Cell Death Discovery最新文献

{"title":"NRP1 promotes hepatic fibrosis by regulating Src/Rab7-mediated lysosomal degradation of TβRI.","authors":"Zhe Jia, Xiaodong Song, Jie Bai","doi":"10.1038/s41420-026-03220-w","DOIUrl":"10.1038/s41420-026-03220-w","url":null,"abstract":"<p><strong>Background and aims: </strong>Activation of hepatic stellate cells (HSCs) and subsequent dysregulation of the TGF-β1 signaling pathway are central to the progression of hepatic fibrosis. Neuropilin-1 (NRP1) has been identified as a co-receptor involved in multiple signaling pathways, yet its role in modulating TGF-β receptor stability in HSCs remains to be fully elucidated. This study investigated the regulatory role of the NRP1/Src/Rab7 axis in TβRI lysosomal degradation during HSC activation.</p><p><strong>Methods: </strong>Hepatic fibrosis was induced in male C57BL/6 mice via intraperitoneal CCl₄ injection for four weeks. HSC-specific knockdown of Nrp1 was achieved using an AAV8-pLrat-shNrp1 vector. TβRI stability and lysosomal degradation were evaluated through cycloheximide (CHX) chase assays and chloroquine treatment. The impact on the TGF-β1/Smad signaling pathway was assessed both in vitro and in vivo.</p><p><strong>Results: </strong>Nrp1 silencing in primary HSCs reduced TβRI protein levels and attenuated p-Smad2/3 signaling without affecting mRNA levels. Consistently, NRP1 deficiency accelerated lysosomal degradation of TβRI, accompanied by increased TβRI-LAMP1 colocalization and enhanced trafficking of TβRI into Rab7-positive late endosomes. Mechanistically, NRP1 loss diminished Src kinase activity and consequently reduced Src-dependent tyrosine phosphorylation of Rab7, leading to elevated Rab7-GTP levels and enhanced late endosomal sorting of TβRI. Rab7 knockdown or Src reactivation partially rescued TβRI stability and restored downstream signaling. In vivo, HSC-specific Nrp1 knockdown attenuated CCl₄-induced fibrosis and reduced TβRI levels, while Rab7 inhibition partially reversed these effects.</p><p><strong>Conclusions: </strong>These data suggest that the NRP1/Src/Rab7 axis contributes to TβRI stability by modulating its lysosomal degradation pathway. Targeting this axis may provide a potential approach for intervening in the progression of hepatic fibrosis.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13572504/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338074","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":"KLF15 activates PGC1α to rewire mitochondrial homeostasis and overcome cisplatin resistance in lung adenocarcinoma.","authors":"Wan Lin, Lijuan Li, Yuwen Bai, Mai Wen, Wenjie Dong, Ruikun Ji, Jianqun Ma, Xiaodong Ling","doi":"10.1038/s41420-026-03235-3","DOIUrl":"10.1038/s41420-026-03235-3","url":null,"abstract":"<p><p>Cisplatin resistance represents a major barrier to effective treatment of lung adenocarcinoma (LUAD), yet its metabolic underpinnings remain incompletely defined. Here, we demonstrate that the transcription factor KLF15 governs cisplatin sensitivity by orchestrating mitochondrial biogenesis and redox homeostasis. KLF15 is downregulated in cisplatin-resistant LUAD cells, which display reduced mitochondrial content and suppressed reactive oxygen species (ROS) accumulation. Restoring KLF15 expression resensitizes LUAD cells to cisplatin both in vitro and in vivo. Mechanistically, KLF15 directly transactivates PGC1α, and loss of PGC1α abrogates KLF15-mediated cisplatin sensitization, restoring drug resistance by attenuating apoptosis. Functionally, LUAD subpopulations with low mitochondrial mass or low KLF15 expression exhibit intrinsic resistance, whereas Mito-high xenografts show enhanced therapeutic response. Together, our findings identify a KLF15-PGC1α regulatory axis that dictates mitochondrial reprogramming and cisplatin responsiveness, highlighting a potential therapeutic axis to overcome chemoresistance in LUAD.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13572412/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338095","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":"Histidine to glutamine substitutants, a regulated process that impacts cell survival and suggests histidine shortage in cancer.","authors":"Domenica Lovecchio, Pierre-René Körner, Lorenzo Valcanover, Onno B Bleijerveld, Bart R J Blokhuis, Abhijeet Pataskar, Jasmine Montenegro Navarro, Demi Wernaart, Liesbeth Hoekman, Daniil Anastasopoulos, Kim Vrijland, Xiaodong Feng, Julien Champagne, Karin E de Visser, Olaf van Tellingen, Frank A Redegeld, Reuven Agami","doi":"10.1038/s41420-026-03225-5","DOIUrl":"10.1038/s41420-026-03225-5","url":null,"abstract":"<p><p>Cancer-associated genetic, epigenetic, and microenvironmental factors impose shortages of tryptophan