Apoptosis最新文献

{"title":"SUCLG2 contributes to platinum resistance in lung adenocarcinoma through enhancing succinylation of GAC and glutamine metabolism","authors":"Zuorui Wang,&nbsp;Hui Wang,&nbsp;Lei Wang,&nbsp;Jiayuan Chen,&nbsp;Lei Jiang,&nbsp;Wenxin Deng,&nbsp;Jing Xu,&nbsp;Yaoguang Hua,&nbsp;Yifan Shi,&nbsp;Yi Yuan,&nbsp;Menglin Huang,&nbsp;Xiangpei Cui,&nbsp;Lanxi Bai,&nbsp;Defu Li,&nbsp;Bentong Yu,&nbsp;Qifan Hu","doi":"10.1007/s10495-026-02443-7","DOIUrl":"10.1007/s10495-026-02443-7","url":null,"abstract":"<div><p>Platinum-based drugs constitute first-line chemotherapy for lung adenocarcinoma (LUAD), yet resistance emerges in 50–70% of patients, representing a major clinical challenge. Synthetase GDP-forming subunit β (SUCLG2), the beta subunit of succinyl-CoA synthetase, is a key enzyme in the tricarboxylic acid (TCA) cycle. Using untargeted proteomic profiling, we identified SUCLG2 as a potential contributor of platinum resistance in LUAD. Further knockout of SUCLG2 significantly enhanced cellular sensitivity to platinum-based drugs. Mechanistically, using targeted metabolomics, we found that SUCLG2 conferred platinum resistance by promoting glutamine metabolism and facilitating the succinylation of glutaminase (GAC). This post‑translational modification enhanced GAC activity, thereby reducing ROS generation and suppressing apoptosis in LUAD cells. SUCLG2 was found to be highly expressed in both LUAD tissues and platinum-resistant cell lines. Consistent with cellular findings, animal experiments confirmed that elevated SUCLG2 expression critically contributes to platinum resistance in vivo. Our findings provide new insights into the molecular mechanisms underlying platinum resistance in LUAD and suggest novel therapeutic strategies.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149029674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"GLG1 in cancer-associated fibroblasts promotes bladder cancer growth while limiting tumor apoptosis","authors":"Jingpeng Liu,&nbsp;Zhongbao Zhou,&nbsp;Baining Zhang,&nbsp;Runze Liu,&nbsp;Yong Zhang","doi":"10.1007/s10495-026-02439-3","DOIUrl":"10.1007/s10495-026-02439-3","url":null,"abstract":"<div><p>Cancer-associated fibroblasts (CAFs) shape bladder cancer progression, but functionally relevant CAF-associated drivers remain insufficiently characterized. This study aimed to identify CAF-enriched genes with translational relevance and to determine whether GLG1 mediates tumor–stromal crosstalk in bladder cancer. Single-cell RNA sequencing from bladder cancer tissues was integrated with Mendelian randomization, Bayesian colocalization, correlation analyses, immunostaining of clinical specimens, CAF-conditioned medium assays, GLG1 knockdown/overexpression, TGF-β1/Smad2/3 assessment, and xenograft modeling. Single-cell profiling of nine bladder cancer samples retained 60,561 cells and identified fibroblast-enriched transcriptional programs. Among 960 fibroblast-enriched genes, Mendelian randomization identified 22 genes whose genetically predicted expression was associated with bladder cancer risk, and colocalization prioritized GLG1, HES4, and HSP90B1. GLG1 was selected for validation because it showed fibroblast-enriched expression, genetic support for bladder cancer association, and shared cis-eQTL/GWAS signals. GLG1 expression was higher in tumor tissues than in adjacent normal tissues, consistent with a stromal localization pattern, and GLG1 positivity was associated with tumor invasiveness. Tumor-derived TGF-β1/Smad2/3 signaling contributed to GLG1 upregulation in fibroblasts. CAF-conditioned medium enhanced EJ-1 cell viability, migration, and Matrigel invasion; these effects were weakened by GLG1 silencing and strengthened by GLG1 overexpression in CAFs. In xenografts, CAFs-shGLG1 reduced tumor growth and Ki-67 positivity and increased TUNEL-positive tumor cells relative to CAFs-shNC, whereas CAFs-OE-GLG1 showed the opposite Ki-67 and TUNEL staining pattern. CAF-associated GLG1 promotes bladder cancer cell viability, migration, Matrigel invasion, and xenograft growth while limiting tumor-cell apoptosis, likely by reinforcing tumor–stromal crosstalk. These findings support GLG1 as a stromal factor involved in bladder cancer progression and provide a basis for further evaluation of its biomarker potential and therapeutic relevance.