Cell Death and Differentiation最新文献

{"title":"Chromatin-associated circRNA ciCRLF3(2) regulates cell differentiation blockage via activating non-homologous end joining–based DNA repair","authors":"Ke-Jia Pu, Xiao-Tong Chen, Shun-Xin Zhu, Yan An, Xin‑Yi Feng, Heng-Jing Huang, Cheng-Lin Zhou, Mei-Ying Ye, Yun-Chun Wei, Yi-Xuan Ma, Chen Fang, Nan Zhang, Dan Wang, Bin-Rong Han, Jun-Yi Lian, Tian-Qi Chen, Yu-Meng Sun, Yue-Qin Chen, Wen-Tao Wang","doi":"10.1038/s41418-025-01574-9","DOIUrl":"https://doi.org/10.1038/s41418-025-01574-9","url":null,"abstract":"<p>DNA damage response (DDR) is a complicated network that responds to DNA lesions to prevent their accumulation; a defective DDR is one hallmark of cancer. Although targeting DDR pathways has been considered as a therapeutic approach, DDR inhibitors have also been reported ineffective for treating some low mutation burden cancers, such as Mixed-lineage leukemia (<i>MLL</i>)-rearranged (<i>MLL</i>-r) leukemia, a clinically fatal and refractory malignancy. Exploring the roles and mechanisms of DDR pathways in these low mutation burden cancers may help understand the chromatin biology and develop therapeutic strategies. Here, we identified a set of DDR-related chromatin-associated circular RNAs (cacircRNAs) that regulate DNA repair via the non-homologous end joining (NHEJ) pathway, which is vital for meeting the high DNA repair demands during the progression of <i>MLL</i>-r leukemia. Among these cacircRNAs, we identified ciCRLF3(2) as a previously unknown component of the NHEJ complex. We showed that ciCRLF3(2) recruits NHEJ regulators to DNA lesions, supporting abundant DNA repair in leukemia cells. ciCRLF3(2) abundance is abnormally upregulated in <i>MLL</i>-r leukemia and indicates a poor prognosis. Targeting ciCRLF3(2) suppressed NHEJ-mediated DNA repair, leading to DNA damage and broad anti-cancer effects in vitro and in vivo. A patient-derived xenograft model of <i>MLL</i>-r leukemia further indicated that ciCRLF3(2) depletion can decrease the leukemic burden. These findings demonstrate the function of cacircRNAs in DDR and chromatin biology and reveal a new avenue for developing strategies to treat low mutation burden cancers, such as <i>MLL</i>-r leukemia.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"12 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144995530","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":"Regulated cell death in fungi from a comparative immunology perspective","authors":"Asen Daskalov","doi":"10.1038/s41418-025-01570-z","DOIUrl":"https://doi.org/10.1038/s41418-025-01570-z","url":null,"abstract":"<p>The death of fungal cells has been studied in a variety of contexts including responses to antifungal drugs, during fungal developmental processes, in response to bacterial or mycoviral fungal pathogens, and during non-self-recognition between distinct strains of the same species (allorecognition). Some of the genetic determinants and molecular mechanisms of fungal cell death processes are now beginning to be understood in detail. Recent advances have uncovered fungal cell death machinery that shares ancestry with key actors of immune cell death in other eukaryotic and prokaryotic taxa. Transkingdom evolutionary links include fungal molecular sensors such as NOD-like receptors and signaling domains related to the TIR (Toll/interleukin-1 receptor) family, which are a staple of immunity throughout the tree of life. Moreover, cell death executioner proteins homologous to the pore-forming proteins that mediate mammalian <i>necroptosis</i> and <i>pyroptosis</i> are also abundant and widespread in fungi, particularly in Ascomycota. These findings prompt us to speculate on the possible origins of fungal cell death and to reconsider fungal innate immunity beyond allorecognition. This review discusses historical landmarks and major recent discoveries regarding the regulation of cell death processes in fungi through the lens of immunity.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"16 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144930456","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":"Uridine 5’-monophosphate (UMP) synthesis connects nucleotide metabolism to programmed cell death in C. elegans","authors":"Hang-Shiang Jiang, Hsiao-Fen Han, Cheng-Yi Chen, Kuan-Lun Hsu, Hung-Tsai Kan, Wan-Ying Lin, Mei-Hsuan Wu, Su-Yi Tsai, Jui-Ching Wu, Yi-Chun Wu","doi":"10.1038/s41418-025-01564-x","DOIUrl":"https://doi.org/10.1038/s41418-025-01564-x","url":null,"abstract":"<p>Nucleotide metabolism is essential for fundamental cellular functions such as growth, repair and proliferation. Emerging evidence suggests that metabolic pathways also influence programmed cell death (PCD), though the underlying mechanisms remain poorly understood. One model organism that has provided key insights into the regulation of PCD is <i>Caenorhabditis elegans</i> (<i>C. elegans</i>). In this