Cell Death & Disease最新文献

{"title":"Hypomethylation induced overexpression of PLOD3 facilitates colorectal cancer progression through TM9SF4-mediated autophagy.","authors":"Renzhong Zhu, Chuanxin Tian, Nan Gao, Zhiqiang Li, Sheng Yang, Yue Zhang, Ming Zhou, Yueming Sun, Chuan Zhang, Kangpeng Jin","doi":"10.1038/s41419-025-07503-5","DOIUrl":"10.1038/s41419-025-07503-5","url":null,"abstract":"<p><p>Colorectal cancer (CRC) ranks among the primary causes of human mortality globally. Numerous studies have highlighted the significant role of PLOD3 in the progression of various cancers. However, the exact function and underlying mechanisms of PLOD3 in CRC remains incompletely understood. To investigate the expression of PLOD3, qRT‒PCR, immunohistochemistry and western blotting were utilized to analyze the expression of PLOD3 in CRC tissues and adjacent normal tissues. Functional assays were conducted to assess the roles of PLOD3 both in vitro and in vivo. To elucidate the potential mechanism of PLOD3 in CRC, a range of techniques, including coimmunoprecipitation, immunofluorescence, CHX pulse-chase, and ubiquitination assays were used. As the results indicated, hypomethylation of the PLOD3 promoter leads to its over- expression in CRC, and elevated PLOD3 levels are associated with a poor prognosis. Both in vitro and in vivo models demonstrated that PLOD3 enhances CRC cell proliferation, invasion, and migration. Furthermore, through mechanistic studies, TM9SF4 was identified as a protein that interacts with PLOD3 and contributes to CRC progression by promoting autophagy. Additionally, PLOD3 could be secreted by CRC cells and secreted PLOD3 could promote CRC cells migration and invasion. These results demonstrated that PLOD3 promotes CRC progression through the PLOD3/TM9SF4 axis and could be a potential biomarker and treatment target for CRC.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"206"},"PeriodicalIF":8.1,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937244/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143708851","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":"ATP6AP1 promotes cell proliferation and tamoxifen resistance in luminal breast cancer by inducing autophagy.","authors":"Zhengwei Yan, Aidi Huang, Dongwen Ma, Chenao Hong, Shengmiao Zhang, Luling He, Hai Rao, Shiwen Luo","doi":"10.1038/s41419-025-07534-y","DOIUrl":"10.1038/s41419-025-07534-y","url":null,"abstract":"<p><p>Autophagy is a highly conserved cellular process essential for maintaining cellular homeostasis and influencing cancer development. Lysosomal acidification and autophagosome-lysosome fusion are two important steps of autophagy degradation that are tightly regulated. Although many key proteins that regulate these two events have been identified, the effector proteins that co-regulate both steps remain to be explored. ATP6AP1, an accessory subunit of V-ATPase, plays a critical role in the assembly and regulation of V-ATPase. However, the function of ATP6AP1 in autophagy remains unknown, and the role of ATP6AP1 in cancer is still poorly understood. In this study, we found that ATP6AP1 is overexpressed in luminal breast cancer tissues and promotes the proliferation and tamoxifen resistance of luminal breast cancer cells both in vitro and in vivo. We also observed that high ATP6AP1 expression correlates with poor overall patient survival. Our research further revealed that ATP6AP1 enhances tamoxifen resistance by activating autophagy. Mechanistically, ATP6AP1 promotes autophagy by regulating both lysosomal acidification and autophagosome-lysosome fusion. Remarkably, ATP6AP1 induces lysosomal acidification through the regulation of V-ATPase assembly and facilitates autophagosome-lysosome fusion by enhancing the interaction between Rab7 and the HOPS complex. Together, our studies identify ATP6AP1 as a crucial regulator of autophagy, potentially serving as a valuable prognostic marker or therapeutic target in human luminal breast cancer.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"201"},"PeriodicalIF":8.1,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937278/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143708790","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":"CARM1 S217 phosphorylation by CDK1 in late G2 phase facilitates mitotic entry.","authors":"Yena Cho, Dae-Geun Song, Su-Nam Kim, Yong Kee Kim","doi":"10.1038/s41419-025-07533-z","DOIUrl":"10.1038/s41419-025-07533-z","url":null,"abstract":"<p><p>The coactivator-associated arginine methyltransferase 1 (CARM1) functions as an epigenetic writer, however, its role in mitosis remains poorly understood. In this study, we identified CARM1 as a novel substrate of cyclin-dependent kinase 1 (CDK1) and revealed its novel function as a scaffold that regulates CDK1 stability. During interphase, CARM1 acts as an adaptor in the Cullin-1-mediated CDK1 degradation process, limiting nuclear levels of CDK1. In late G2 phase, the CDK1/Cyclin B1 complex translocates to the nucleus, where it phosphorylates the S217 residue of CARM1. This phosphorylation not only inhibits CARM1's enzymatic activity but also facilitates its translocation to the cytoplasm, leading to the loss of its scaffolding function. Consequently, the CDK1/Cyclin B1 complex resides for longer in the nucleus and initiates mitosis. In addition, depletion or inhibition of CARM1 facilitates entry into mitosis, resulting in accelerated cell growth. Overall, our findings expand the cellular functions of CARM1 beyond its enzymatic activity.