Autophagy最新文献

{"title":"PRKN dephosphorylation by PTEN-L couples mitophagy inhibition to GSDME pyroptosis suppression.","authors":"Chenghao Yan, Xu Liu, Xinyu Gong, Xiaofang Wu, Haodong Xu, Liming Wang","doi":"10.1080/15548627.2026.2751925","DOIUrl":"https://doi.org/10.1080/15548627.2026.2751925","url":null,"abstract":"<p><p>Mitochondrial damage is a potent trigger of inflammatory cell death; however, how damaged mitochondria transduce stress signals to initiate cell death execution, and how this process is finely regulated, remain incompletely understood. We recently identified that the PINK1-PRKN axis, activated upon mitochondrial depolarization, not only initiates mitophagy but also drives pyroptosis via the ubiquitination and degradation of MCL1, which in turn promotes BAX and BAK1 activation, leading to CASP3 activation and GSDME cleavage. PTEN-L functions as a negative regulator of this pathway by directly dephosphorylating PRKN, which concurrently suppresses both mitophagy and pyroptosis, thereby coupling organelle quality control to inflammatory cell death.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":""},"PeriodicalIF":14.3,"publicationDate":"2026-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149225452","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Golgi disassembly: a key process for autophagy-mediated regulation of oocyte spindle migration.","authors":"Jiaqi Zhang, Nan Wang, Xiaomeng Wang, Jie Qiao, Peng Yuan, Liying Yan","doi":"10.1080/15548627.2026.2747860","DOIUrl":"10.1080/15548627.2026.2747860","url":null,"abstract":"<p><p>Although the Golgi apparatus undergoes extensive disassembly during mitosis to ensure its equitable partitioning into two daughter cells, the extreme asymmetry of oocyte meiosis obviates this need, raising fundamental questions about the existence and necessity of Golgi disassembly in oocytes. Herein, we demonstrated the existence of a Golgi disassembly process during oocyte meiosis I, which peaked at germinal vesicle breakdown (GVBD) and was largely completed by metaphase II (MII). Strikingly, the vesiculation stage of Golgi disassembly exhibited a function divergent from mitosis by governing spindle cortical migration during metaphase I (MI), thereby ensuring oocyte polarity establishment. Moreover, we found that macroautophagy/autophagy negatively regulated the vesiculation stage of Golgi disassembly: its hyperactivation suppressed vesiculation, whereas its inhibition conversely accelerated this process. Mechanistically, MIA2 and SFT2D2 were identified as key downstream effectors through which autophagy controlled Golgi vesiculation. MIA2 mediated autophagy-dependent regulation of Golgi dynamics through its two LIR motifs, thereby linking autophagic signaling to Golgi remodeling. Specifically, autophagy activation downregulated MIA2, thus inhibiting the ubiquitin-dependent degradation of SFT2D2, consequently suppressing Golgi vesiculation and spindle migration during oocyte meiosis I; conversely, autophagy inhibition accelerated these processes by increasing MIA2 to promote SFT2D2 degradation. These findings elucidate the key role of autophagy in regulating Golgi disassembly, thereby providing a new organelle-based perspective on how autophagy contributes to oocyte spindle migration. Furthermore, our work identifies a novel Golgi-dependent mechanism for oocyte polarity establishment and uncovers the divergent functions of Golgi remodeling across distinct division modes.<b>Abbreviations:</b> ACTB/β-actin: actin, beta; ATG5: autophagy related 5; Baf-A1: bafilomycin A₁; BFA: brefeldin A; Co-IP: co-immunoprecipitation; DAB: 3,3'-diaminobenzidine; F-actin: fibrous actin; GOLGA1/Golgin-97: golgin A1; GOLGA2/GM130: golgin A2; GV: germinal vesicle; GVBD: germinal vesicle breakdown; IEM: immunoelectron microscopy; IVM:<i>in vitro</i> maturation; LIR: LC3-interacting region; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MIA2: MIA SH3 domain ER export factor 2; MI: metaphase I; MII: metaphase II; PB: polar body; PLA: proximity ligation assay; RAB11A: RAB11A, member RAS oncogene family; SFT2D2: SFT2 domain containing 2; SQSTM1/p62: sequestosome 1; ST6GAL1: ST6 beta galactoside alpha 2, 6 sialyltransferase 1; TEM: transmission electron microscopy; TUBA/α-tubulin: tubulin, alpha; TUBG/γ-tubulin: tubulin, gamma.