nematode, apoptosis is often initiated through asymmetric cell division (ACD), a process that unequally distributes fate determinants between daughter cells to produce a larger surviving cell and a smaller cell destined for apoptosis. Here, we demonstrate that the simultaneous disruption of PCD and ACD leads to aberrant cell survival and the formation of extra hypodermal cells. Through a genetic screen in the <i>grp-1</i> ACD mutant background, we identified <i>pyr-1</i> as a regulator of PCD. <i>pyr-1</i> encodes the <i>C. elegans</i> carbamoyl-phosphate synthetase/aspartate transcarbamoylase/dihydroorotase (CAD) enzyme which catalyzes the rate-limiting step of de novo pyrimidine biosynthesis, producing uridine 5’-monophosphate (UMP). UMP is a critical metabolite for the synthesis of nucleotides, lipids and carbohydrates. Genetic analysis of UMP metabolic pathways, combined with exogenous nucleoside supplementation, confirms that UMP availability is essential for PYR-1-mediated PCD. Loss of <i>grp-1</i> induces cellular stress by disrupting fate determinant partitioning during ACD, whereas <i>pyr-1</i> mutations cause metabolic stress through UMP depletion. While both mutations independently activate autophagy, they function redundantly to upregulate the mitochondrial chaperone <i>hsp-6</i>. Knockdown of autophagy-related genes and <i>hsp-6</i> reveals that these pathways serve as compensatory mechanisms to protect against cell death in the <i>pyr-1; grp-1</i> double mutants. Collectively, our findings establish a direct link between metabolism and cell death, demonstrating how UMP availability and proper ACD coordinate apoptotic regulation and developmental outcomes. This study highlights the intricate interplay between metabolic homeostasis and PCD, providing new insights into the metabolic control of cell fate decisions.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"71 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144987449","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: TTK promotes mitophagy by regulating ULK1 phosphorylation and pre-mRNA splicing to inhibit mitochondrial apoptosis in bladder cancer.","authors":"Kang Chen, Jinyu Chen, Yukun Cong, Qingliu He, Chunyu Liu, Jiawei Chen, Haoran Li, Yunjie Ju, Liang Chen, Yarong Song, Yifei Xing","doi":"10.1038/s41418-025-01571-y","DOIUrl":"10.1038/s41418-025-01571-y","url":null,"abstract":"","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":15.4,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944218","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":"TAB2 controls a TAK1-independent cell death checkpoint at the level of TNFR1 complex II in the TNF pathway","authors":"Tom Delanghe, Mike Vadi, Annelore Haems, Lisa Wijns, Inge Bruggeman, Jon Huyghe, Dario Priem, Peter Vandenabeele, Mathieu JM Bertrand","doi":"10.1038/s41418-025-01568-7","DOIUrl":"https://doi.org/10.1038/s41418-025-01568-7","url":null,"abstract":"<p>Tumor necrosis factor (TNF) signaling determines the cell’s fate by promoting either survival or cell death via apoptosis, necroptosis or pyroptosis. Excessive or chronic cell death by TNF was shown to drive inflammatory pathologies, highlighting the importance of the mechanisms that normally block TNF cytotoxicity. This study investigates the role of TAB2, an adaptor protein traditionally linked to TAK1 activation in the TNF pathway. Contrary to expectations, TAB2 deficiency did not impair TAK1-dependent NF-κB or MAPK signaling, nor did it affect TAK1- and IKK-dependent inhibitory phosphorylation of RIPK1 in TNFR1 complex I, indicating that TAK1 remains functional in absence of TAB2. Still, TAB2 deficiency switches the TNF response from survival to apoptosis, demonstrating a crucial TAK1-independent pro-survival function of TAB2 in the pathway. This switch was absent in TAB3-deficient conditions, highlighting a non-redundant function of TAB2. We show that TAB2 is an integral part of TNFR1 complex II, limiting the abundance of the cytotoxic complex through direct association. The ubiquitin-binding NZF domain of TAB2 is critical for this function as cells expressing a NZF-deficient mutant switched the TNF response towards apoptosis, while not affecting TAK1-mediated signaling. Moreover, we found that the NZF domain of TAB2 also represses TNF-mediated necroptosis in conditions of Caspase-8 inhibition, thereby showing that TAB2 represses two different cell death modalities in the TNF pathway by limiting the abundance of two variations of the cytotoxic complex II. Together, our results reveal the existence of a new cell death checkpoint in the TNF pathway that is controlled by TAB2, through a mechanism independent of its established function in TAK1 recruitment and activation.