Cell Death & Disease最新文献

{"title":"MAP3K13-232aa encoded by circMAP3K13 enhances cisplatin-induced pyroptosis by directly binding to IKKα in gastric adenocarcinoma.","authors":"Kaining Du, Xiaojing Zhang, Ying Qin, Huizhen Ma, Chuhan Bing, Shiqi Deng, Yang Chen, Jiequan Qin, Shanshan Chang, Siyu Xiao, Lehua Peng, Xiaoya Xie, Xianling Feng, Xianli Fu, Yanjie Wei, Xinmin Fan, Hassan Ashktorab, Duane Smoot, Zhe Jin, Yin Peng","doi":"10.1038/s41419-025-07991-5","DOIUrl":"10.1038/s41419-025-07991-5","url":null,"abstract":"<p><p>Gastric cancer (GC) is one of the most common and lethal malignancies in developing countries, with particularly high prevalence in China. Circular RNAs (circRNAs) have garnered increasing attention for their roles in disease pathogenesis. While circRNAs can be translated, there have been few investigations into the biological functions of \"translatable circRNAs\" in the initiation and progression of gastric adenocarcinoma. In this study, we identified a circRNA, circMAP3K13, which inhibits the proliferation and migration of GC cells. CircMAP3K13 was found to encode a previously unreported 26 kDa protein, designated MAP3K13-232aa. Mechanistically, MAP3K13-232aa binds directly to the kinase domain of IKKα and enhances its activity, thereby promoting NF-κB signaling. This activation leads to upregulation of NLRP3 and increased cisplatin-induced pyroptosis in GC cells. Moreover, MAP3K13-232aa enhances pyroptosis and reduces tumorigenicity and metastasis in vivo. Taken together, both circMAP3K13 and its encoded protein MAP3K13-232aa represent potential therapeutic targets in GC.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"667"},"PeriodicalIF":9.6,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12402440/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Long noncoding RNA H19 promotes the acquisition of a mesenchymal-like invasive phenotype in mesothelial primary cells through an HDAC1-mediated WT1/Sp1 switch.","authors":"Giulio Bontempi, Federica Michetti, Michela Terri, Cecilia Battistelli, Alice Conigliaro, Sabrina Garbo, Claudia Montaldo, Sergio Valente, Clemens Zwergel, Antonello Mai, Azadeh Nahavandi Araghi, Alessandro Domenici, Paolo Menè, Marco Tripodi, Raffaele Strippoli","doi":"10.1038/s41419-025-07956-8","DOIUrl":"https://doi.org/10.1038/s41419-025-07956-8","url":null,"abstract":"<p><p>Peritoneal fibrosis is a pathological alteration of the peritoneal membrane occurring in pro-inflammatory conditions, including peritoneal dialysis (PD), a renal replacement therapy. Characteristic of this process is the acquisition of invasive/pro-fibrotic abilities by mesothelial cells (MCs) through induction of mesothelial to mesenchymal transition (MMT), a cell-specific form of EMT. Long noncoding (lnc) RNAs act as major players in physiologic regulatory circuitries of the cell. While LncRNA-H19 (lncH19), one of the first lncRNAs identified, has been broadly studied in tumorigenesis, its role in peritoneum fibrotic diseases has been scarcely addressed so far. Aim of this study was to investigate the role of H19 in the acquisition of a mesenchymal-like phenotype in primary fibrotic MCs from PD patients, and to elucidate epigenetic mechanisms controlling its expression. Genetic silencing/ectopic expression experiments revealed that H19 promoted the expression of MMT markers while downregulating the epithelial marker E-Cadherin, and favored MC directed migration and invasion on a collagen matrix. Silencing of three main H19 isoforms revealed a synergistic activity in the induction of a mesenchymal phenotype. Treatment with MS-275, an HDAC1-3 specific inhibitor previously known to promote MMT reversal, as well as HDAC1 genetic silencing, downregulated lncRNA H19 expression. Bioinformatic analysis revealed a binding sequence of Wilm's Tumor Protein 1 (WT1), the master gene of mesothelial differentiation, on the H19 promoter at an area with multiple acetylation peaks partially overlapping the binding site of Specificity protein 1 (Sp1), another transcription factor active in cellular plasticity regulation. Genetic silencing and Chromatin Immunoprecipitation (ChIP) experiments demonstrated that HDAC1 inhibition promotes a switch between WT1 and Sp1 in H19 promoter occupancy, favoring an inhibitory effect of WT1 on H19 expression and the reversal towards an epithelial-like phenotype. Overall, we discovered an HDAC1-WT1/Sp1-H19 axis potentially relevant to the design of new therapies aimed at counteracting peritoneal fibrosis.