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-26"},"PeriodicalIF":14.3,"publicationDate":"2026-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149167298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A host-virus arms race over FAM134B in African swine fever virus infection.","authors":"Tao Wang, Rui Luo, Ruojia Huang, Yuan Sun, Hua-Ji Qiu","doi":"10.1080/15548627.2026.2751870","DOIUrl":"https://doi.org/10.1080/15548627.2026.2751870","url":null,"abstract":"<p><p>Although reticulophagy, the selective autophagy of the endoplasmic reticulum (ER), restricts several RNA viruses, whether this pathway constrains DNA virus infection remains unknown. Recently, we found that FAM134B (family with sequence similarity 134 member B), an ER-resident cargo receptor that mediates reticulophagy, restricts African swine fever virus (ASFV), a large cytoplasmic DNA virus, by targeting the major capsid proteins p72 and pA137R for lysosomal degradation, thereby blocking capsid assembly at perinuclear viral factories. ASFV counters this restriction through the virulence factor pMGF300-2 R encoded by the <i>MGF300-2 R</i> gene of ASFV, which binds to FAM134B, recruits LC3B (microtubule-associated protein 1 light chain 3 beta), an ATG8 (autophagy-related protein 8) family member, via the C-terminal LC3-interacting region (LIR) motif, and directs FAM134B into autophagic degradation. Deletion of the <i>MGF300-2 R</i> gene in the ASFV genome restores FAM134B abundance, reduces viral replication, and attenuates virulence in pigs. These findings establish reticulophagy as a previously unrecognized antiviral barrier against a large DNA virus and reveal a host-virus arms race centered on the reticulophagy receptor.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":""},"PeriodicalIF":14.3,"publicationDate":"2026-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149225533","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TBK1-mediated phosphorylation of WIPI2 links bacteria recognition to autophagosome formation in xenophagy.","authors":"Chuying Qian, Hongtao Zhang, Jin Li, Wei Wan, Wei Liu","doi":"10.1080/15548627.2026.2746965","DOIUrl":"10.1080/15548627.2026.2746965","url":null,"abstract":"<p><p>Xenophagy, a selective autophagy pathway, is a critical innate immune defense mechanism that targets pathogens for lysosomal degradation. However, the molecular mechanisms enabling autophagosomes to specifically recognize and engulf bacteria remain incompletely understood. Here, we identify WIPI2, a core component that drives autophagosome biogenesis, as a novel phosphorylation substrate of TBK1 during <i>Salmonella</i> Typhimurium infection. We demonstrate that TBK1 phosphorylates WIPI2 at Ser96, which enhances its interaction with ATG16L1 and its binding to PtdIns3P. Crucially, the recruitment of WIPI2 to intracellular bacteria is dependent on its interaction with ATG16L1, which is localized to the <i>Salmonella</i>-containing vacuole. Furthermore, TBK1-mediated phosphorylation of WIPI2 is required for efficient bacterial clearance. Collectively, our findings reveal a molecular mechanism whereby TBK1-mediated phosphorylation of WIPI2 directs localized phagophore expansion around invading bacteria, thereby bridging bacterial recognition with autophagosome assembly.<b>Abbreviations</b>: ATG: autophagy related; ATG5: autophagy related 5; ATG16L1: autophagy related 16 like 1; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; CFU: colony-forming units; GFP: green fluorescent protein; GST: glutathione S-transferase; IL6: interleukin 6; KO: knockout; LPS: lipopolysaccharides; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; OPTN: optineurin; PtdIns: phosphatidylinositol; PtdIns3P: phosphatidylinositol-3-phosphate; RB1CC1/FIP200: RB1 inducible coiled-coil 1; RFP: red fluorescent protein;<i>S</i>. Typhimurium:<i>Salmonella</i>Typhimurium; SCV:<i>Salmonella</i>Typhimurium-containing vacuole; SQSTM1/p62: sequestosome 1; TBK1/NAK: TANK binding kinase 1; ULK1: unc-51 like autophagy activating kinase 1; V-ATPase: vacuolar-type H⁺-translocating ATPase; WIPI1: WD repeat domain, phosphoinositide interacting 1; WIPI2: WD repeat domain, phosphoinositide interacting 2; WT: wild-type.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-15"},"PeriodicalIF":14.3,"publicationDate":"2026-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149139430","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Live visualization of dynamic autophagy processes in LC3 reporter mice using enhanced two-photon microscopy.","authors":"Saeed Bohlooli Darian, Jeongmin Oh, Chan-Gi Pack, Jun Ki Kim","doi":"10.1080/15548627.2026.2746966","DOIUrl":"10.1080/15548627.2026.2746966","url":null,"abstract":"<p><p>We developed a computationally enhanced intravital imaging framework for high-resolution analysis of macroautophagy/autophagy dynamics in vivo. By integrating two-photon microscopy with an optimized tissue stabilization method, motion artifacts were minimized, enabling real-time imaging of LC3-positive structures in the liver and skeletal muscle under physiological stress conditions, including starvation, ischemia, and ethanol exposure. Image quality was further improved using a trained denoising model and enhanced Super-Resolution Radial Fluctuations (eSRRF), enabling nanoscale visualization of autophagy-related compartments. To differentiate increased autophagosome formation from impaired degradation, autophagic flux was assessed via chloroquine-mediated lysosomal inhibition, enabling functional interpretation beyond static structural measurements. Together, this pipeline overcomes major technical limitations of intravital imaging and provides a robust framework for integrated structural and functional investigation of autophagy and related intracellular processes in vivo.