Cell Death and Differentiation最新文献

{"title":"Daniel Aberdam, the legacy of a mentor.","authors":"Huiqing Zhou, Bernard Attali, Neil Lagali, Ruby Shalom-Feuerstein","doi":"10.1038/s41418-025-01520-9","DOIUrl":"https://doi.org/10.1038/s41418-025-01520-9","url":null,"abstract":"","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":" ","pages":""},"PeriodicalIF":13.7,"publicationDate":"2025-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144215033","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":"DNA damage response defects induced by the formation of TDP-43 and mutant FUS cytoplasmic inclusions and their pharmacological rescue","authors":"Stefania Modafferi, Stefania Farina, Francesca Esposito, Ornella Brandi, Michela Di Salvio, Ilaria Della Valle, Sara D’Uva, Eveljn Scarian, Giada Cicio, Adelaide Riccardi, Federica Pisati, Anna Garbelli, Tiziana Santini, Orietta Pansarasa, Mariangela Morlando, Nadia D’Ambrosi, Mauro Cozzolino, Gianluca Cestra, Fabrizio d’Adda di Fagagna, Ubaldo Gioia, Sofia Francia","doi":"10.1038/s41418-025-01530-7","DOIUrl":"https://doi.org/10.1038/s41418-025-01530-7","url":null,"abstract":"<p>Formation of cytoplasmic inclusions (CIs) of TDP-43 and FUS, along with DNA damage accumulation, is a hallmark of affected motor neurons in Amyotrophic Lateral Sclerosis (ALS). However, the impact of CIs on DNA damage response (DDR) and repair in this pathology remains unprobed. Here, we show that CIs of TDP-43 and FUS^P525L, co-localizing with stress granules, lead to a dysfunctional DDR activation associated with physical DNA breakage. Inhibition of the activity of the DDR kinase ATM, but not of ATR, abolishes DDR signaling, indicating that DNA double-strand breaks (DSBs) are the primary source of DDR activation. In addition, cells with TDP-43 and FUS^P525L CIs exhibit reduced DNA damage-induced RNA synthesis at DSBs. We previously showed that the two endoribonucleases DROSHA and DICER, also known to interact with TDP-43 and FUS during small RNA processing, contribute to DDR signaling at DSBs. Treatment with enoxacin, which stimulates DDR and repair by boosting the enzymatic activity of DICER, restores a proficient DDR and reduces DNA damage accumulation in cultured cells with CIs and in vivo in a murine model of ALS. In <i>Drosophila melanogaster</i>, Dicer-2 overexpression rescues TDP-43-mediated retinal degeneration. In summary, our results indicate that the harmful effects caused by TDP-43 and FUS CIs include genotoxic stress and that the pharmacological stimulation of the DNA damage signaling and repair counteracts it.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"26 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144164774","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":"Targeting the BCKDK/BCLAF1/MYC/HK2 axis to alter aerobic glycolysis and overcome Trametinib resistance in lung cancer","authors":"Hao Wu, Jiajia Yang, Zixia Yang, Yawen Xiao, Ran Liu, Jing Jia, Xinrui Zhang, Yuting Zhang, Zheng Fu, Zhi Yao, Junqiang Lv","doi":"10.1038/s41418-025-01531-6","DOIUrl":"https://doi.org/10.1038/s41418-025-01531-6","url":null,"abstract":"<p>The protein branched-chain ketoacid dehydrogenase kinase (BCKDK), which regulates the metabolism of branched-chain amino acids, has recently been implicated in tumor progression. However, the role of BCKDK in lung cancer remains largely unexplored. In this study, we explored the mechanisms by which BCKDK influences lung cancer progression and contributes to drug resistance. By integrating single-cell RNA and bulk RNA sequencing data from lung cancer patients, we identified BCKDK as a novel gene related to malignant epithelial cells, involved in tumor initiation and associated with poor patient prognosis. Subsequently, through a series of molecular biology experiments, we demonstrated that BCKDK promotes aerobic glycolysis, Trametinib resistance, and tumor progression