and arginine, which induce specific codon reassignments (substitutants) in their proteomes. Whether cancers are deprived of other amino acids is unknown. Histidine is an essential amino acid reported to be low in certain tumor types. Therefore, we investigated the potential for a histidine shortage in cancer. Using cultured cancer cells, we pinpointed histidine to glutamine (H>Q) substitutants as the most pronounced proteomic event following histidine deprivation. We then scanned cancer proteomes for H>Q proteins and observed a marked enrichment in pancreatic, uterine, and kidney cancers. Mechanistically, we propose that H>Q is a result of tRNA misalignment, and used tRNA glutamine (tRNA(Gln)) modifications at the wobble position to demonstrate it. We further show that URM1-mediated U34 thiolation boosts H>Q production and influences the survival of cancer cells following histidine deprivation, suggesting a potential role for H>Q. Additional characterization of H>Q substitutants revealed preferred sequences and the maintenance of H>Q host protein expression despite the absence of histidine, indicating cellular regulation and functional consequences. Thus, histidine shortage induces H>Q substitutants, a regulated mistranslation event that pinpoints histidine limitation in cancer and impacts cell survival.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13572455/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338048","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":"Ferroptosis-induced oxidative stress in therapy-resistant glioblastoma.","authors":"Sofia Remedia, Cristina Martelli, Marcella Bonanomi, Bruno Giovanni Galuzzi, Francesca Servidio, Clarissa Gervasoni, Martina Nespoli, Chiara Pellizzer, Alessandro Giammona, Daniela Gaglio, Daniele Capitanio, Gloria Bertoli, Luisa Ottobrini, Alessia Lo Dico","doi":"10.1038/s41420-026-03227-3","DOIUrl":"10.1038/s41420-026-03227-3","url":null,"abstract":"<p><p>Temozolomide (TMZ) resistance remains a major obstacle in glioma treatment. Ferroptosis, an iron-dependent, lipid peroxidation-driven regulated cell death, represents a promising alternative strategy. We investigated molecular determinants of ferroptosis sensitivity in TMZ-resistant glioma, focusing on HIF-1α and oxidative stress. One TMZ-sensitive (U251) and three TMZ-resistant (T98, U118, LN18) cell lines were treated with ferroptosis inducers (Erastin, FIN56, RSL3). Viability, ROS (total and mitochondrial), lipid peroxidation, and ferroptosis-related gene/protein expression were assessed. MitoTEMPO and deferoxamine (DFX) were used to probe mitochondrial ROS and iron dependence, respectively. Integrated metabolomic-proteomic analyses and an orthotopic U118-Luc model supported in vitro findings. Ferroptosis inducers reduced viability and bypassed TMZ resistance in vitro and suppressed tumor growth in vivo with partial body-weight loss. Resistant cells displayed high HIF-1α with elevated GSH/NRF2 activity and reduced lipid peroxidation. Treatments increased oxidative stress and downregulated GPX4, xCT, FSP1, and ATF4; MitoTEMPO rescued cells, implicating mitochondrial ROS. Ferroptosis induction reduced HIF-1α expression/nuclear localization and decreased HIF-1α/VEGF/SOX2/NRF2 in tumor tissue, supporting therapeutic potential.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13572394/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338010","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":"Nitric oxide refines retinal circuit architecture independently of retinal wave dynamics.","authors":"Lais Takata Walter, Marília Inês Móvio, Guilherme Shigueto Vilar Higa, Cayo Antônio Soares de Almeida, Reza Raeisossadati, Fernando da Silva Borges, Mariana Sacrini Ayres Ferraz, Giselle Cerchiaro, Christian Schmeltzer, Sten Rüdiger, Alexandre Hiroaki Kihara","doi":"10.1038/s41420-026-03228-2","DOIUrl":"10.1038/s41420-026-03228-2","url":null,"abstract":"<p><p>How diffusible neuromodulators control neural circuit assembly remains a key open question in neuroscience. While nitric oxide (NO) is known to regulate mature synaptic plasticity, its role during development, specifically whether it shapes circuits through activity-dependent or activity-independent pathways, has not been fully understood. Here, we combine ultrasensitive electron paramagnetic resonance (EPR) spectroscopy, 4096-channel high-density multielectrode array (HD-MEA) recordings, and advanced graph-theoretical analysis to study how NO contributes to retinal network formation during a critical period of synaptogenesis. In the rat retina, nNOS expression begins at postnatal day 10 in two distinct amacrine cell subtypes, coinciding with the first detectable NO production. Acute or selective nNOS inhibition preserved