Cell Death and Differentiation最新文献

{"title":"m⁶A-mediated CABLES1 translation potentiates tumor radioresistance via facilitating nonhomologous end-joining repair.","authors":"Changzhi Li, Xianchao Tang, Zimi Zeng, Liqian Yang, Fang Cao, Haiyan Zhu, Liqing Zhu, Jie Shen, Xiaocui Bian, Libin Wang, Yang Liu, Fengbiao Mao, De Chang, Pengtao Jiao, Haiying Wang, Kailong Li","doi":"10.1038/s41418-026-01755-0","DOIUrl":"https://doi.org/10.1038/s41418-026-01755-0","url":null,"abstract":"<p><p>Radiotherapy is a mainstay of cancer treatment, yet its efficacy is still substantially restricted due to radioresistance. The mechanisms underlying radioresistance remain elusive, impeding drug development and therapeutics. Here, using a high-throughput random gene perturbation method based on piggyBac transposon, we screened and identified CABLES1, an adaptor protein, as a key regulator of tumor radioresistance. The function of CABLES1 in radioresistance was further validated in multiple human cell lines in vitro and a mouse xenograft model in vivo. High expression of CABLES1 is significantly correlated with radioresistance in cancer patients. Mechanistically, CABLES1 interacts with XRCC6/XRCC5 heterodimer and activates DNA-PKcs by promoting DNA-PK holoenzyme formation, thus facilitating the efficiency of nonhomologous end-joining (NHEJ) repair and radioresistance. Notably, YTHDF1 recognizes METTL14-deposited m⁶A modification on CABLES1 mRNA to enhance its translation in response to ionizing radiation (IR), thereby sustaining the elevation of NHEJ repair capacity and radioresistance. Through high-throughput screening of a small molecule library, we showed that theaflavin 3,3'-digallate (TF-3) specifically disrupts the CABLES1-XRCC6 interaction, thereby sensitizing cancer cells to radiotherapy. Together, our study unveils the molecular mechanism by which CABLES1 potentiates tumor radioresistance, providing a novel synthetic lethal strategy for targeting cancer.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147855966","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"GET3 regulates apoptosis via tail-anchoring of MCL1.","authors":"Chun Yin Yu, Mingxuan Du, Tsz Kwan Yeung, Randy Yat Choi Poon","doi":"10.1038/s41418-026-01752-3","DOIUrl":"https://doi.org/10.1038/s41418-026-01752-3","url":null,"abstract":"<p><p>The BCL2-like protein MCL1 plays pivotal roles in apoptosis and non-apoptotic functions. While many BCL2 family members are predicted to be tail-anchored (TA) proteins, direct evidence for MCL1's membrane targeting via the GET pathway, a major pathway for membrane insertion of TA proteins, has been lacking. Using degron-mediated depletion of GET3 (ASNA1/TRC40) in human cell lines, we uncovered a role of GET3 in regulating apoptosis. Depleting GET3 induced a slowdown of the cell cycle in HeLa and non-cancerous RPE1 cells. However, GET3 deficiency induced a more pronounced toxicity in HeLa cells, marked by enhanced apoptosis and reduced clonogenic survival. Notably, MCL1 expression diminished upon GET3 depletion and increased with GET3 overexpression, suggesting that MCL1 may be a TA-containing cargo of GET3. Moreover, we observed a direct interaction between GET3 and MCL1 via the C-terminal hydrophobic tail. Functionally, GET3 depletion enhanced apoptosis triggered by pharmaceutical inhibition of MCL1. Furthermore, GET3 deficiency promoted MCL1 downregulation and accelerated apoptosis during prolonged mitotic arrest. These findings underscore the importance of the GET pathway in regulating apoptosis and MCL1's tail-anchoring.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834158","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"USP4 modulates ZBP1 ubiquitination to regulate microglial PANoptosis and functional outcomes following traumatic brain injury.","authors":"Feng Shuang, Nan Li, Tianwei Guo, Danfeng Zhang, Hang Zhu, Xin Jin, XiaoLin Qu, Ruting Wei, Hui Luo, Chao Lin","doi":"10.1038/s41418-026-01749-y","DOIUrl":"https://doi.org/10.1038/s41418-026-01749-y","url":null,"abstract":"<p><p>Secondary damage in traumatic brain injury (TBI) is characterized by the abnormal release of damage-associated molecular patterns and excessive production of pro-inflammatory cytokines. Neuroinflammation is a hallmark of TBI. However, the mechanisms through which immune cells contribute to cognitive deficits and secondary inflammatory pathology remain poorly understood. In this study, we found that ZBP1-mediated microglial PANoptosis, which is a distinct form of innate immune-driven inflammatory cell death, is triggered following TBI. We further determined that microglial PANoptosis is induced by the synergistic action of heme and TNF-α. Mechanistically, we