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"663"},"PeriodicalIF":9.6,"publicationDate":"2025-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12398590/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944324","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"WEE1 inhibitor exerts synergistic effect with KRAS G12C inhibitor via MYBL2-RRM2 axis in KRAS^G12C-mutant lung cancer.","authors":"Chao Zhou, Yuqing Liu, Hongyu Liu, Jun Lu, Bo Zhang, Liang Zhu, Shuyuan Wang, Huimin Lei, Baohui Han","doi":"10.1038/s41419-025-07992-4","DOIUrl":"10.1038/s41419-025-07992-4","url":null,"abstract":"<p><p>The clinical effect of KRAS G12C inhibitors (G12Ci) as monotherapy is poor, prompting the development of combination treatment strategies. Here, we demonstrate that the WEE1 kinase inhibitor (WEE1i), Adavosertib, can sensitize the effect of G12Ci through the MYBL2-RRM2 axis, which is associated with poor prognosis in lung cancer. Overexpressing the MYBL2-RRM2 axis or supplementing the products of the RRM2 enzyme, dNTPs/dNs, can partially reverse this synergistic inhibitory effect. We also observed marked effects of the combination therapy in tumor xenografts models. Collectively, these results uncover the WEE1 kinase inhibitors, some of which are available clinically, as effective enhancers for G12Ci therapy.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"661"},"PeriodicalIF":9.6,"publicationDate":"2025-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12398517/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944439","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transcriptional activation of PHKG2 by TP53 promotes ferroptosis through nuclear export of NRF2 in head and neck squamous cell carcinoma.","authors":"Yalian Yu, Meng Luan, Jian Zang, Le Luo, Tianyi Wang, Tianci Wang, Yan Wang, Hongbo Wang","doi":"10.1038/s41419-025-07985-3","DOIUrl":"10.1038/s41419-025-07985-3","url":null,"abstract":"<p><p>Head and neck squamous cell carcinoma (HNSCC) is a common malignancy with a poor prognosis despite multiple available treatments. Ferroptosis, an iron-dependent form of regulated cell death characterized by lipid peroxidation, has recently emerged as a promising strategy for cancer therapy, particularly in head and neck malignancies. However, its regulatory mechanisms remain largely unclear. In this study, we demonstrate that TP53 transcriptionally activates PHKG2, which promotes ferroptosis. PHKG2 enhances the activity of protein phosphatase 1 (PP1) by phosphorylating PPP1R3B, disrupting its interaction with PP1C. Activated PP1 dephosphorylates NRF2, promoting its nuclear export and suppressing GPX4 transcription, thereby enhancing ferroptosis sensitivity. Both in vitro and in vivo, PHKG2 overexpression significantly suppressed tumor growth and increased lipid peroxidation levels. These findings define a previously unrecognized TP53/PHKG2-PP1-NRF2 signaling axis in the regulation of ferroptosis in HNSCC and suggest a novel therapeutic target.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"662"},"PeriodicalIF":9.6,"publicationDate":"2025-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12398534/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944456","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting DDX3X suppresses progression of KRAS-driven lung cancer by disrupting antioxidative homeostasis and inducing ferroptosis.","authors":"Meijuan Dian, Liang Yun, Qingyu Meng, Songwen Lin, Ming Ji, Ying Zhou, Wenqian Liu, Zhuoying Yang, Yayan Zhao, Gaoyuan Li, Jianjun Jiang, Weichao Hao, Zhijie Chen, Zehao Zhou, Ruihao Zhang, Tianyuan Liu, Yujing He, Tianbao Yan, Haofei Wang, Shane J F Cronin, Josef M Penninger, Kaican Cai, Shuan Rao","doi":"10.1038/s41419-025-07980-8","DOIUrl":"10.1038/s41419-025-07980-8","url":null,"abstract":"<p><p>Approximately 30% of human cancers carry various RAS mutations, including KRAS, NRAS, and HRAS. Among these mutations, KRAS is the most prevalent isoform detected in lung cancer. While several small molecular inhibitors targeting specifically KRAS^G12C have been developed and tested clinically, alternative approaches are still necessary due to expected drug resistance. In this study, we present evidence that the loss of DDX3X significantly delays tumor progression in various KRAS-driven lung cancer models. Inhibition of DDX3X disrupts cysteine and glutathione metabolism, thereby inducing ferroptosis in lung cancer cells. This effect is primarily mediated by the downregulation of Cystathionine-β-synthase (CBS), the rate-limiting enzyme in cysteine generation. Mechanistically, DDX3X directly binds to the transcription factor JUND, which mediates the transcriptional regulation of METTL16, a key N⁶-methyladenosine methyltransferase, and subsequently regulates m⁶A modification and translation of CBS transcripts. This cascade induces hypermethylation and high expression of CBS, consequently triggering cysteine production and maintaining antioxidative homeostasis, which is essential for the survival of KRAS-driven lung cancer cells. Finally, we demonstrate that a newly developed DDX3X PROTAC degrader J10 efficiently delays lung cancer progression with multiple advantages compared to DDX3X small molecular inhibitor RK-33 and limited side effects. These findings unveil the potential of DDX3X as a valuable target for adjuvant therapies in managing KRAS-driven lung cancer.