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s10495-026-02439-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149029719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lactylation and regulated cell death: the substrate defines the outcome","authors":"Shanjie Luan","doi":"10.1007/s10495-026-02445-5","DOIUrl":"10.1007/s10495-026-02445-5","url":null,"abstract":"","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148982193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Drugging small-molecule compounds in autophagy-dependent cell death to overcome cancer therapy resistance","authors":"Zhiqi Peng,&nbsp;Xiong Pei,&nbsp;Ruohan Gao,&nbsp;Dongbo Wu,&nbsp;Bo Liu","doi":"10.1007/s10495-026-02437-5","DOIUrl":"10.1007/s10495-026-02437-5","url":null,"abstract":"<div><p>Cancer therapy resistance remains a major challenge linked to metabolic rewiring, stress adaptation, and defective cell death. Autophagy is a lysosome-dependent process that can either promote tumor survival under stress or contribute to autophagy-dependent cell death (ADCD). Protective autophagy supports resistance through metabolic adaptation, organelle quality control, immune evasion, and maintenance of cancer stemness, whereas excessive or dysregulated autophagy may trigger lethal self-digestion. Emerging studies show that small molecules can reprogram autophagy from a survival pathway into a cytotoxic process by targeting AMPK/mTOR/ULK1 signaling, stress-response pathways, lysosomal function, and selective autophagy networks such as mitophagy and ferritinophagy. Importantly, ADCD can bypass apoptosis resistance, eradicate drug-tolerant persister cells, and enhance therapeutic efficacy in refractory tumors. This review outlines a mechanistic framework linking autophagy plasticity to therapy resistance, discusses pharmacological strategies for inducing ADCD, and highlights autophagy-to-lethality conversion as a promising therapeutic paradigm for overcoming resistance in refractory cancers while identifying future directions for clinical translation and rational combination therapies.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148982163","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"GOLPH3-mediated sialylation of CXCR4 drives malignant progression and M2 macrophage polarization in colorectal cancer","authors":"Wangwu Liu,&nbsp;Yi Qiu,&nbsp;Ling Zeng,&nbsp;Yuze Wu,&nbsp;Jiabin Du,&nbsp;Lufeng Chen,&nbsp;Donglin Li,&nbsp;Chunxiao Wang,&nbsp;Zhongshi Hong,&nbsp;Bingchen Lin,&nbsp;Chengzhi Qiu","doi":"10.1007/s10495-026-02421-z","DOIUrl":"10.1007/s10495-026-02421-z","url":null,"abstract":"<div><p>Sialylation, a post-translational protein modification, correlates with tumor malignancy. This study investigates how GOLPH3 regulates CXCR4 sialylation in colorectal cancer (CRC) and its impact on cancer cell phenotypes. Predicted glycosylation sites on CXCR4 were identified using the NetNGlyc-1.0 tool. The GOLPH3-CXCR4 interaction and GOLPH3-sialyltransferase associations were bioinformatically predicted (BIOGRAD) and validated experimentally via co-immunoprecipitation (Co-IP). CXCR4 sialylation was assessed by immunoprecipitation (IP) and lectin blotting (LB). Immunohistochemical (IHC) assessment of protein expression levels of Ki-67, GOLPH3, and CD206 in tissues. Functional assays, including colony formation, flow cytometry, scratch, and Transwell assays, evaluated proliferation, apoptosis, migration, and invasion in CRC. A co-culture system, flow cytometry, and Enzyme-Linked Immunosorbent Assay (ELISA) were conducted to assess macrophage M2 polarization, and a xenograft tumor model was constructed for in vivo validation. GOLPH3 promotes the interaction between CXCR4 and its ligand CXCL12 by inducing sialylation at the 180th amino acid residue of CXCR4. This regulatory mechanism plays an important role in modulating macrophage function, which manifests as facilitating cell proliferation, migration and invasion, suppressing cellular apoptosis, and promoting M2-type macrophage polarization. Furthermore, N180 mutation assays offer direct experimental evidence to validate the causal relationship within this regulatory network. These findings reveal a GOLPH3-ST6GAL1 axis that enhances CXCR4 sialylation to drive CRC progression and an immunosuppressive microenvironment via CXCL12/CXCR4 signaling, suggesting a novel regulatory mechanism underlying glycosylation modification of this chemokine receptor.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148982196","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Berberine shows potential in mitigating PM2.5-induced breast cancer progression by inducing DNA damage and inhibiting error-prone DNA repair pathways","authors":"Anadi Bisht,&nbsp;Aishwarya Jaiswal,&nbsp;Rana P. Singh,&nbsp;Sagnik Dey,&nbsp;Ritu Kulshreshtha","doi":"10.1007/s10495-026-02423-x","DOIUrl":"10.1007/s10495-026-02423-x","url":null,"abstract":"<div><p>Breast cancer remains the most common cancer among women, with 2.3 million new cases reported globally in 2022. Alongside established risk factors such as age, family history, genetics, obesity, smoking, and alcohol, exposure to fine particulate matter (PM_2.5) has recently emerged as an environmental contributor. This risk is especially concerning