Cell Death & Disease最新文献

{"title":"ISCU-p53 axis orchestrates macrophage polarization to dictate immunotherapy response in esophageal squamous cell carcinoma.","authors":"Jialiang Luo, Xu Zhang, Zhicheng Liang, WeiTao Zhuang, Mingxin Jiang, Min Ma, Shuying Peng, Shujie Huang, Guibin Qiao, Qingyun Chen","doi":"10.1038/s41419-025-07787-7","DOIUrl":"10.1038/s41419-025-07787-7","url":null,"abstract":"<p><p>Immunological heterogeneity in esophageal squamous cell carcinoma (ESCC) poses a significant challenge to the efficacy and response to immunotherapy. In this study, we used single-cell RNA sequencing to uncover substantial heterogeneity in the tumor microenvironments (TMEs) among patients received PD-1 inhibitor with partial response (PR), stable disease (SD), and that who underwent surgery without prior therapy. Notably, tumors classified as SD demonstrated an immunosuppressive environment, characterized by a higher prevalence of M2-like macrophages and lower frequencies of T and B cells, especially PD1^highCD8⁺ T cells. These PD1^highCD8⁺ T cells were found to frequently engage with macrophages within the TMEs. Focusing on macrophages, we observed elevated expression of the Iron-Sulfur Cluster Assembly Enzyme (ISCU) in macrophages infiltrating SD tumors. ISCU was identified as a promoter of M2 macrophage polarization in a p53-dependent manner. Mechanistically, ISCU sequestrates p53 in the cytoplasm, reducing its nuclear location and relieving transcriptional repression of xCT and Arg1. Consequently, the increased expression of xCT and Arg1 modulates macrophage sensitivity to ferroptosis and the arginine metabolic pathway, thus affecting macrophage differentiation and inflammatory responses. Furthermore, inhibition of ISCU expression was found to repolarize macrophages, enhance CD8⁺ T cell cytotoxicity, and boost the efficacy of anti-PD-1 antibody. Collectively, our findings highlight the complex interplay within ESCC TMEs and suggest that targeting ISCU might be a novel strategy to reprogram the immunosuppressive TME, potentially improving immunotherapy outcomes in ESCC patients. Schematic illustration of the mechanism by which ISCU facilitates M2 macrophage polarization. ISCU interacted with p53, promoting its retention in the cytoplasm during M2 macrophage polarization. This nuclear reduction of p53 results in the upregulation of xCT and Arg1, as both are negatively regulated at the transcriptional level by p53. The increased expression of xCT and Arg1 modulates macrophage sensitivity to ferroptosis and the arginine metabolic pathway, respectively, thus affecting macrophage differentiation and inflammatory responses. The graphical abstract was created with BioRender.com.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"462"},"PeriodicalIF":8.1,"publicationDate":"2025-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144336351","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":"ARNTL-mediated INO80-DHX15 axis reprograms the glycolytic metabolism and augments the progression of endometrial carcinoma.","authors":"Lei Ye, Genyi Jiang, Yihan Sun, Bilan Li","doi":"10.1038/s41419-025-07776-w","DOIUrl":"10.1038/s41419-025-07776-w","url":null,"abstract":"<p><p>Immune evasion is a major mechanism responsible for tumor cell survival and dissemination. This study aims to explore key molecules involved in immunosuppression and metastasis of endometrial carcinoma (EC). Primary and metastatic tumors were collected from four patients with EC for array analysis. Metastatic tumors exhibited increased macrophage infiltration, while decreased CD8⁺ T cell infiltration, and aryl hydrocarbon receptor nuclear translocator-like (ARNTL) was identified as a key factor involved. High ARNTL expression was linked to poor tumor differentiation, advanced stage, and increased metastasis in another cohort of 300 EC patients. ARNTL knockout (ARNTL-KO) in EC cells reduced cell proliferation, migration, and invasion, and increased cell death in vitro, and it blocked the tumorigenicity and metastatic activity of cells in mice. The ARNTL-KO EC cells reduced the M2 polarization of macrophages and induced CD8⁺ T cell proliferation both in vitro and in vivo. ARNTL activated the transcription of INO80 complex ATPase subunit (INO80), a chromatin remodeler, which further promoted the transcription of DEAH-box helicase 15 (DHX15) through histone acetylation modifications. Overexpression of either INO80 or DHX15 increased glycolytic activity and immunosuppression in ARNTL-KO EC cells. Collectively, this study suggests that the ARNTL-mediated INO80-DHX15 axis induces glycolysis and immunosuppression during EC progression.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"463"},"PeriodicalIF":8.1,"publicationDate":"2025-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144336350","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":"PUMA reduces FASN ubiquitination to promote lipid accumulation and tumor progression in human clear cell renal cell carcinoma.","authors":"Qianqian Luo, Qi Wang, Jian Shi, Qingyang Lv, Zirui Dong, Wen Li, Yaru Xia, Jingchong Liu, Hongmei Yang","doi":"10.1038/s41419-025-07782-y","DOIUrl":"10.1038/s41419-025-07782-y","url":null,"abstract":"<p><p>While the p53 upregulated modulator of apoptosis (PUMA) is traditionally recognized for promoting cell apoptosis and enhancing chemotherapy efficacy in various cancers, its role in clear cell renal cell carcinoma (ccRCC) remains unclear due to ccRCC's chemotherapy resistance. In this study, we discover a novel oncogenic role for PUMA in ccRCC, diverging from its known apoptotic function, through assessments of public datasets, clinical tissue samples, and cell line experiments. Abnormally high expression of PUMA positively correlates with clinical stages and poor prognosis. Notably, PUMA's role in ccRCC appears to be independent of apoptosis. Instead, it facilitates tumor progression and lipid accumulation through mechanisms involving the key metabolic regulator, fatty acid synthase (FASN). Specifically, the N44-102 amino acid sequence of PUMA, distinct from the previously studied BH3 domain, is crucial for its interaction with FASN. As a mechanism, PUMA stabilizes FASN by binding to ubiquitin-specific protease 15 (USP15), reducing FASN ubiquitination and degradation, thereby forming the PUMA-USP15-FASN axis. These findings challenge the established view of PUMA's role in cancer biology. Furthermore, PUMA knockdown significantly inhibits tumor growth and enhances the sensitivity of ccRCC tumors to metabolic inhibition. These results position PUMA as a novel metabolic regulator and a potential therapeutic target in ccRCC. The combined inhibition of PUMA and FASN further supports the therapeutic potential of targeting this metabolic axis.