identified USP4 as a critical deubiquitinase for ZBP1 in microglia. USP4 was found to interact with, deubiquitinate, and stabilize ZBP1. Notably, AKT-mediated phosphorylation was found to be essential for maintaining USP4 protein stability. Pharmacological inhibition of USP4 using Vialinin A led to ZBP1 degradation, reduced microglial PANoptosis, and the amelioration of TBI-related functional deficits. Moreover, USP4 expression levels were found to be negatively correlated with prognosis patients with severe TBI. Collectively, our findings highlight a crucial role for USP4 in facilitating ZBP1-mediated inflammasome activation, microglial death, and cognitive impairment post-TBI, underscoring its potential as a therapeutic target.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834256","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The RNA binding protein LIN28A mediates chromatin dynamics during neuronal differentiation.","authors":"Silvia Piscitelli, Emanuela Cascone, Chiara D'Ambrosio, Giuseppina Divisato, Emilia Giannino, Laura De Lisio, Guido Leoni, Daniel D'Andrea, Danilo Swann Matassa, Chiara Lanzuolo, Valentina Rosti, Maria Chiara Zizolfi, Monica Matuozzo, Emanuele di Patrizio Soldateschi, Paolo Maiuri, Andrea Scaloni, Fabiana Passaro, Silvia Parisi","doi":"10.1038/s41418-026-01753-2","DOIUrl":"https://doi.org/10.1038/s41418-026-01753-2","url":null,"abstract":"<p><p>The transition of embryonic stem cells (ESCs) from a pluripotent state to lineage commitment is governed by complex regulatory mechanisms, including chromatin remodeling, as well as transcriptional and post-transcriptional processes. Recent studies have emphasized the interplay between these mechanisms, revealing intricate, multilayered regulatory networks that require further elucidation. In this study, we reveal a new connection between the RNA-binding protein LIN28A and the epigenetic regulation of ESC differentiation. LIN28A is upregulated during the early stages of neural commitment and undergoes a shift in subcellular localization from the nucleus to the cytoplasm upon differentiation. Generation and analysis of Lin28a knockout (KO) ESCs revealed that, although these cells can self-renew, they exhibit a pronounced defect in differentiating into neural precursors. However, mesodermal and endodermal differentiation proceeds normally in Lin28a KO cells, suggesting a neuronal-specific function for LIN28A. Proteomic analyses revealed a dynamic, context-dependent LIN28A interactome, with distinct sets of putative interacting partners in ESCs compared to those in differentiating cells. Among the ESC-specific putative interactors, we validated an RNA-dependent association of LIN28A with components of Polycomb Repressive Complex 2 (PRC2), a key chromatin-modifying complex that deposits the repressive histone modification H3K27me3. Chromatin immunoprecipitation followed by sequencing (ChIP-seq) demonstrated that loss of LIN28A results in persistent PRC2 occupancy at the promoters of developmental genes, accompanied by partial uncoupling between PRC2 binding and H3K27me3 deposition. Lin28a KO causes differentiation defects that are not rescued by pharmacological inhibition of PRC2 enzymatic activity, suggesting that LIN28A regulates PRC2 chromatin dynamics independently of H3K27me3 deposition. Furthermore, we identified an interaction between LIN28A and the long non-coding RNA Neat1, which may serve as a scaffold facilitating PRC2 eviction from chromatin. Taken together, our findings reveal a previously unrecognized role for LIN28A in regulating PRC2-mediated chromatin dynamics and underscore its importance in epigenetic control of neuronal differentiation.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transcriptional and ubiquitinative suppression of macrophage CST3 disrupts colonic homeostasis through defective efferocytosis.","authors":"Honggang Wang, Chenyang Jiao, Hailin Xing, Chao Cheng, Shaoqi Cheng, Wenliang Jiang, Ziwei Xu, Jianbo Yang, Jing Sun, Jie Zhao","doi":"10.1038/s41418-026-01750-5","DOIUrl":"https://doi.org/10.1038/s41418-026-01750-5","url":null,"abstract":"<p><p>To elucidate the role and regulatory mechanisms of macrophage-derived cystatin C (CST3) in Crohn's disease (CD), focusing on colonic inflammation, macrophage-epithelial interactions, and barrier dysfunction. Colonic samples from CD patients, including inflamed and non-inflamed regions, were subjected to scRNA-seq. In vitro macrophage-epithelial co-culture models and untargeted metabolomics were employed, and the findings were validated using macrophage-specific CST3 knockout (KO) and overexpression mice under TNBS-induced and IL-10 KO colitis conditions. Mechanistic