for low- and middle-income countries (LMICs), where both PM_2.5 exposure and cancer burden are disproportionately high; however, mechanistic studies from these regions remain limited. To address this gap and develop mitigation strategies, we investigated the oncogenic potential of water-soluble PM_2.5 collected from ambient air on breast cancer and evaluated the potential role of nutraceuticals in mitigating these effects. PM_2.5 exposure increased proliferation, migration, and ROS generation, while promoting the formation of multinucleated giant cells, leading to genomic instability. Berberine, a natural alkaloid, countered these effects by increasing DNA damage and exploiting tumor-specific genomic vulnerabilities through disruption of DNA damage response and repair networks, thereby promoting programmed cell death. Transcriptomic profiling of Delhi PM_2.5-treated MCF7 cells revealed a Delhi PM_2.5-associated carcinogenic gene signature enriched in MAPK signalling, reactive oxygen species, metabolic, lysosomal, and ribosomal pathways. We also found that several genes, including <i>BIRC5</i>,<i> WSB1</i>, and <i>RCC1</i>, within this PM_2.5-induced gene signature were dysregulated in breast cancer patients and were inversely regulated by berberine treatment, suggesting that berberine counteracts the transcriptional effects of PM_2.5. Our findings highlight ambient PM_2.₅ exposure as a driver of breast cancer progression and identify berberine as a promising candidate in mitigating PM_2.5 effects; however, thorough preclinical and clinical validations are warranted.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148927800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Activating a novel cell death pathway to target PI-resistant multiple myeloma and enhance immunogenic cell death","authors":"Xinyun Zhang,&nbsp;Zhiming Wang,&nbsp;Yilei Shi,&nbsp;Qi Li,&nbsp;Si Chen,&nbsp;Lexin He,&nbsp;Yali Chai,&nbsp;Hao Xu,&nbsp;Yuchen Zhang,&nbsp;Meifang Zhao,&nbsp;Wenzhuo Zhuang,&nbsp;Bingzong Li","doi":"10.1007/s10495-026-02426-8","DOIUrl":"10.1007/s10495-026-02426-8","url":null,"abstract":"<div><p>Resistance to proteasome inhibitors (PIs) and inadequate engagement of anti-tumor immunity remain major barriers to effective treatment of multiple myeloma (MM). Here, we identified anwulignan, a bioactive natural product, as a translationally promising agent that retains activity in PI-resistant MM cells and promotes anti-myeloma immune responses. Anwulignan demonstrated potent cytotoxic activity against MM cells and exhibited strong synergy with proteasome inhibitors both in vitro and in vivo. In mouse MM models, anwulignan significantly suppressed tumor growth while maintaining favorable tolerability and safety profiles. Mechanistically, nucleophosmin 1 (NPM1) has been identified as a direct molecular target of anwulignan. Elevated NPM1 expression correlates with poor clinical outcomes in MM, and its inhibition by anwulignan induces cell cycle arrest and apoptosis. In addition to its tumor-intrinsic cytotoxic effects, anwulignan activated the caspase-1–dependent gasdermin D (GSDMD) pyroptosis pathway, thereby inducing immunogenic cell death. Genetic silencing of GSDMD markedly impaired anwulignan-mediated tumor suppression in vitro and in vivo, highlighting pyroptosis as a critical effector mechanism. In immunocompetent syngeneic MM models, anwulignan treatment increased bone marrow and splenic T-cell proportions and achieved superior tumor control compared with GSDMD-deficient tumors. Collectively, these findings establish anwulignan as a dual-function therapeutic that directly targets MM cell survival while simultaneously promoting anti-tumor immunity through pyroptosis-driven immunogenic cell death. This study provides a strong translational rationale for leveraging natural products as immune-engaging strategies to target drug-resistant multiple myeloma and improve therapeutic outcomes.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 10","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148903566","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lactate-associated H3K18la upregulates RNF166 to promote immune evasion in hepatocellular carcinoma by remodeling c-Jun ubiquitination","authors":"Bingyi Ren,&nbsp;Yichen Yang,&nbsp;Kai Sheng,&nbsp;Qiuyu Mu,&nbsp;Zhiyuan Bai,&nbsp;Min Tian,&nbsp;Yang Ren,&nbsp;Yi Lv,&nbsp;Kang Liu","doi":"10.1007/s10495-026-02435-7","DOIUrl":"10.1007/s10495-026-02435-7","url":null,"abstract":"<div><p>Hepatocellular carcinoma (HCC) is a leading cause of cancer-related mortality, and PD-L1-mediated immune evasion is a major mechanism of tumor immune suppression and an important target of immune checkpoint blockade. Here, we identified RNF166 as an E3 ubiquitin ligase that promotes immune evasion in HCC. RNF166 