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"30 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144923925","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":"Oestradiol-mediated ferroptosis defense shapes sex differences in acute kidney injury","authors":"Shengrong Wu, Li Zhuang, Boyi Gan","doi":"10.1038/s41418-025-01573-w","DOIUrl":"https://doi.org/10.1038/s41418-025-01573-w","url":null,"abstract":"<p>Acute kidney injury (AKI) is a leading cause of morbidity and mortality. For decades, clinical observations and epidemiological studies have indicated that premenopausal women are less prone to AKI than men and postmenopausal women [1, 2]. However, the biological basis for this sex bias has remained largely unknown. In a recent <i>Nature</i> paper [3], Tonnus et al. provide a compelling mechanistic explanation, demonstrating that female renal tubules are inherently resistant to ferroptosis—a predominant mode of cell death involved in ischemic AKI—through oestradiol-mediated protection against this cell death.</p><p>AKI often arises from acute tubular necrosis, a pathological condition characterized by spatially propagating cell death along the nephron; this propagation has been shown to be driven, at least in part, by ferroptosis, a form of lipid peroxidation–driven cell death exacerbated by iron overload and impaired antioxidant defenses [4, 5]. Notably, previous studies reported that female mice were substantially more resistant to AKI and renal tubular ferroptosis propagation than male counterparts [6]. Using ischemia–reperfusion injury (IRI) models and ex vivo assays with isolated renal tubules, Tonnus et al. confirmed these findings and showed that ferroptotic cell death waves were prominent in male tubules but virtually absent in females; furthermore, while ferroptosis inhibitors have shown a robust protective effect in male mice, their benefit in females has been modest [3]. This resistance could not be explained by differences in the expression of classical ferroptosis regulators such as glutathione peroxidase 4 (GPX4).</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"7 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144915580","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":"Fluorescent protein tagging of C. elegans core apoptosis pathway components reveals mitochondrial localization of CED-9 Bcl-2, CED-4 Apaf1 and CED-3 Caspase in non-apoptotic and apoptotic cells","authors":"Eric J. Lambie, Alan Greig, Barbara Conradt","doi":"10.1038/s41418-025-01567-8","DOIUrl":"https://doi.org/10.1038/s41418-025-01567-8","url":null,"abstract":"<p>We used CRISPR-Cas-mediated modification of the genomic loci for <i>C. elegans</i> genes <i>ced-9</i> Bcl-2, <i>ced-4</i> Apaf1 and <i>ced-3</i> Caspase to add the coding sequence for the mNeonGreen (mNG) fluorescent protein to the endogenous open reading frames. In each case, the addition of mNG caused little or no apparent alteration of gene function. We found that tagged versions of CED-9, CED-4 and CED-3 proteins colocalize with mitochondria in all cells of live mid-late stage embryos and are distributed along the entire length of mitochondria. However, CED-4 also exhibits localized puncta of ~4-fold enrichment, and these are preferentially oriented toward the nucleus. We do not observe any shift in the localization pattern of tagged CED-4 in cells that are committing to apoptosis during normal development. However, when <i>egl-1</i> BH3-only is overexpressed or <i>ced-9</i> removed by mutation, CED-4::mNG is no longer distributed along the entire length of mitochondria and instead becomes enriched in the bright puncta. Finally, localization of CED-3::mNG to mitochondria is independent of both CED-9 and CED-4. This study represents the first analysis of the distribution and sub-cellular localization of endogenous CED-9 Bcl-2, CED-4 Apaf1 and CED-3 Caspase proteins in live embryos. Our results impact the current model of apoptosis commitment in <i>C. elegans</i>.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"22 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144911221","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":"Large-scale transcriptomic analyses reveal downstream target genes of ZFY1 and ZFY2 transcription factors in male germ cells","authors":"Hayden Holmlund, Manon Coulée, Yasuhiro Yamauchi, Benazir Yarbabaeva, Muhammetnur Tekayev, Isabella R. Garcia, Olivier U. Feudijo, Alberto de la Iglesia, Lee Larcombe, Peter J. I. Ellis, Julie Cocquet, Monika A. Ward","doi":"10.1038/s41418-025-01569-6","DOIUrl":"https://doi.org/10.1038/s41418-025-01569-6","url":null,"abstract":"<p>The mouse zinc finger genes <i>Zfy1</i> and <i>Zfy2</i> are essential for male fertility. Recently, we produced <i>Zfy1</i> knock-out (KO), <i>Zfy2</i> KO, and <i>Zfy1/2</i> double-knock-out (<i>Zfy</i> DKO) mice, and found that <i>Zfy</i> DKO males were infertile. The mechanism by which ZFY contributes to reproduction remains unknown but based on predicted protein sequence and in vitro assays we hypothesize that it controls expression of genes essential for spermatogenesis. To identify