<b>Abbreviations</b>: CQ: chloroquine; eSRRF: enhanced super-resolution radial fluctuations; EtOH: ethanol; GFP: green fluorescent protein; I/R: ischemia-reperfusion; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MTR: MitoTracker Red; rFRC: rolling Fourier ring correlation.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-11"},"PeriodicalIF":14.3,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149139413","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Innate immune signaling relays environmental cues to mitophagy for metabolic adaptation to obesity.","authors":"Courtney J Campbell, Scott A Soleimanpour","doi":"10.1080/15548627.2026.2747028","DOIUrl":"https://doi.org/10.1080/15548627.2026.2747028","url":null,"abstract":"<p><p>The mechanisms by which pancreatic β cells sense and communicate environmental cues to mitochondria to maintain insulin secretion remain poorly understood. We identified that β cells transduce metabolic stress, such as during obesity or glucolipotoxicity, through the innate immune signaling adaptor TRAF6 to regulate mitochondrial quality control. TRAF6 was dispensable for β-cell function at baseline yet was essential for glucose-stimulated insulin secretion in mouse or human β cells following nutrient excess. TRAF6 was required for the recruitment of components of both ubiquitin- and receptor-mediated mitophagy pathways to clear dysfunctional mitochondria following metabolic stress. Interestingly, concomitant loss of the ubiquitin-mediated mitophagy effector Parkin restored glucose homeostasis and mitophagy flux in TRAF6-deficient β cells by relieving impediments in receptor-mediated mitophagy. Together, we found that TRAF6 forms a molecular relay linking environmental signals to multiple mitophagy pathways to equip β cells with the means to adapt to metabolic demand and prevent diabetes.<b>Abbreviations</b>: ADP: adenosine diphosphate; ATP: adenosine triphosphate; BNIP3: BCL2 interacting protein 3; GSIS: glucose-stimulated insulin secretion; HFD: high-fat diet; MFN2: mitofusin 2; PRKN: parkin RBR E3 ubiquitin protein ligase; RNF41/NRDP1: ring finger protein 41; SQSTM1/p62: sequestosome 1; T2D: type 2 diabetes; TAX1BP1: Tax1 binding protein 1; TLR: Toll-like receptor; TRAF6: TNF receptor associated factor 6.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2026-10-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149186547","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Micromitophagy in plant spermatogenesis.","authors":"Xiaorong Huang, Bo Fu, Meng-Xiang Sun","doi":"10.1080/15548627.2026.2747857","DOIUrl":"https://doi.org/10.1080/15548627.2026.2747857","url":null,"abstract":"<p><p>Mitochondria of embryos in most plants and animals are inherited from the egg cell rather than the sperm cell, a phenomenon known as mitochondrial maternal inheritance. Nevertheless, how plants regulate paternal mitochondrial elimination (PME) has long remained a mystery. We discovered micromitophagy in higher plants and revealed that micromitophagy could serve as a specific mechanism underlying PME, which is triggered by fate determination of male germline (MG) cells. This process underpins maternal mitochondrial inheritance and normal early embryogenesis. Mechanistically, we demonstrate that the vacuole-localized ATG5 (autophagy-related protein 5) undergoes neofunctionalization and interacts with the mitochondrion-localized HSP90.2 (heat shock protein 90.2) to mediate paternal micromitophagy. Collectively, through interdisciplinary research on spermatogenesis, micromitophagy and mitochondrial inheritance, our work fills a long-standing gap in plant PME, and offers new insights into the functional divergence of autophagy-related genes and the adaptive evolution of autophagy.<b>Abbreviations</b>: PME, paternal mitochondrial elimination; 3-MA, 3-Methyladenine; ATG5, autophagy-related protein 5; HSP90.2, heat shock protein 90.2; MG, male germline; TEM, transmission electron microscopy; MVB, Multivesicular body.