Liquids, 02 engineering and technology, engineering.material, Solid-phase microextraction, 01 natural sciences, Analytical Chemistry, chemistry.chemical_compound, Coating, Coated Materials, Biocompatible, Hexafluorophosphate, Fiber, Solid Phase Microextraction, Detection limit, Chromatography, Polydimethylsiloxane, Chemistry, 010401 analytical chemistry, 021001 nanoscience & nanotechnology, Electroplating, 0104 chemical sciences, Ionic liquid, engineering, Environmental Pollutants, Gas chromatography, 0210 nano-technology, Nuclear chemistry
Abstract: A novel polycarbazole (PCz)-ionic liquid (IL, i.e. 1-hydroxyethyl-3-methylimidazolium bis[(trifluoromethyl)sulfonyl]imide, [HOEMIm][NTf2]) composite coating (PCz-IL) was fabricated by electrodeposition. The IL could facilitate the electrodeposition of poor-conductive PCz and a more porous coating was obtained. The composite coating exhibited enhanced extraction capacity for some environmental pollutants (i.e. o-chlorotoluene, p-bromotoluene, o-nitrotoluene, m-nitrotoluene, p-nitrotoluene), as they could interact through π-π and hydrophobic interactions. Compared with [HOEMIm][NTf2] coated fiber, some other PCz-IL fibers (here IL=1-hydroxyethyl-3-methylimidazolium hexafluorophosphate and 1-methyl-3-octylimidazolium hexafluorophosphate) and commercial fibers (i.e. polydimethylsiloxane and polyacrylate), the PCz-IL fiber showed better performance. It was used for the determination of the environmental pollutants by coupling with gas chromatography, the limits of detection were 47.8-65.9 ng L(-1) under the optimized conditions and the linear ranges were 0.1-500 μg L(-1) with correlation coefficients above 0.9947 for different compounds. The relative standard deviations (RSDs) were 3.4-4.6% for five successive extractions with single fiber, and the RSDs for inter-fiber were 6.5-10.4% (n=5). The fiber was successfully applied to the detection of real samples and the recoveries for standards added were 88.6-108.8% with RSDs below 9.7%.
Published: 2015

244. Chaperone-mediated autophagy prevents apoptosis by degrading BBC3/PUMA

Author: Li Guan, Zhanxiang Wang, Wei Xie, Xiaotong Li, Haifeng Jiao, Lei Zhang, Mian Wu, Han You, Jiahuai Han, and Junmin Zha
Subjects: Programmed cell death, Apoptosis, Models, Biological, Phosphoserine, Chaperone-mediated autophagy, Puma, Lysosome, Cell Line, Tumor, Proto-Oncogene Proteins, medicine, Autophagy, Serine, Humans, Phosphorylation, HSPA8, Molecular Biology, biology, Kinase, Protein Stability, Tumor Necrosis Factor-alpha, Cell Biology, biology.organism_classification, Basic Research Paper, Cell biology, I-kappa B Kinase, medicine.anatomical_structure, Proteolysis, Apoptosis Regulatory Proteins, Molecular Chaperones
Abstract: Autophagy is a potentially inimical pathway and together with apoptosis, may be activated by similar stress stimuli that can lead to cell death. The molecular cues that dictate the cell fate choice between autophagy and apoptosis remain largely unknown. Here we report that the proapoptotic protein BBC3/PUMA (BCL2 binding component 3) is a bona fide substrate of chaperone-mediated autophagy (CMA). BBC3 associates with HSPA8/HSC70 (heat shock 70 kDa protein 8), leading to its lysosome translocation and uptake. Inhibition of CMA results in stabilization of BBC3, which in turn sensitizes tumor cells to undergo apoptosis. We further demonstrate that upon TNF (tumor necrosis factor) treatment, IKBKB/IKKβ (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase beta)-mediated BBC3 Ser10 phosphorylation is crucial for BBC3 stabilization via blocking its degradation by CMA. Mechanistically, Ser10 phosphorylation facilitates BBC3 translocation from the cytosol to mitochondria. BBC3 stabilization resulting from either Ser10 phosphorylation or CMA inhibition potentiates TNF-induced apoptotic cell death. Our findings thus reveal that the selective degradation of BBC3 underlies the prosurvival role of CMA and define a previously unappreciated proapoptotic role of IKBKB that acts through phosphorylation-mediated stabilization of BBC3, thereby promoting TNF-triggered apoptosis.
Published: 2015