in lung cancer by upregulating MYC transcription. Mechanistically, BCKDK interacts with BCLAF1 to promote its phosphorylation at the serine 285 site. This modification facilitates BCLAF1 binding to the MYC promoter, thereby enhancing MYC transcription. Subsequently, elevated MYC levels upregulate hexokinase 2, promoting aerobic glycolysis and lung cancer progression. In addition, the elevated glycolysis product, lactate, promotes Trametinib resistance by upregulating the ABC transporters. Taken together, our data identify BCKDK as a novel regulator of aerobic glycolysis that promotes lung cancer progression and Trametinib resistance through the BCKDK/BCLAF1/MYC/HK2 axis. Targeting BCKDK in combination with Trametinib may offer a promising treatment for lung cancer.</p><figure><p>Graphical representation of the BCKDK/BCLAF1/MYC/HK2 axis and its role in Trametinib resistance and lung cancer progression. Created with BioRender.com.</p></figure>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"4 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144177350","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":"NDUFS3 promotes proliferation via glucose metabolism reprogramming inducing AMPK phosphorylating PRPS1 to increase the purine nucleotide synthesis in melanoma","authors":"Guohang Xiong, Fang Yun, Lu Jiang, Zihan Yi, Xiaojia Yi, Lijuan Yang, Xuedan Zhang, Xiaoyu Li, Zhe Yang, Qiao Zhang, Buqing Sai, Yingmin Kuang, Yuechun Zhu","doi":"10.1038/s41418-025-01525-4","DOIUrl":"https://doi.org/10.1038/s41418-025-01525-4","url":null,"abstract":"<p>NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (NDUFS3) is the core subunit of the respiratory chain complex I (CI). We found NDUFS3 were abnormally elevated in human melanoma and promoted melanoma proliferation. Furthermore, NDUFS3 could promote the oxidative phosphorylation (OXPHOS) and the pentose phosphate pathway (PPP), as well as attenuated glycolysis. As NDUFS3-mediated the metabolic changes of OXPHOS and glucose metabolism, melanoma cells produced more ATP, resulting in the inhibition of AMP kinase (AMPK). AMPK induced phosphoribosyl pyrophosphate synthetase1 (PRPS1) phosphorylation, which resulted in suppressed PRPS1 activity. Briefly, the NDUFS3-AMPK-PRPS1 signaling axis coupled OXPHOS, glucose metabolism, and purine nucleotide biosynthesis to regulate melanoma proliferation. Our study highlighted an unrecognized role for NDUFS3 in melanoma, which might be used as a potential therapeutic target for the treatment of this type of cancer.</p><figure><p>NDUFS3 regulating PRPS1 activity through AMPK to affect melanoma proliferation.</p></figure>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"2 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144113537","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":"Thymic egress and peripheral T cell homeostasis regulated by Rho GTPase-activating protein 30","authors":"Huiling Zhang, Zhihan Guo, Jingjing Yi, Jiaying Wu, Yihan Wang, Tingrong Ren, Yuqi Zhang, Haiping Zhao, Nana Wu, Gaigai Wei, Duanwu Zhang","doi":"10.1038/s41418-025-01529-0","DOIUrl":"https://doi.org/10.1038/s41418-025-01529-0","url":null,"abstract":"<p>T cells are central to adaptive immunity, with proper thymic development and egress critical for T cell homeostasis in peripheral tissues. The molecular mechanisms governing thymic egress remain poorly understood. Here, we identify Rho GTPase-activating protein 30 (ARHGAP30), predominantly expressed in lymphoid organs and previously uncharacterized in immunity, as a key regulator of thymocyte migration and egress. Loss of ARHGAP30 leads to impaired thymic development and severe T cell lymphopenia. Notably, <i>Arhgap30</i>-deficient mice exhibit a reduced number of immature single-positive (SP) thymocytes but a normal number of mature SP thymocytes, indicating a blockade in thymic egress. Mechanistically, ARHGAP30 deficiency lowers GTP-bound active RAC1 independent of its GAP activity, impairing actin polarization and thymocyte motility. ARHGAP30 selectively binds and stabilizes active RAC1, preventing its proteasomal degradation via K48-linked ubiquitination. These findings establish ARHGAP30 as a critical checkpoint for thymic egress and underscore its essential role in maintaining peripheral T cell homeostasis.