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2026-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149172283","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alphavirus Nsp3 protein hijacks receptor-mediated mitophagy via BNIP3L/NIX to dampen IFN response and promote viral replication.","authors":"Xiaoyi Qi, Yuan Zhao, Zhenbang Zhu, Wei Wen, Wenqiang Wang, Xiangdong Li","doi":"10.1080/15548627.2026.2747029","DOIUrl":"https://doi.org/10.1080/15548627.2026.2747029","url":null,"abstract":"<p><p>Alphaviruses encompass a variety of human and animal pathogens, such as getah virus (GETV), chikungunya virus (CHIKV), and Sindbis virus (SINV). Increasing evidence suggests that innate immunity plays an important role in host resistance to alphavirus infection, while alphaviruses have evolved multiple strategies to evade host antiviral innate immunity. Mitochondria, as key immune hubs, play a central role in the initiation of innate antiviral responses. It remains unclear whether alphaviruses inhibit innate immune responses by manipulating mitochondria. In this study, we found that GETV infection damages mitochondrial structure and function, as shown by mitochondrial membrane potential depolarization, reduction in mitochondrial numbers, and an imbalance in mitochondrial dynamics. GETV infection induces mitophagy in host cells and promotes viral replication. Nsp3 protein of alphaviruses (CHIKV, SINV, GETV) can directly trigger receptor-mediated mitophagy through its interaction with BNIP3L/NIX. Knockdown of <i>BNIP3L</i> could alleviate mitophagy caused by GETV infection. Mitophagy induced by alphavirus Nsp3 protein leads to degradation of MAVS which inhibits the IFN response and promotes viral replication. Collectively, our results demonstrated that alphaviruses Nsp3 serves as a novel virulence factor, inducing BNIP3L-mediated mitophagy to degrade MAVS and evade the host immune response.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":""},"PeriodicalIF":14.3,"publicationDate":"2026-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149139422","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evolutionarily conserved selective autophagy pathways.","authors":"András Jipa, Virág Vincze, Daniela Evdokimova, Dániel Dénes, Lilla Beatrix Péter, Zsombor Esküdt, Bence Csaba Béres, Gábor Juhász","doi":"10.1080/15548627.2026.2736925","DOIUrl":"https://doi.org/10.1080/15548627.2026.2736925","url":null,"abstract":"<p><p>Selective autophagy is a regulated process that ensures the specific recognition and lysosomal degradation of defined intracellular substrates, including damaged organelles, protein aggregates, and invading pathogens. Despite intense research interest, several mechanistic aspects of selective autophagy remain incompletely understood. Comparative analysis across different models offers a valuable framework for identifying evolutionarily conserved molecular components and regulatory principles. In this review, we provide a detailed overview of seven major evolutionarily conserved selective autophagy pathways: mitophagy, xenophagy, pexophagy, lysophagy, ER-phagy, Golgiphagy, and ribophagy, building on data from four widely used model organisms (mammals, <i>Drosophila melanogaster, Caenorhabditis elegans</i>, and <i>Saccharomyces cerevisiae</i>). We focus on the core molecular machinery including the modes of cargo recognition via already characterized and predicted selective receptors, and orchestration of cargo capture into forming autophagosomes.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-26"},"PeriodicalIF":14.3,"publicationDate":"2026-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149119728","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"RABC1 regulates ER-phagy to maintain ER homeostasis in plants.","authors":"Shuai Hu, Xiaohui Ma, Zhengjia Wang, Jinbo Shen","doi":"10.1080/15548627.2026.2739788","DOIUrl":"10.1080/15548627.2026.2739788","url":null,"abstract":"<p><p>Endoplasmic reticulum (ER)-phagy is an important ER quality-control pathway that selectively removes misfolded or unfolded proteins and damaged ER membranes through autophagic degradation in the vacuole. Recent studies have identified small guanosine triphosphatases (GTPases) as important regulators of the autophagy pathway. However, how they couple stress signals to ER-phagy remains poorly understood in plants. Our recent work demonstrated that RABC1 regulates ER-phagy under dithiothreitol (DTT)-, tunicamycin (TM)-, and heat-induced ER stress through interaction with the exocyst complex component SEC5A. Upon ER stress, green fluorescent protein (GFP)-RABC1 was recruited to the ATG8e-positive autophagosomes from the ER and Golgi in root cells, whereas autophagic flux and calnexin 1 (CNX1)-mRFP-tagged ER membranes turnover were impaired in the <i>rabc1</i> mutant. Together, our findings support a model in which RABC1 acts as a molecular switch that interacts with distinct effectors to regulate autophagy under different stress conditions.<b>Abbreviations:</b> RAB, ras-related in brain; ER, endoplasmic reticulum; GTPases, guanosine triphosphatases; GFP, green fluorescent protein; CNX1, calnexin 1; GDP, guanosine diphosphate; GTP, guanosine triphosphate; SAR1D, secretion associated ras related GTPase 1D; COPII, coat protein complex II; LDs, lipid droplets; DTT, dithiothreitol; TM, tunicamycin; TOR, target of rapamycin; ATG, autophagy-related; Rho, ras homology.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2026-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070643","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}