245. [Spatial variability of soil nitrogen and related affecting factors at a county scale in hilly area of Mid-Sichuan Basin]

Author: You-Lin, Luo, Qi-Quan, Li, Chang-Quan, Wang, Bin, Li, Xin, Zhang, Wen-Ying, Feng, Qian, Weng, and Mian, Wu
Subjects: China, Soil, Spatial Analysis, Nitrogen
Abstract: Spatial distribution characteristics of soil total nitrogen ( TN ) and available nitrogen ( AN ) were analyzed by using geostatistical methods and the effects of the influencing factors were quantified by regression analysis based on 555 soil samples collected in RenShou county. The results showed that the contents of soil TN ranged from 0.34-2.57 g x kg(-1) with a mean value of 1.12 g x kg(-1), which indicated the TN of the study area was at a medium level, and AN ranged from 25.86-184.17 mg x kg(-1) with a mean value of 74.35 mg x kg(-1), which indicated the AN of the study area was low. The values of the nugget to sill ratio were 0.608 and 0.790 respectively, which suggestd TN had moderate spatial dependence, which was determined by the co-effects of structural and random factors, while AN was mainly affected by random factors. The contents of TN and AN in north area were much higher than those of south area and distribution of Patchy. The soil parent materials were able to explain 6.3% and 1.0% of TN and AN spatial variability. Soil types explained 26.5% - 36.1% of TN variability and 27.7% - 28.7% of AN variability. Topographical factors explained 5.5% of TN variability and 6.1% of AN variability, the structural factors of soil types reflected spatial variability of nitrogen in the study area. The randomness factors of land use types explained 37.7% of TN variability and 40.0% of AN variability that were much larger than the other factors, which suggested land use had the higherst independent explaining capacity for nitrogen spatial variability among those influence factors and land use type was the main factor to accurately predict the spatial distribution of soil nitrogen in the hilly area of Middle Sichuan Basin.
Published: 2015

246. MiR-181a regulates lipid metabolism via IDH1

Author: Lin Miao, Ting Wu, Bo Chu, Yide Mei, and Mian Wu
Subjects: Genetically modified mouse, Lipid Metabolism Disorder, Transgene, Mice, Transgenic, CHO Cells, Biology, Article, Cell Line, Mice, Cricetulus, medicine, Animals, Triglycerides, Regulation of gene expression, Binding Sites, Multidisciplinary, Base Sequence, Neurodegeneration, Lipid metabolism, Lipid Metabolism, medicine.disease, Isocitrate Dehydrogenase, Cell biology, Citric acid cycle, MicroRNAs, Cholesterol, Isocitrate dehydrogenase, Gene Expression Regulation, RNA Interference
Abstract: Lipid metabolism is important for cellular energy homeostasis. Excessive cellular lipid accumulation is associated with various human diseases such as obesity, cardiovascular disease or even cancer. It has been recognized that miR-181a is an important modulator in regulating T lymphocyte differentiation, vascular development and cerebellar neurodegeneration. Here we reports a novel function of miR-181a in the regulation of lipid metabolism. MiR-181a is able to target isocitrate dehydrogenase 1 (IDH1), a metabolic enzyme in TCA cycle. Via targeting IDH1, miR-181a decreases expression of genes involved in lipid synthesis and increases expression of genes involved in β-oxidation, thereafter inhibiting lipid accumulation. MiR-181a transgenic mice show a lower body weight as compared with their wild-type littermates and moreover, miR-181a transgenic mice exhibit less lipid accumulation. Collectively, these findings uncover a novel miR-181a-IDH1 axis that has an important role in regulating lipid metabolism and implicate miR-181a as a potential therapeutic target for lipid metabolism disorders.
Published: 2015
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247. Efficacy of dendritic cell-cytokine-induced killer immunotherapy plus intensity-modulated radiation therapy in treating elderly patients with esophageal carcinoma