the spatiotemporal features of Stage III retinal waves but significantly changed network topology, increasing network degree and density. Molecular profiling showed that nNOS blockade lowered the expression of chemical (SYN, SYP) and electrical (Cx36, Cx45) synaptic genes, disrupted their laminar distribution in vivo, and increased neurite length in primary retinal cultures without altering branching complexity. By combining ultrasensitive NO detection, large-scale electrophysiology, and mathematical network analysis, our results identify NO as a key regulator of circuit refinement that operates largely independently of the spatiotemporal dynamics of retinal waves during development. These findings reveal a molecular mechanism by which diffusible modulators shape neural networks independently of patterned activity and offer a framework for understanding how altered NO signaling might contribute to neurodevelopmental disorders characterized by impaired synaptic organization.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13572502/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338071","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":"TFCP2L1 suppresses breast cancer progression by promoting ferroptosis through direct and PI3K/AKT-mediated inhibition of GPX4.","authors":"Xiaoxiao Wang, Wei Lu, Yandi Cui, Keqiang He, Yuanzhi Bie, Shou-Dong Ye, Xiangfen Li","doi":"10.1038/s41420-026-03231-7","DOIUrl":"10.1038/s41420-026-03231-7","url":null,"abstract":"<p><p>Breast cancer is the most prevalent type of malignant tumor among women. Here, we identified transcription factor CP2-like 1 (TFCP2L1) as a suppressor of breast cancer cells. Patients with breast cancer have poorer prognoses when TFCP2L1 is expressed at low levels. Consistently, the expression of TFCP2L1 is greater in normal breast tissues and cells than in breast cancer tissues and cell lines. Gain- and loss-of-function experiments and xenograft tumor assays revealed that overexpression of TFCP2L1 significantly inhibited the proliferation and migration of breast cancer cells. Conversely, the knockdown of TFCP2L1 promoted the growth and migration of breast cancer cells. Mechanistically, TFCP2L1 suppresses breast cancer progression by inhibiting the expression of glutathione peroxidase 4 (GPX4), a key positive regulator of ferroptosis. Therefore, the addition of a ferroptosis inhibitor, Ferrostatin-1, can mediate the function of TFCP2L1 in breast cancer cells. On the other hand, high-throughput transcriptome sequencing revealed that TFCP2L1 negatively regulates the activity of the PI3K/AKT signaling pathway. The administration of SC79, an AKT activator, partially reversed the negative effects of TFCP2L1 on GPX4 transcription. Together, these findings indicate that TFCP2L1 functions partially by directly and indirectly regulating GPX4-mediated ferroptosis and may serve as a potential therapeutic target for breast cancer.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13562584/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338000","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":"How deep is deep enough? The importance of the detection limits of the CML minimal residual disease gDNA assay.","authors":"Giovanni Micheloni, Vittoria Moretti, Annalisa Frattini, Francesco Acquati, Giorgio Binelli, Clara Belotti, Chiara Francesca Longo, Lucy Costantino, Martina Milani, Tamara Intermesoli, Rolland A Reinbold, Giuseppe Montalbano, Orietta Spinelli, Roberto Valli, Giovanni Porta","doi":"10.1038/s41420-026-03221-9","DOIUrl":"10.1038/s41420-026-03221-9","url":null,"abstract":"","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13562504/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338057","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":"TRA2A negatively regulates HIV-1-induced macrophage pyroptosis by mediating TXNIP expression in an m6A-dependent manner.","authors":"Xing Tao, Jinming Su, Tongxue Qin, Xiu Chen, Rongfeng Chen, Yinlu Liao, Ran Duan, Shiyi Lai, Youjin Huang, Jinmiao Li, Li Ye, Hao Liang, Junjun Jiang","doi":"10.1038/s41420-026-03236-2","DOIUrl":"10.1038/s41420-026-03236-2","url":null,"abstract":"<p><p>Human Immunodeficiency Virus (HIV) infection remains a global health challenge, with the roles of N6-methyladenosine (m6A) RNA modification and Transformer 2 Alpha Homolog (TRA2A) in viral regulation yet to be fully elucidated; this study aimed to investigate how TRA2A-mediated m6A modification of Thioredoxin Interacting Protein (TXNIP) regulates macrophage pyroptosis during HIV-1 infection. Lentiviral-mediated knockdown and overexpression of TRA2A were employed to evaluate its effects on TXNIP expression, m6A modifications, and HIV-1 replication, while pyroptosis and inflammatory