investigations included Co-IP, ChIP-qPCR, ubiquitination assays, rescue experiments, and functional analyses of efferocytosis, macrophage polarization, and barrier integrity. CST3 expression was considerably reduced in macrophages from inflamed CD tissues through suppressor of SMAD5-dependent transcriptional repression and MYCBP2-mediated K48-linked ubiquitination and degradation. Loss of CST3 impaired efferocytosis and M2 polarization by inhibiting the ACVR1C/TGF-β/SMAD pathway. CST3 deficiency also disrupted intestinal epithelial proliferation, compromised barrier function, and increased apoptosis via enhanced NAMPT-INSR signaling and accumulation of the inflammatory cytokines. In mice, macrophage-specific CST3 deletion exacerbated colitis, whereas its overexpression alleviated inflammation and restored epithelial integrity. These findings establish macrophage CST3 as a key regulator of immune-metabolic-epithelial crosstalk in CD, and indicate that restoring CST3 function or targeting its regulatory axis may represent a novel therapeutic strategy for CD.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ypel5 preserves female fertility by regulating folliculogenesis and oocyte maturation.","authors":"Ling Ding, Qianying Guo, Yao Li, Fanqing Xu, Qiang Liu, Shaogang Qin, Ying Kuo, Jie Qiao, Peng Yuan, Liying Yan","doi":"10.1038/s41418-026-01744-3","DOIUrl":"https://doi.org/10.1038/s41418-026-01744-3","url":null,"abstract":"<p><p>Maintaining the primordial follicle pool and precisely regulating folliculogenesis are critical for female fertility. Despite advances in understanding ovarian development, the molecular mechanisms safeguarding follicle survival and oocyte maturation remain incompletely defined. Here, we identify YPEL5 as an essential regulator of folliculogenesis and oocyte development. Using an oocyte-specific conditional knockout (cKO) mouse model, we demonstrate that Ypel5 deletion causes complete female infertility, characterized by accelerated depletion of the primordial follicle pool, defective antral follicle formation, and impaired oocyte maturation. Loss of Ypel5 results in increased DNA damage, disrupted mitochondrial homeostasis, elevated oxidative stress, and ultimately triggers apoptotic depletion of primordial follicle oocytes. Moreover, Ypel5-deficient oocytes exhibit severe abnormalities in spindle organization and mitochondrial distribution, culminating in defective oocyte maturation. Collectively, these findings establish YPEL5 as a critical regulator of follicle development and oocyte maturation, and provide mechanistic insights into the molecular basis of female infertility.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834251","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"NINJ1 ubiquitination by TRIM72 protects against plasma membrane rupture and AKI-CKD progression","authors":"Keng Ye, Siyi Lin, Caiming Chen, Zhimin Chen, Kongwen Lin, Guoping Li, Huabin Ma, Jianfeng Wu, Tak W. Mak, Li Chen, Yanfang Xu","doi":"10.1038/s41418-026-01746-1","DOIUrl":"https://doi.org/10.1038/s41418-026-01746-1","url":null,"abstract":"The progression of acute kidney injury (AKI) to chronic kidney disease (CKD) remains a major clinical challenge. It is primarily triggered by renal tubular epithelial cell (RTEC) death that leads to persistent sterile inflammation, maladaptive repair and irreversible renal fibrosis. A pivotal event in RTEC death is plasma membrane rupture (PMR), which leads to the release of Damage-Associated Molecular Patterns (DAMPs). In this study, we identified Tripartite Motif-Containing 72 (TRIM72) as a critical regulator of Ninjurin-1 (NINJ1), a key mediator of PMR. Using tubule-specific knockout mice (Ninj1fl/flKspcre and Hmgb1fl/flKspcre) in a folic acid-induced AKI-CKD model, together with in vitro RTEC and immune cell assays, we delineated the TRIM72-NINJ1-HMGB1 signaling axis. We found that TRIM72 functions as an E3 ubiquitin ligase that targets NINJ1 at lysine 111 for proteasomal degradation, thereby restraining NINJ1-mediated PMR. Loss of TRIM72 stabilized NINJ1, exacerbated RTEC membrane rupture, and amplified the release of HMGB1. The resulting HMGB1 release propagated inflammation by promoting both macrophage-myofibroblast transition (MMT) and neutrophil extracellular trap (NET) formation, two major drivers of renal fibrosis. Consistently, tubule-specific deletion of either Ninj1 or Hmgb1 markedly attenuated the progression from AKI to CKD. Together, these findings establish the TRIM72-NINJ1-HMGB1 cascade as a central molecular pathway dictating the fate of injured RTECs and highlight TRIM72 as a promising therapeutic target for halting the transition from AKI to CKD.