Author: N Ba, Lin Wang, Wang Xinling, G Y Shi, Mian Wu, L Yan, Z S Zhang, and H Q Zhang
Subjects: Oncology, Male, medicine.medical_specialty, Esophageal Neoplasms, medicine.medical_treatment, Cell- and Tissue-Based Therapy, law.invention, Immune system, Cytokine-Induced Killer Cells, Randomized controlled trial, law, Internal medicine, Genetics, medicine, Carcinoma, Humans, Molecular Biology, Aged, business.industry, General Medicine, Immunotherapy, Dendritic cell, Dendritic Cells, Middle Aged, medicine.disease, Radiation therapy, Bone marrow suppression, Toxicity, Immunology, Female, Radiotherapy, Intensity-Modulated, business
Abstract: We investigated the clinical efficacy of adoptive cytokine-induced killer (CIK) cell and dendritic cell (DC) therapy plus intensity-modulated radiation therapy (IMRT) for treating elderly patients with esophageal carcinoma (EC). In total, 68 elderly patients with EC were randomized to receive IMRT plus DC-CIK immunotherapy (study group, N = 34) or IMRT only (control group, N = 34). Clinical efficacy, immune function, toxicity and side effects, and life quality were evaluated after treatment. The efficacy rate was significantly higher in the study group than in the control group. Remarkable increases were noted for quality of life and immune function in the study group relative to the control group. Regarding toxicity and side effects, compared with the control group, the study group displayed a higher fever rate, a lower incidence rate of bone marrow suppression, and a similar rate of digestive tract reactions. DC-CIK immunotherapy plus IMRT exhibited better short-term efficacy than IMRT alone in elderly patients with EC. The therapy could improve patients'quality of life and immune function, decrease bone marrow suppression, and lengthen survival time.
Published: 2015

248. Functional Evolution of Phosphatidylethanolamine Binding Proteins in Soybean and Arabidopsis

Author: Jianxin Ma, Zheng Wang, Tengfei Liu, Qing Li, Yuanyuan Ji, Tian Tang, Yanting Shen, Chao Fang, Yunfeng Liu, Min Wang, Zhengkui Zhou, Zhixi Tian, Congcong Li, and Mian Wu
Subjects: Subfamily, Molecular Sequence Data, Arabidopsis, Locus (genetics), Phosphatidylethanolamine Binding Protein, Plant Science, Flowers, Biology, Genes, Plant, Evolution, Molecular, Gene Expression Regulation, Plant, Genes, Duplicate, Gene duplication, Amino Acid Sequence, Amino Acids, Gene, Phosphatidylethanolamine binding, Research Articles, Plant Proteins, chemistry.chemical_classification, Genetics, food and beverages, Cell Biology, biology.organism_classification, Amino acid, Protein Transport, chemistry, Soybeans, Functional divergence, Protein Binding, Subcellular Fractions
Abstract: Gene duplication provides resources for novel gene functions. Identification of the amino acids responsible for functional conservation and divergence of duplicated genes will strengthen our understanding of their evolutionary course. Here, we conducted a systemic functional investigation of phosphatidylethanolamine binding proteins (PEBPs) in soybean (Glycine max) and Arabidopsis thaliana. Our results demonstrated that after the ancestral duplication, the lineage of the common ancestor of the FLOWERING LOCUS T (FT) and TERMINAL FLOWER1 (TFL1) subfamilies functionally diverged from the MOTHER OF FT AND TFL1 (MFT) subfamily to activate flowering and repress flowering, respectively. They also underwent further specialization after subsequent duplications. Although the functional divergence increased with duplication age, we observed rapid functional divergence for a few pairs of young duplicates in soybean. Association analysis between amino acids and functional variations identified critical amino acid residues that led to functional differences in PEBP members. Using transgenic analysis, we validated a subset of these differences. We report clear experimental evidence for the functional evolution of the PEBPs in the MFT, FT, and TFL1 subfamilies, which predate the origin of angiosperms. Our results highlight the role of amino acid divergence in driving evolutionary novelty after duplication.
Published: 2015