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"202"},"PeriodicalIF":8.1,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937338/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143708797","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":"GLI2 inhibits cisplatin sensitivity in gastric cancer through DEC1/ZEB1 mediated EMT.","authors":"Wenshuai Zhu, Jingguo Sun, Fubo Jing, Yuanxin Xing, Muhua Luan, Zhaotian Feng, Xiaoli Ma, Yunshan Wang, Yanfei Jia","doi":"10.1038/s41419-025-07564-6","DOIUrl":"10.1038/s41419-025-07564-6","url":null,"abstract":"<p><p>Cisplatin (CDDP) based chemotherapy has emerged as the predominant therapeutic regimen for patients with advanced gastric cancer (GC). However, its efficacy is dampened by the development of chemoresistance, which results in poor prognosis of patients. GLI2, a key transcription factor in the Hedgehog (Hh) signaling pathway, is regarded as a target for cancer therapy. However, the significance of GLI2 for CDDP resistance in GC has not been well established. Here, we show that GLI2 expression was upregulated in EMT-type GC and associated with poor prognosis. GLI2 promotes proliferation, migration, and CDDP resistance of GC cells by inducing EMT. In terms of mechanism, GLI2 binds to the promoter region of DEC1 and enhances its expression, thereby co-transcriptionally regulating ZEB1 expression. Animal experiments have demonstrated that both GLI2 knockdown and GLI2 inhibitor significantly enhance CDDP sensitivity in GC. Our data not only identify a novel GLI2/DEC1/ZEB1/EMT pathway in GC CDDP resistance but also provide novel strategies to treat GC in the future.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"204"},"PeriodicalIF":8.1,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937514/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143708740","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":"Overexpression of βTrCP1 elicits cell death in cisplatin-induced senescent cells.","authors":"Alejandro Belmonte-Fernández, Joaquín Herrero-Ruíz, M Cristina Limón-Mortés, Carmen Sáez, Miguel Á Japón, Mar Mora-Santos, Francisco Romero","doi":"10.1038/s41419-025-07556-6","DOIUrl":"10.1038/s41419-025-07556-6","url":null,"abstract":"<p><p>Senescence is a non-proliferative cellular state derived from aging or in response to exogenous insults, such as those that cause DNA damage. As a result of cancer treatments like cisplatin, certain tumor cells may undergo senescence. However, rather than being beneficial for patients, this is detrimental because these cells might proliferate again under specific conditions and, more importantly, because they synthesize and secrete molecules that promote the proliferation of nearby cells. Therefore, to achieve complete tumor remission, it is necessary to develop senolytic compounds to eliminate senescent cells. Here, we studied the role of βTrCP1 in cell proliferation and senescence and found that lentiviral overexpression of βTrCP1 induces the death of senescent cells obtained after cisplatin treatment in both two-dimensional cell cultures and tumorspheres. Mechanistically, we demonstrated that overexpression of βTrCP1 triggers proteasome-dependent degradation of p21 CIP1, allowing damaged cells to progress through the cell cycle and consequently die. Furthermore, we identified nucleophosmin 1 (NPM1) as the intermediary molecule involved in the effect of βTrCP1 on p21 CIP1. We determined that increased amounts of βTrCP1 partially retains NPM1 in the nucleoli, preventing it from associating with p21 CIP1, thus leaving it unprotected from degradation by the proteasome. These results have allowed us to discover a potential new target for senolytic drugs, as retaining NPM1 in the nucleoli under senescent conditions induces cell death.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"203"},"PeriodicalIF":8.1,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937513/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143708855","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":"Retraction Note to: BRD4 promotes tumor progression and NF-κB/CCL2-dependent tumor-associated macrophage recruitment in GIST.","authors":"Jianfeng Mu, Pengfei Sun, Zhiming Ma, Pengda Sun","doi":"10.1038/s41419-025-07520-4","DOIUrl":"10.1038/s41419-025-07520-4","url":null,"abstract":"","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"200"},"PeriodicalIF":8.1,"publicationDate":"2025-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11933419/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143699671","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":"Hippocampus- and