which genes ZFY regulates, we performed comparative transcriptome analysis of sorted male germ cells at three different spermatogenesis stages from three <i>Zfy</i> KO models and control wild-type males. Significantly altered germ cell transcriptomes were identified with <i>Zfy2</i> KO and <i>Zfy</i> DKO. Analyses of differentially expressed genes supported that <i>Zfy</i> loss altered spermatogenesis, DNA packaging/chromatin organization, and apoptosis pathways. Alternative splicing was deregulated in <i>Zfy</i> KO models, affecting sperm function and chromatin regulation pathways. In support of in-silico findings, <i>Zfy</i> DKO males were shown to have impaired post-meiotic chromatin remodeling and sperm chromatin organization, functional sperm deficiencies, and increased germ cell apoptosis. ZFY regulation of apoptotic pathways was demonstrated also in transfected human cells. We conclude that <i>Zfy</i> is a critical regulator of meiosis and spermiogenesis in addition to its previously described function as a cell-cycle regulator.</p><figure></figure>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"28 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144906145","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":"A novel feedback loop between DYRK2 and USP28 regulates cancer homeostasis and DNA damage signaling","authors":"Lucía Suanes-Cobos, Irene Aguilera-Ventura, Miguel Torres-Ramos, Alejandra Serrano-Yubero, Claudia Moreno Fernández-Aliseda, Silvia Fernández, Martín Garrido-Rodríguez, Susana de la Luna, Cristian Prieto-Garcia, Markus E. Diefenbacher, Ernesto Mejías-Pérez, Marco A. Calzado","doi":"10.1038/s41418-025-01565-w","DOIUrl":"https://doi.org/10.1038/s41418-025-01565-w","url":null,"abstract":"<p>Posttranslational modifications, such as ubiquitination and phosphorylation, play pivotal roles in regulating protein stability in response to cellular stress. Dual-specificity tyrosine phosphorylation-regulated kinase 2 (DYRK2) and ubiquitin-specific peptidase 28 (USP28) are critical regulators of cell cycle progression, DNA damage response, and oncogenic signaling. However, their functional interplay remains largely unexplored. Here, we describe a novel bidirectional regulatory mechanism between DYRK2 and USP28 that integrates DNA damage response and ubiquitin-mediated protein degradation. We demonstrate that DYRK2 phosphorylates USP28, promoting its ubiquitination and proteasomal degradation in a kinase activity-independent manner, thereby contributing to the maintenance of oncogenic protein homeostasis. Conversely, USP28 functions as a deubiquitinase for DYRK2, stabilizing its protein levels and enhancing its kinase activity. Notably, we show that DYRK2 interacts and co-localizes with USP28, with the 521–541 DYRK2 region, particularly residue T525, playing a crucial role in USP28-mediated DYRK2 stabilization. Functionally, this reciprocal regulation modulates p53 signaling, influencing apoptotic responses to DNA damage. DYRK2-mediated phosphorylation of p53 at S46 is significantly reduced upon USP28 depletion, suggesting that USP28 facilitates DYRK2-dependent apoptosis. Additionally, our results highlight a complex regulatory axis involving USP28 and DYRK2, with implications for oncogenic cell death and genomic stability. Overall, our findings uncover a novel feedback loop in which DYRK2 and USP28 dynamically regulate each other to control proto-oncoprotein homeostasis and DNA damage signaling. This interplay offers potential therapeutic opportunities for targeting cancers with dysregulated ubiquitination and genomic instability.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"82 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144900397","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":"Bcl-2 modifying factor (Bmf): “a mysterious stranger” in the Bcl-2 family proteins","authors":"N. V. Pervushin, D. K. Nilov, B. Zhivotovsky, G. S. Kopeina","doi":"10.1038/s41418-025-01562-z","DOIUrl":"https://doi.org/10.1038/s41418-025-01562-z","url":null,"abstract":"<p>Members of the Bcl-2 family are essential regulators of cell fate. Some of them (proapoptotic) promote cell death, while others (antiapoptotic) support cell survival. Bcl-2 modifying factor (Bmf) is an understudied BH3-only protein of this family that is widely expressed in many normal and cancer tissues. Bmf’s proapoptotic activity is essential in physiological and pathological processes, including hematopoiesis, gametogenesis, diabetes, tumorigenesis, etc. However, Bmf has remained in the shadow of other BH3-only proteins for many years. This review aims to rectify this injustice and elucidate the multifaceted functions of Bmf, its regulation, and its significance in both normal and pathological contexts.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"31 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144900556","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}