responses were assessed through LDH release assays, cytokine measurements, and analysis of the NLRP3/Caspase-1/GSDMD signaling pathway. Results showed significant downregulation of TRA2A in macrophages from HIV-1 patients, and TRA2A knockdown promoted viral replication while activating NLRP3/Caspase-1/GSDMD-mediated pyroptosis; mechanistically, TRA2A recognized m6A sites on TXNIP mRNA to reduce its stability, thereby inhibiting inflammasome activation, with these effects reversed by TRA2A overexpression or TXNIP/pyroptosis inhibitors, confirming TRA2A's critical role in balancing antiviral defense and inflammation control. Collectively, TRA2A functions as an m6A regulator to balance antiviral defense and inflammation via the TXNIP-mediated NLRP3 pathway, establishing a novel regulatory axis and highlighting TRA2A as a potential dual-target therapeutic candidate.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":"12 1","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13309537/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338096","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":"Nrf2 promotes NLRP3 inflammasome assembly and activation by Klf9-TXNIP axis.","authors":"You Zhou, Hui You, Xin-Yu Xia, Ke Zhang, Hui Jiang, Liang-Hua Liu, Hong-Ping Liu, Ming-Cai Zhao, Su-Yu He","doi":"10.1038/s41420-026-03219-3","DOIUrl":"10.1038/s41420-026-03219-3","url":null,"abstract":"<p><p>NLRP3 inflammasome activation shows a crucial role in the innate immune response that triggers inflammation. Activation is controlled by two sequential steps: a priming step, followed by an assembly step. Nrf2 has been shown to promote NLRP3 inflammasome activation; however, the underlying mechanisms remain elusive. This study identifies Nrf2 as an encourager of NLRP3 inflammasome activation. We show that Nrf2 inhibition suppresses NLRP3 inflammasome activation in macrophages, including THP-1 cells and BMDMs. In addition, Nrf2 facilitates NLRP3 inflammasome assembly. Mechanically, Nrf2 increases Klf9 expression by binding to the Klf9 promoter. Klf9 stabilizes TXNIP by deubiquitination, thereby enhancing the TXNIP-NLRP3 interaction, which is required for NLRP3 inflammasome assembly and full activation. Finally, Nrf2 deficiency exerts a protective effect and alleviates NLRP3 inflammasome activation in mouse models of DSS-induced colitis and MSU crystals-induced acute gouty arthritis. Our study reveals a novel regulatory mechanism of NLRP3 inflammasome by Nrf2 and indicates Nrf2 may be a promising target for treating NLRP3 inflammasome-driven diseases.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13572388/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338080","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":"Molecular diversity of mitochondrial autophagy receptors: context-dependent effects in human health and disease.","authors":"Ana Rožić, Mija Marinković, Ivana Novak","doi":"10.1038/s41420-026-03207-7","DOIUrl":"10.1038/s41420-026-03207-7","url":null,"abstract":"<p><p>Mitophagy receptors are central regulators of mitochondrial quality control, integrating metabolic, stress-related, and developmental cues to maintain cellular homeostasis. Accumulating evidence indicates that their dysregulation contributes to a broad spectrum of human diseases through highly context-dependent mechanisms. In cardiovascular and neurological disorders, receptor-mediated mitophagy shapes cell survival, synaptic function, stress adaptation, and tissue integrity, with both insufficient and excessive activity proving detrimental. In cancer, mitophagy receptors display dual and stage-specific roles, acting as tumor suppressors in early disease while later supporting metabolic adaptation, stemness, and therapy resistance. Metabolic diseases highlight the tissue-specific complexity of mitophagy regulation, where precise control of mitochondrial turnover is essential for insulin sensitivity, calcium signaling, and energy homeostasis. In hematological, inflammatory, and autoimmune disorders, receptor-mediated mitophagy emerges as a fundamental determinant of lineage commitment, immune cell function, and inflammatory balance. Collectively, these findings position mitophagy receptors not as uniform stress responders, but as dynamic modulators of disease progression, whose precise and context-sensitive targeting may offer novel therapeutic opportunities across diverse pathological conditions.</p>","PeriodicalId":9735,"journal":{"name":"Cell Death Discovery","volume":" ","pages":""},"PeriodicalIF":10.4,"publicationDate":"2026-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13558601/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148327351","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}