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"4 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144113545","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":"NLRX1 mediated impaired microglial phagocytosis of NETs in cerebral ischemia and reperfusion injury","authors":"Jialing Peng, Yuxin Huang, Tengjing He, Yang Zhan, Jun Liu","doi":"10.1038/s41418-025-01526-3","DOIUrl":"https://doi.org/10.1038/s41418-025-01526-3","url":null,"abstract":"<p>Ischemic stroke is one of the common causes of disability and death, and subsequent pathological processes consequent to revascularization could promote secondary tissue damage leading to neuronal death, namely cerebral ischemia and reperfusion injury. Neutrophils could invade injured brain parenchyma after vascularization and exert neurotoxicity by forming neutrophil extracellular traps (NETs). However, unwanted NETs were accumulated in the infarcted core of transient middle cerebral artery occlusion (tMCAO) rats and the mechanism is unknown. Efficient microglial phagocytosis is crucial for the homeostasis of cerebral parenchyma after stroke, and dysfunction of microglial phagocytosis of NETs were observed in the infarcted core cortex at tMCAO 1 d and the accumulation of NETs persisted to 7 d, which exerting deleterious neuronal damage after stroke. However, the detailed mechanisms underlying the dysfunction of microglial phagocytosis of NETs remained unclear. Our results further demonstrated that NLRX1 was mainly enhanced in the microglial cells in the infarcted core cortex at tMCAO 1 d and promoted galectin-3 expression on the lysosomes, facilitating the lysosomal dysfunction and impaired microglial phagocytosis via mTOR/TFEB signaling. NLRX1-silencing was able to suppress the galectin-3 intensity, inhibit the phosphorylation of mTOR and facilitate the nuclear localization of TFEB, ameliorating the lysosomal dysfunction and microglial phagocytosis of NETs. Our results uncovered the regulation of NLRX1 in the dysfunctional microglial phagocytosis of NETs and provided insights into the therapeutic potential for targeting at microglial lysosomal function in cerebral ischemia and reperfusion injury.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"133 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144113538","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":"Gain-of-function PPM1D mutations attenuate ischemic stroke","authors":"Wenyan He, Yan Li, Junwan Fan, Yang Liu, Meng Yuan, Si Cheng, Xinying Huang, Bo Yan, Zhuoran Zhang, Yuwen Xiu, Huimin Zhu, Tian Lan, Zhilin Chang, Yong Jiang, Hao Li, Xia Meng, Yilong Wang, Luc Van Kaer, Alexei Verkhratsky, Yongjun Wang, Fu-Dong Shi, Wei-Na Jin","doi":"10.1038/s41418-025-01523-6","DOIUrl":"https://doi.org/10.1038/s41418-025-01523-6","url":null,"abstract":"<p>Identification of genetic aberrations in stroke, the second leading cause of death worldwide, is of paramount importance for understanding the disease pathogenesis and generating new therapies. Whole-genome sequencing from 10,241 ischemic stroke patients identified eight patients carrying gain-of-function mutations on coding variants in the protein phosphatase magnesium-dependent 1 δ (<i>PPM1D</i>) gene. Patients carrying <i>PPM1D</i> mutations exhibit better stroke-related clinical phenotypes, including improvements in peripheral inflammation, fibrinogen, low-density lipoprotein, cholesterol and plateletcrit level. Experimental brain ischemia in <i>Ppm1d</i>-deficient (<i>Ppm1d</i>⁻^<i>/</i>⁻) mice resulted in enlarged lesions and pronounced neurological impairments. Spatial transcriptomics revealed a distinct <i>Ppm1d</i>-associated gene expression pattern, indicating disrupted endothelial homeostasis during ischemic brain injury. Proteomic analysis demonstrated that differentially expressed proteins in primary brain endothelial cells from <i>Ppm1d</i>⁻^<i>/</i>⁻ mice were significantly enriched in the peroxisome proliferator-activated receptors (PPARs)-mediated metabolic signaling. Mechanistically, <i>Ppm1d</i> deficiency promoted aberrant fatty acid β-oxidation and increased oxidative stress, which impaired endothelial cell function through the PPARα pathway. A small molecule, T2755, was identified to engage Trp427 and stabilize PPM1D, thereby mitigating ischemic brain injury in mice. Collectively, we find that PPM1D protects against ischemic brain injury and validates its pharmacological stabilizer T2755 as a promising therapy for ischemic stroke.</p><figure><p><b>Gain-of-function</b> <b><i>PPM1D</i></b> <b>mutations attenuate ischemic cerebral injury</b>. Whole-genome sequencing data of 10,241 ischemic stroke patients from the Third Chinese National Stroke Registry (CNSR-III) identified eight patients with gain-of-function mutations in the protein phosphatase magnesium-dependent 1 δ (<i>PPM1D</i>) gene (17q23.2). These mutation carriers displayed improved peripheral inflammation, decreased fibrinogen, low-density lipoprotein, cholesterol and plateletcrit level. <i>Ppm1d-deficient</i> (<i>Ppm1d</i>⁻^<i>/</i>⁻) mice exhibited exacerbated stroke outcomes, characterized by enlarged infarct volumes, disrupted cerebrovascular architecture, and enhanced neuro-inflammation. Mechanistically, <i>Ppm1d</i> deficiency induced the disturbance of endothelial fatty acid metabolism involving the PPARα pathway. Through integrated computational modeling, virtual screening, and in vitro validation, T2755 was identified as a small molecule PPM1D stabilizer. Pharmacological PPM1D stabilization with T2755 significantly attenuated ischemic brain injury in murine models.</p></figure>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"31 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144113540","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":"GPX4-AUTAC induces ferroptosis in breast cancer by promoting the selective autophagic degradation of GPX4 mediated by TRAF6-p62","authors":"Rong Gong, Xiaoya Wan, Shilong Jiang, Yidi Guan, Yizhi Li, Ting Jiang, Zonglin Chen, Changxin Zhong, Linhao He, Zhongyuan Xiang, Junya Yang, Biao Xu, Jinming Yang, Yan Cheng","doi":"10.1038/s41418-025-01528-1","DOIUrl":"https://doi.org/10.1038/s41418-025-01528-1","url":null,"abstract":"<p>Emerging evidence indicates that activation of ferroptosis by inhibition of glutathione peroxidase 4 (GPX4) may be exploited as a therapeutic strategy to suppress tumor growth and progression. However, application of GPX4 inhibitors in cancer treatment is hampered by their poor selectivity, which results in unfavorable toxicity. Herein, we identified GPX4 as a candidate for the autophagy pathway. We showed that GPX4 is ubiquitinated by TNF receptor-associated factor 6 (TRAF6), which promotes its recognition by p62 and leads to its selective autophagic degradation. Utilizing targeted protein degradation (TPD) approach, we developed a GPX4-targeted AUTAC and demonstrated that GPX4-AUTAC promoted the ubiquitination of GPX4, and enhanced the binding with GPX4 and p62, leading to the selective autophagy-dependent degradation of GPX4. Furthermore, GPX4-AUTAC treatment strongly induced ferroptosis and exhibited potent anti-cancer activity against breast cancer in vitro, in vivo, and patient-derived organoids (PDOs). Combination treatment of GPX4-AUTAC with sulfasalazine, a ferroptotic inducer, or chemotherapy drugs showed a synergistic anti-cancer effect against breast cancer. These results uncover a new targeted degradation strategy for GPX4 by inducing selective autophagy and provide a rationale for the use of GPX4-AUTAC as a novel therapeutic approach to treatment of breast cancer.