neocortex-specific deletion of Aeg-1 causes learning memory impairment and depression in mice.","authors":"Ya-He Wang, Ning Zhou, Pan-Pan Wan, Xin-Tong Li, Chun-Yang Yu, Jinjiang Chou, Zong-Yi Feng, Lian-Xiang Zhang, Juan-Juan Li, Bao-Cong Yu, Zhen-Ning Tang, Kun-Mei Liu, Le Guo","doi":"10.1038/s41419-025-07508-0","DOIUrl":"10.1038/s41419-025-07508-0","url":null,"abstract":"<p><p>Astrocyte elevated gene-1 (AEG-1) has been characterized as an oncogene promoting the progression of various tumors. The role of AEG-1 in neurological diseases was highlighted by recent researches. However, the physiological function of AEG-1 remains elusive. Our study aimed to investigate the physiological role of AEG-1 in the central nervous system by generating a mouse model with specific deletion of Aeg-1 in the hippocampus and neocortex (Aeg-1^fl/flCre⁺ mice). Behavioral assessments revealed that Aeg-1 deficiency caused impaired learning and memory capabilities in juvenile and adult mice. Depressive-like behaviors were also observed in Aeg-1^fl/flCre⁺ mice. Gene Ontology (GO) enrichment analyses indicated that AEG-1 was involved in the neuronal morphogenesis. Interestingly, Aeg-1 knockout was irrelevant to the neuron loss but reduced the dendritic length and the dendritic spines density in hippocampus. Electrophysiological analyses showed a decreased response of paired-pulse facilitation (PPF) and a compromised efficiency of excitatory synaptic transmission following Aeg-1 deletion in hippocampus. In conclusion, our findings suggest that Aeg-1 deficiency in the hippocampus and neocortex leads to learning and memory impairments and depression in mice, which is mediated by the abnormalities of neuronal morphology and the impaired synaptic functions.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"199"},"PeriodicalIF":8.1,"publicationDate":"2025-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11930984/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143691302","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":"LL37 complexed to double-stranded RNA induces RIG-I-like receptor signalling and Gasdermin E activation facilitating IL-36γ release from keratinocytes.","authors":"Jennifer Keller, Judit Danis, Isabella Krehl, Eleftheria Girousi, Takashi K Satoh, Barbara Meier-Schiesser, Lajos Kemény, Márta Széll, W Wei-Lynn Wong, Steve Pascolo, Lars E French, Thomas M Kündig, Mark Mellett","doi":"10.1038/s41419-025-07537-9","DOIUrl":"10.1038/s41419-025-07537-9","url":null,"abstract":"<p><p>The Interleukin-36 (IL-36) cytokine family have emerged as important players in mounting an inflammatory response at epithelial barriers and tailoring appropriate adaptive immune responses. As members of the Interleukin-1 superfamily, IL-36 cytokines lack a signal peptide for conventional secretion and require extracellular proteolysis to generate bioactive cytokines. Although the IL-36 family plays an important role in the pathogenesis of plaque and pustular psoriasis, little is known about the release mechanisms of these cytokines from keratinocytes and the physiological stimuli involved. Nucleic acid released from damaged or dying keratinocytes initiates early inflammatory signals that result in the breaking of tolerance associated with psoriasis pathogenesis onset. Cathelicidin peptide, LL37 binds to DNA or double-stranded RNA (dsRNA) and activates a type I Interferon responses in plasmacytoid dendritic cells and keratinocytes. Here, we demonstrate that LL37 binds to dsRNA and induces IL-36γ release from human primary keratinocytes. LL37/dsRNA complexes activate RIG-I-like Receptor signalling, resulting in Caspase-3 and Gasdermin E (GSDME) cleavage. Subsequent GSDME pore formation facilitates IL-36γ release. This response is magnified by priming with psoriasis-associated cytokines, IL-17A and IFNγ. IL-36γ release in this manner is largely independent of cell death in primary keratinocytes and lacked extracellular proteolysis of IL-36γ. Conversely, transfection of keratinocytes directly with dsRNA synthetic analogue, Poly(I:C) induces NLRP1 inflammasome activation, which facilitates IL-36γ expression and release in a GSDMD-dependent manner. Inflammasome-associated cell death also enables extracellular processing of IL-36γ by the release of keratinocyte-derived proteases. These data highlight the distinct responses triggered by dsRNA sensors in keratinocytes. Depending on the inflammatory context and magnitude of the exogenous threat, keratinocytes will release IL-36γ coupled with cell death and extracellular cleavage or release the inactive pro-form, which requires subsequent processing by neutrophil proteases to unleash full biological activity, as occurring in psoriatic skin. Cytoplasmic sensing of dsRNA in keratinocytes mediates IL-36γ release via caspase activity and GSDM pore formation Keratinocytes release IL-36γ upon stimulation with intracellular dsRNA alone or complexed to the psoriasis-associated cathelicidin anti-microbial peptide LL37. Left: Transfected dsRNA triggers NLRP1 inflammasome assembly and IL-1β release, which can enhance IL-36γ expression, resulting in IL-36γ release and extracellular cleavage by released proteases. Right: LL37/dsRNA complexes activate a MDA5-MAVS pathway facilitating the release of IL-36γ through Caspase-3 activation and GSDME pore formation.