249. BECN1s, a short splice variant of BECN1, functions in mitophagy

Author: Wenyu Wang, Qiao Wu, An Xu, Yide Mei, Mian Wu, Mengran Qiao, and Bing Cheng
Subjects: Mediator, Basic Research Papers, Mechanism (biology), Alternative splicing, Mitophagy, Autophagy, Regulator, Cell Biology, BECN1, Biology, Mitochondrion, Molecular Biology, Cell biology
Abstract: Mitochondria selective autophagy, known as mitophagy, plays a pivotal role in several biological processes, such as elimination of the damaged mitochondria, removal of the mitochondria from immature red blood cells and sperm. The defects in mitophagy are associated with a wide spectrum of human diseases, including neurodegenerative disease, aging, cardiac disease and autoimmune disease. However, the mechanism underlying mitophagy remains largely unclear. Here, we report the characterization of a novel splice variant of BECN1/Beclin 1, BECN1s, which is produced by an alternative splicing mechanism. BECN1s is primarily associated with the outer-membrane of mitochondria. Unlike unspliced BECN1, which is essential for nonselective macroautophagy induction, BECN1s is indispensible for mitochondria-selective autophagy. Furthermore, BECN1s plays an important role in starvation- and membrane depolarization-induced mitophagy. Taken together, our findings broaden the view of BECN1 as an important regulator in autophagy, and implicate BECN1s as a specific mitophagy mediator.
Published: 2015
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250. Truncated RIP3 (tRIP3) acts upstream of FADD to induce apoptosis in the human hepatocellular carcinoma cell line QGY-7703

Author: Shanshan Feng, Yonghui Yang, Li Ma, and Mian Wu
Subjects: Programmed cell death, Carcinoma, Hepatocellular, Fas-Associated Death Domain Protein, Molecular Sequence Data, Biophysics, Apoptosis, Biochemistry, Serine, Leucine, Cell Line, Tumor, Humans, Amino Acid Sequence, FADD, Amino Acids, Molecular Biology, Adaptor Proteins, Signal Transducing, Death domain, Inhibitor of apoptosis domain, Sequence Homology, Amino Acid, biology, Kinase, Cell Biology, Molecular biology, Receptor-Interacting Protein Serine-Threonine Kinases, biology.protein, Signal transduction, Protein Kinases, Sequence Alignment, Signal Transduction
Abstract: RIP3 (receptor-interacting protein 3) is a serine/threonine kinase that promotes apoptosis in various cell types. The C-terminal domain of RIP3 is critical for its apoptosis induction. In this study, we showed that a truncated form of RIP3 (tRIP3) containing only the unique C-terminal region (aa 224-518) induced significant apoptosis in human hepatocellular carcinoma cells QGY-7703. A FADD-dominant negative (FADD-DN) was shown to significantly block apoptosis induced by tRIP3. In contrast, the RIP3 dominant negative (RIP3-DN) was found unable to block FADD-induced apoptosis. Thus, we conclude that tRIP3 may function upstream of FADD to induce apoptosis in TNFR-1 signaling pathway. Additionally, sequence alignments of RIP3 with other death domain (DD)-containing proteins revealed that amino acids Leu 477 and Leu 488 in RIP3 are highly conserved, nonetheless, neither mutational change at Leu 477 nor at Leu 488 confers obvious effect on cell death, indicating that these two amino acids might not be critical for its pro-apoptotic activity as expected.
Published: 2006

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