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"9 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144104629","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":"Cockayne syndrome mice reflect human kidney disease and are defective in de novo NAD biosynthesis","authors":"Komal Pekhale, Vinod Tiwari, Mansoor Hussain, Christy C. Bridges, Deborah L. Croteau, Moshe Levi, Avi Z. Rosenberg, Briana Santo, Xiaoping Yang, Tomasz Kulikowicz, Xiaoxin X. Wang, Jong-Hyuk Lee, Vilhelm A. Bohr","doi":"10.1038/s41418-025-01522-7","DOIUrl":"https://doi.org/10.1038/s41418-025-01522-7","url":null,"abstract":"<p>Cockayne Syndrome (CS) is a premature aging disorder caused by mutations in the CSA and CSB genes involved in DNA metabolism and other cellular processes. CS patients display many features including premature aging, neurodegeneration, and kidney abnormalities. Nicotinamide dinucleotide (NAD⁺) deprivation has been observed in CS patient-derived cells. NAD⁺ has essential roles in regulating cellular health, stress responses, and renal homeostasis. While kidney dysfunction is a common feature in CS patients, its molecular pathogenesis is not understood. Here, we report that severe kidney pathology is present in CS A and B mice. We find that the NAD⁺ biosynthetic pathways are impaired in kidneys from these mice. Using human renal tubular epithelial cells, we show that CSA/B downregulation causes persistent activation of the ATF3 transcription factor on the quinolinate phosphoribosyl transferase gene locus, a rate-limiting enzyme in de novo NAD⁺ biosynthesis in the kidney, causing impaired transcription and deficient NAD⁺ homeostasis.</p>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"41 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143980020","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":"Fatty acid synthesis promotes mtDNA release via ETS1-mediated oligomerization of VDAC1 facilitating endothelial dysfunction in sepsis-induced lung injury","authors":"Shiyuan He, Tingting Pan, Rui Tian, Qian He, Decui Cheng, Hongping Qu, Ranran Li, Ruoming Tan","doi":"10.1038/s41418-025-01524-5","DOIUrl":"https://doi.org/10.1038/s41418-025-01524-5","url":null,"abstract":"<p>Sepsis involves endothelial cell dysfunction leading to the development of lung injury. Fatty acid synthesis contributes to the development of inflammatory injury in sepsis. However, the regulatory mechanisms of fatty acid synthesis-related endothelial activation remain unclear. In this study, we found that fatty acid synthesis in patients with sepsis was greatly disordered. Inhibition of fatty acid synthesis significantly alleviated sepsis-induced endothelial damage and lung injury both in vitro and in vivo. We further found that the release of mtDNA participated in fatty acid synthesis-related regulation of endothelial inflammatory and coagulation activation. Mechanistically, fatty acid synthesis promoted the oligomerization of voltage-dependent anion channel 1 (VDAC1) via ETS proto-oncogene 1 (ETS1)-mediated inhibition of VDAC1 ubiquitination, thereby leading to the increased release of mtDNA and subsequent activation of cGAS-STING signaling and pyroptosis in endothelial cells. Our findings revealed that fatty acid synthesis promoted endothelial dysfunction through mtDNA release, providing new insight into the therapeutic strategies for treating sepsis-associated lung injury.</p><figure></figure>","PeriodicalId":9731,"journal":{"name":"Cell Death and Differentiation","volume":"123 1","pages":""},"PeriodicalIF":12.4,"publicationDate":"2025-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143980022","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}