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"198"},"PeriodicalIF":8.1,"publicationDate":"2025-03-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11929817/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143691303","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":"Inhibition of 11β-hydroxysteroid dehydrogenase 1 alleviates pulmonary fibrosis through inhibition of endothelial-to-mesenchymal transition and M2 macrophage polarization by upregulating heme oxygenase-1.","authors":"Su-Yeon Lee, Ji-Hee Kim, Yeonhwa Song, Sanghwa Kim, Hyo Jin Kang, Jason Kim, Yoon-Jin Lee, Haeng Ran Seo","doi":"10.1038/s41419-025-07522-2","DOIUrl":"10.1038/s41419-025-07522-2","url":null,"abstract":"<p><p>The intracellular enzyme 11β-hydroxysteroid dehydrogenase type 1 (11βHSD1) catalyzes the interconversion of active glucocorticoid (cortisol) and its intrinsically inert form (cortisone) in metabolic tissues. Although 11βHSD1 is considered a promising therapeutic target in metabolic disorders such as type 2 diabetes, obesity, and nonalcoholic steatohepatitis because of its hepatic functions, its roles in other tissues have received less attention. In this study, we show that the 11βHSD1-specific inhibitor J2H-1702 facilitates the reversion of endothelial-to-mesenchymal transition in multicellular lung spheroid models encapsulating the complex crosstalk among lung cancer cells, vascular endothelial cells, and macrophages. In vascular endothelial cells, J2H-1702 not only suppressed interleukin-1α (IL-1α) expression but also attenuated reactive oxygen species-induced DNA damage by upregulating heme oxygenase-1. Additionally, in macrophages, which are key regulators of fibrogenesis, inhibition of 11βHSD1 markedly reduced IL-1β expression, thereby modulating the pro-inflammatory phenotype of activated macrophages. In mouse models of pulmonary fibrosis, including a bleomycin-induced idiopathic model and a radiation-induced model, J2H-1702 alleviated pulmonary fibrosis and markedly improved the efficacy of nintedanib. Collectively, our data suggest that J2H-1702 holds promise as a clinical candidate for the treatment of pulmonary fibrosis associated with reactive oxygen species-induced DNA damage, endothelial-to-mesenchymal transition, and inflammatory responses.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"196"},"PeriodicalIF":8.1,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11928689/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143677060","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":"Decoy-PROTAC for specific degradation of \"Undruggable\" STAT3 transcription factor.","authors":"Shiqing Li, Xin Wang, Jiabao Huang, Xiuping Cao, Yana Liu, Shiyan Bai, Tao Zeng, Qi Chen, Chunsen Li, Chunhua Lu, Huanghao Yang","doi":"10.1038/s41419-025-07535-x","DOIUrl":"10.1038/s41419-025-07535-x","url":null,"abstract":"<p><p>Signal transducer and activator of transcription 3 (STAT3) is widely recognized as an attractive target for cancer therapy due to its significant role in the initiation and progression of tumorigenesis. However, existing STAT3 inhibitors have suffered from drawbacks including poor efficacy, limited specificity, and undesirable off-target effects, due to the challenging nature of identifying active sites or allosteric regulatory pockets on STAT3 amenable to small-molecule inhibition. In response to these obstacles, we utilize the innovative proteolysis targeting chimera (PROTAC) technology to create a highly specific decoy-targeted protein degradation system for STAT3 protein, termed D-PROTAC. This system fuses DNA decoy that targets STAT3 with an E3 ligase ligand, utilizing a click chemistry approach. Experimental results demonstrate that D-PROTAC efficiently mediates the degradation of the STAT3 protein across various cancer cell types, leading to the downregulation of crucial downstream STAT3 targets, inhibiting tumor cell growth, triggering cell cycle arrest and apoptosis, and suppressing tumor immune evasion. Furthermore, D-PROTAC is capable of achieving significant tumor suppression in xenograft models. Overall, our research validates that D-PROTAC can successfully target and eliminate the \"undruggable\" STAT3, showcasing specificity and potent antitumor effects. This strategy will suggest a promising avenue for the development of targeted therapies against the critical functions of STAT3 in human cancers and potentially other diseases.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"197"},"PeriodicalIF":8.1,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11928565/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143676999","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}