expression was upregulated in HCC tissues and correlated with PD-L1 levels, whereas RNF166 did not directly affect the proliferation or apoptosis of HCC cells. In immunocompetent mouse models, RNF166 overexpression accelerated tumor growth and suppressed CD8 + T-cell infiltration and cytotoxic function, while these effects were dependent on PD-L1 signaling and were attenuated in immunodeficient settings. Mechanistically, RNF166 physically interacted with c-Jun and promoted K63-linked ubiquitination of c-Jun at K50/K56, which was associated with reduced K48-linked ubiquitination and enhanced c-Jun stability. Stabilized c-Jun bound to the PD-L1 promoter and promoted PD-L1 transcription, thereby linking RNF166-mediated c-Jun stabilization to tumor immune suppression. Upstream, lactate accumulation increased H3K18la enrichment at the RNF166 promoter and contributed to RNF166 transcriptional upregulation. Therapeutically, pharmacological inhibition of c-Jun with T-5224 enhanced the antitumor effect of anti-PD-L1 blockade. Collectively, our findings delineate a lactate-H3K18la-RNF166-c-Jun-PD-L1 axis that promotes immune evasion in HCC and suggest that targeting RNF166 or the RNF166-c-Jun axis may improve PD-1/PD-L1-based immunotherapy.</p></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 9","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13547187/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148900036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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 to: Photobiomodulation therapy moderates cancer cachexia‑associated muscle wasting through activating PI3K/AKT/FoxO3a pathway","authors":"Yonghua Li,&nbsp;Yibing Chen,&nbsp;Yuan Liao,&nbsp;Ting Huang,&nbsp;Qing Tang,&nbsp;Chengsi He,&nbsp;Liu Xu,&nbsp;Haocai Chang,&nbsp;Hongsheng Li,&nbsp;Quentin Liu,&nbsp;Dongming Lai,&nbsp;Qing Xia,&nbsp;Zhengzhi Zou","doi":"10.1007/s10495-026-02405-z","DOIUrl":"10.1007/s10495-026-02405-z","url":null,"abstract":"","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 9","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148886348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Copper, cuproptosis, and cancer: biology concepts of a novel cell death","authors":"Reza Eshraghi,&nbsp;Nastaran Hosseini,&nbsp;Mohammad Sepehr Yazdani,&nbsp;Shirin Badihi,&nbsp;Pedram Pirmoradian,&nbsp;Ashkan Bahrami,&nbsp;Bahar Darouei,&nbsp;Shayan Ghanouni,&nbsp;Alfred K. Lam,&nbsp;Michael R. Hamblin","doi":"10.1007/s10495-026-02432-w","DOIUrl":"10.1007/s10495-026-02432-w","url":null,"abstract":"<div><p>Copper is an essential trace element required for mitochondrial respiration, redox regulation, iron metabolism, and cellular signalling, but excessive or mislocalised copper can be cytotoxic. Cuproptosis is a recently identified form of regulated cell death in which copper binds to lipoylated mitochondrial proteins, promotes their aggregation, destabilises iron–sulfur cluster proteins, and induces mitochondrial proteotoxic stress. Copper therefore has context-dependent roles in cancer. Physiological copper supports tumour metabolism, angiogenesis, extracellular-matrix remodelling, and selected oncogenic signalling pathways, whereas therapeutic copper depletion can inhibit copper-dependent tumour processes. Conversely, copper ionophores and related approaches may increase intracellular copper sufficiently to induce cuproptosis in metabolically susceptible cancer cells. This review describes systemic and intracellular copper homeostasis, including intestinal absorption, intracellular trafficking, mitochondrial copper distribution, storage, and export. Particular attention is given to CTR1/SLC31A1, the functionally distinct copper-transporting ATPases ATP7A and ATP7B, metallothioneins, copper chaperones, and cytochrome c oxidase assembly factors. We also examine how cancer cells reprogramme copper handling to support proliferation, angiogenesis, metastasis, and immune evasion. Finally, we discuss the molecular basis of cuproptosis, including the roles of FDX1, FDXR, LIAS, DLAT, mitochondrial respiration, protein lipoylation, and iron–sulfur cluster destabilisation. Current evidence indicates that cuproptosis susceptibility varies among tumour types and depends on copper handling, mitochondrial metabolic state, and the integrity of the protein-lipoylation machinery. Defining these determinants will be necessary for the development of tumour-selective copper-targeted therapies.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":8062,"journal":{"name":"Apoptosis","volume":"31 9","pages":""},"PeriodicalIF":9.0,"publicationDate":"2026-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13541888/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148886313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}