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"660"},"PeriodicalIF":9.6,"publicationDate":"2025-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12398621/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction: Macrophages downregulate NEDD9 to counteract S. Typhimurium- mediated FAK-AKT activation and lysosome inhibition.","authors":"Julia Fischer, Lisa Rusyn, Frederike Krus, Liudmila Lobastova, Marc Herb, Alexander Gluschko, Zahra Hejazi, Nina J Hos, Chiara Calabrese, Jannik Stemler, Petra Mayer, Ruth Hanssen, Sebastian J Theobald, Jörg Janne Vehreschild, Jonel Trebicka, Martin Krönke, Jochen W U Fries, Clara Lehmann, Phuong-Hien Nguyen, Jan Rybniker, Nirmal Robinson, Tamina Seeger-Nukpezah","doi":"10.1038/s41419-025-07919-z","DOIUrl":"https://doi.org/10.1038/s41419-025-07919-z","url":null,"abstract":"","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"658"},"PeriodicalIF":9.6,"publicationDate":"2025-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12397303/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Retrograde transport of neurotrophin receptor TrkB-FL induced by excitotoxicity regulates Golgi stability and is a target for stroke neuroprotection.","authors":"Gema María Esteban-Ortega, Elena Torres-Campos, Margarita Díaz-Guerra","doi":"10.1038/s41419-025-07990-6","DOIUrl":"https://doi.org/10.1038/s41419-025-07990-6","url":null,"abstract":"<p><p>Excitotoxicity, aberrant function of survival pathways dependent on brain-derived neurotrophic factor (BDNF), and disruption of the Golgi complex are shared pathological hallmarks in relevant neurological diseases, including stroke. However, the precise interdependence among these mechanisms is not completely defined, knowledge essential for developing neuroprotective strategies. For ischemic stroke, a leading cause of death, disability, and dementia, interfering with excitotoxicity-the major mechanism of neuronal death in the penumbra area-has shown promising results. We are exploring neuroprotection by promoting survival cascades dependent on the BDNF receptor, full-length tropomyosin-related kinase B (TrkB-FL), as these pathways become aberrant after excitotoxicity. We previously developed MTFL₄₅₇, a blood-brain barrier (BBB) permeable neuroprotective peptide containing a TrkB-FL sequence, which efficiently prevents excitotoxicity-induced receptor processing and preserves BDNF-dependent pathways in an ischemia model, where it decreases infarct size and improves neurological outcome. In this work, using cellular and animal models, we demonstrate that excitotoxicity-induced TrkB-FL downregulation is secondary to receptor endocytosis, interaction with the endosomal protein hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs), retrograde transport to the Golgi, and subsequent disruption of this organelle. Interestingly, peptide MTFL₄₅₇ interferes with the TrkB-FL/Hrs interaction and receptor trafficking-processes required for excitotoxic Golgi fragmentation and TrkB-FL cleavage-demonstrating a central role for TrkB-FL in controlling Golgi stability. These results suggest the potential for peptide MTFL₄₅₇ to preserve the function of this organelle and critical neuronal survival pathways in stroke and possibly other neurodegenerative diseases associated with excitotoxicity.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"659"},"PeriodicalIF":9.6,"publicationDate":"2025-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12397353/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944469","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"DJ-1 counteracts Caveolin-1-mediated necroptosis to inhibit epithelial barrier dysfunction in colitis.","authors":"Mengli Yu, Jie Zhang, Bingru Lin, Wei Zhu, Xin Song, Jiaqi Pan, Dingwu Li, Xinjue He, Jing Sun, Zhe Shen, Chaohui Yu","doi":"10.1038/s41419-025-07989-z","DOIUrl":"https://doi.org/10.1038/s41419-025-07989-z","url":null,"abstract":"<p><p>Caveolin-1 (CAV1), a pivotal protein implicated in endothelial cell-mediated angiogenesis, assumes an ambiguous role with elusive underlying mechanisms in the pathogenesis of inflammatory bowel disease (IBD). In this investigation, we delineated the involvement of CAV1 in murine models of dextran sulfate sodium (DSS)-induced colitis. CAV1 knockout mice manifested attenuated pathological and inflammatory damage to the epithelium, whereas