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"4 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147751833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Endothelial USP2a-METTL16 loop potentiates IL-6 signaling via m6A-mediated IL-6R stabilization in pulmonary vascular remodeling","authors":"Hanqing Zhu, Ping Yuan, Xiangyang Wu, Yuxia Huang, Wentian Zhang, Xingxing Sun, Jianhua Xu, Tianran Zhou, Junfang Xu, Li Chen, Wenlan Yang, Jinming Liu, Haipeng Liu, Fenghou Gao, Jian Guo","doi":"10.1038/s41418-026-01747-0","DOIUrl":"https://doi.org/10.1038/s41418-026-01747-0","url":null,"abstract":"Dysfunction of vascular endothelial cells is recognized as a critical driver in pulmonary vascular remodeling of pulmonary hypertension (PH). Although interleukin-6 (IL-6) has been firmly established as an indispensable factor leading to pulmonary vascular remodeling, its downstream molecular mechanisms remain incompletely elucidated. Here, we discover that ubiquitin-specific protease 2a (USP2a) is upregulated in lung tissues of PH patients and preclinical PH models, and in IL-6-stimulated endothelial cells. Both the endothelial cell-specific Usp2a genetic deletion and the pharmacological inhibition of USP2a with the inhibitor ML364 alleviate experimental PH manifestations. Mechanistically, USP2a attenuates the degradation of methyltransferase-like 16 (METTL16) by deubiquitination. Notably, METTL16 reciprocally enhances USP2a expression via interactions with eIF3a and eIF3b in a methyltransferase activity-independent manner, establishing a self-reinforcing USP2a-METTL16 regulatory loop. Subsequent investigations reveal that METTL16 enhances N6-methyladenosine (m6A)-mediated IL-6 receptor (IL-6R) mRNA stabilization, thereby promoting the expression of IL-6R. This study demonstrates that endothelial USP2a-METTL16 loop potentiates IL-6 signaling via IL-6R and represents a promising therapeutic target for PH.\u0000\u0000The alternative text for this image may have been generated using AI.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"32 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147751834","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction: The tumor suppressor protein PML controls apoptosis induced by the HIV-1 envelope.","authors":"J-L Perfettini, R Nardacci, C Séror, M Bourouba, F Subra, L Gros, G Manic, A Amendola, P Masdehors, F Rosselli, D M Ojcius, C Auclair, H de Thé, M-L Gougeon, M Piacentini, G Kroemer","doi":"10.1038/s41418-026-01745-2","DOIUrl":"https://doi.org/10.1038/s41418-026-01745-2","url":null,"abstract":"","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2026-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147763492","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"FAAH initiates a positive feedback loop to promote lung adenocarcinoma progression through inhibition of ferroptosis","authors":"Xinyi He, Cheng Tang, Tongtong Jiang, Chaohao Yang, Xiang Zhang, Zhuan Ju, Jiuzhou Zhao, Renji Wei, Ting Wang, Yanlu Xiong, Lintao Jia, Xiao Zhang","doi":"10.1038/s41418-026-01742-5","DOIUrl":"https://doi.org/10.1038/s41418-026-01742-5","url":null,"abstract":"Ferroptosis represents an iron-dependent form of cell death characterized by accumulation of lipid peroxides. However, it is largely elusive how authentic lipid metabolites contribute to ferroptosis, and whether this is dysregulated in malignant cells due to metabolic rewiring. Here, we identify fatty acid amide hydrolase (FAAH) as a crucial ferroptosis regulator in lung adenocarcinoma (LUAD). FAAH is upregulated and correlated with poor prognosis of LUAD patients. FAAH overexpression inhibits ferroptosis, whereas FAAH knockdown robustly enhances ferroptosis of LUAD cells. Mechanistically, FAAH promotes the palmitoylation of STAT3 through converting N-palmitoylethanolamine to palmitic acid. Palmitoylated STAT3 undergoes cytomembrane translocation and phosphorylation by JAK2, and transcriptionally activates GPX4 to suppress ferroptosis. Concomitantly, activated STAT3 licenses FAAH transcription, thus forming a positive feedback loop in LUAD cells. FAAH targeting represses tumor growth and boosts the anti-tumor efficacy of cisplatin in vivo. These findings uncover a novel regulatory circuit of ferroptosis driven by a saturated fatty acid, and demonstrate the applicability of targeting FAAH to overcome ferroptosis resistance in LUAD therapy.\u0000\u0000The alternative text for this image may have been generated using AI.","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"68 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2026-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147709327","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}