mice overexpressing CAV1 exhibited contrasting outcomes. In vivo, the accumulation of epithelial CAV1 contributed to the disruption of the epithelial barrier by promoting necroptosis. Subsequent mechanistic analyses revealed that the colitis-protective protein DJ-1 regulated CAV1 through a proteasome-mediated protein degradation pathway. Utilizing necroptosis-modeled organoids from murine intestines and pharmacological inhibition of necroptosis, our findings demonstrated that the DJ-1/CAV1 pathway governed epithelial inflammation via necroptosis in the context of colitis. In summary, our research revealed that epithelial CAV1 aggravated necroptosis in experimental colitis, leading to impairment of the epithelial barrier, which was negatively regulated by DJ-1.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"657"},"PeriodicalIF":9.6,"publicationDate":"2025-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12394565/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944375","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"DCAF7 recruits USP2 to facilitate hepatocellular carcinoma progression by suppressing clockophagy-induced ferroptosis.","authors":"Honglv Jiang, Xiaohui Wang, Zhenhua Zhu, Cheng Song, Dan Li, Yixuan Yun, Li Hui, Leilei Bao, Darran P O'Connor, Jingjing Ma, Guoqiang Xu","doi":"10.1038/s41419-025-07977-3","DOIUrl":"https://doi.org/10.1038/s41419-025-07977-3","url":null,"abstract":"<p><p>DDB1- and CUL4-associated factor 7 (DCAF7) has recently been identified as a critical regulator of tumorigenesis and a potential modulator of ferroptosis. However, the precise function of DCAF7 in regulating the progression of hepatocellular carcinoma (HCC) ferroptosis remains elusive. In this study, we demonstrate that DCAF7 and the deubiquitinase USP2 are highly expressed in HCC. Genetic ablation of DCAF7 or pharmacological inhibition of USP2 sensitizes HCC to ferroptosis and inhibits HCC progression both in vitro and in vivo. Mechanistically, DCAF7 recruits USP2 to inhibit clockophagy (the selective autophagic degradation of core clock protein BMAL1 mediated through p62/SQSTM1) by reducing BMAL1 K63-linked polyubiquitination. Targeting either DCAF7 or USP2 triggers clockophagy-induced ferroptosis through the HIF1α-SLC7A11 axis in HCC cells. Collectively, our study establishes DCAF7 and USP2 as novel suppressors of clockophagy-induced ferroptosis and reveals the potential therapeutic targets for HCC treatment.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"654"},"PeriodicalIF":9.6,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12394690/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting the SYVN1-EGFR axis: a breakthrough strategy for TKI-resistant NSCLC.","authors":"Xinsheng Xie, Weilai Tong, Yue Xie, Haoxin Jiang, Alan Jiang, Junming Huang, Zhili Liu, Jingjing Yu","doi":"10.1038/s41419-025-07978-2","DOIUrl":"https://doi.org/10.1038/s41419-025-07978-2","url":null,"abstract":"<p><p>Non-small cell lung cancer (NSCLC) is the leading cause of cancer-related death. Currently, molecular targeted therapy remains a crucial approach to the treatment of NSCLC. However, the development of acquired drug resistance poses significant challenges for subsequent treatment. Identifying new therapeutic targets is of great significance for improving the prognosis of patients with NSCLC. Here, we verify synoviolin-1 (SYVN1) as a potential new therapeutic target for NSCLC. SYVN1 is highly expressed in NSCLC, and its upregulation is associated with poor prognosis. We show that the N-terminus (1-290 aa) of SYVN1 directly interacts with the intracellular domain of the epidermal growth factor receptor (EGFR) and activates EGFR signaling, promoting NSCLC growth in vitro and in vivo. Specifically, SYVN1 facilitates Lys 63-linked ubiquitination of EGFR and inhibits proteasome-mediated EGFR degradation. Moreover, we found that SYVN1 inhibits EGFR endocytosis, thereby increasing the amount of EGFR on the cell membrane. Furthermore, we confirmed that LS-102, an enzyme activity inhibitor of SYVN1, inhibits cell proliferation induced by SYVN1. Significantly, LS-102 in combination with the EGFR-TKI AZD9291 exhibits strong inhibitory effects on NSCLC growth and reverses the resistance of NSCLC to AZD9291. Together, our study demonstrates that the SYVN1-EGFR axis plays a critical role in NSCLC development and suggests that targeting the SYVN1-EGFR axis to destabilize EGFR may represent a putative therapeutic strategy for TKI-resistant NSCLC.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"655"},"PeriodicalIF":9.6,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12394631/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144944309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}