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"460"},"PeriodicalIF":8.1,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12177072/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144324539","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":"Gap junction protein beta 5 interacts with Gαi3 to promote Akt activation and cervical cancer cell growth.","authors":"Ping Li, Jie Chen, Juan Wang, Tianbo Liu","doi":"10.1038/s41419-025-07768-w","DOIUrl":"10.1038/s41419-025-07768-w","url":null,"abstract":"<p><p>Identifying novel therapeutic targets for cervical cancer is crucial for improving patient outcomes and reducing the global burden of this disease. Gap junction protein beta 5 (GJB5) is a member of the connexin family of proteins involved in cell-to-cell communication. This study investigated GJB5's expression and functional significance in cervical cancer. Analysis of The Cancer Genome Atlas (TCGA) data demonstrated significantly increased GJB5 mRNA expression in cervical cancer tissues compared to normal cervical epithelium. Moreover, high GJB5 expression correlated with reduced overall survival and other adverse clinical outcomes. Single-cell RNA sequencing corroborated GJB5 overexpression within the malignant tumor cell population. The downregulation of GJB5 through shRNA or CRISPR/Cas9 gene knockout techniques significantly impaired the viability, proliferation, and migratory capacity of cervical cancer cells, while concurrently inducing apoptotic processes. Conversely, the forced overexpression of GJB5 resulted in enhanced malignant behaviors. Investigations into the underlying mechanisms revealed that GJB5 is integral to the activation of the Akt-mTOR (mammalian target of rapamycin) signaling pathway. GJB5 knockdown or knockout led to diminished phosphorylation of Akt and S6 kinase, whereas GJB5 overexpression correlated with increased Akt-mTOR signaling in primary human cervical cancer cells. Additionally, we identified a novel interaction between GJB5 and the Gαi3 (G alpha inhibitory protein 3), underscoring the crucial role of GJB5 in mediating Akt activation via Gαi3. In vivo studies utilizing xenograft models provided further evidence for the oncogenic function of GJB5. The knockdown of GJB5 resulted in a marked reduction in the growth of cervical cancer xenografts. Observations of proliferation arrest, inactivation of the Akt-mTOR pathway, and the induction of apoptosis were noted in GJB5-depleted cervical cancer xenograft tissues. Collectively, these findings underscore GJB5 as a key oncogenic driver in cervical cancer and indicate that targeting GJB5 could be a promising therapeutic approach for this disease.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"461"},"PeriodicalIF":8.1,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12179280/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144332531","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":"TAK1 inhibition activates pore-forming proteins to block intracellular bacterial growth through modulating mitochondria.","authors":"Wilfred López-Pérez, Roland E González-Calderón, Kazuhito Sai, Prashant Rai, Jacqueline M MacStudy, Yosuke Sakamachi, Cameron Parsons, Sophia Kathariou, Michael B Fessler, Jun Ninomiya-Tsuji","doi":"10.1038/s41419-025-07760-4","DOIUrl":"10.1038/s41419-025-07760-4","url":null,"abstract":"<p><p>Mitogen-activated protein kinase kinase kinase 7 (MAP3K7), known as TAK1, is a central mediator of intracellular host defense signaling promoting inflammatory gene expression. Hence, TAK1 is a prime target of intracellular bacterial effectors in blocking inflammatory responses. However, when TAK1 is inhibited, host cells alternatively activate multiple cell death pathways, namely caspase 8-dependent apoptosis and pyroptosis, and receptor interacting protein kinase 3 (RIPK3)-dependent necroptosis. While these pathways ultimately lead to cell death, we found that they also modulate mitochondria to produce mitochondrial reactive oxygen species (ROS). Although as cell death executors, mixed lineage kinase-like (MLKL) and gasdermins are known to form pores in the plasma membrane, we found that TAK1 inhibition translocates them to mitochondria resulting in elevated mitochondrial ROS. Ablation of both MLKL and gasdermins diminished TAK1 inhibition-induced elevation of ROS and exacerbated intracellular bacterial colonization. Our results reveal that these cell death pathways have an alternative host defense role to prevent intracellular pathogen colonization.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"456"},"PeriodicalIF":8.1,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12177065/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144324540","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":"Blocking XIAP:CASP7-p19 selectively induces apoptosis of CASP3/DR malignancies by a novel reversible small molecule.","authors":"Shih-Hsun Chen, Szu-Ying Wu, Yun-Xun Chang, En-Ning Lui, Chih-Kang Chang, Sheng-Wei Lin, Michael Hsiao, Jinn-Moon Yang, Po-Huang Liang","doi":"10.1038/s41419-025-07774-y","DOIUrl":"10.1038/s41419-025-07774-y","url":null,"abstract":"<p><p>X-linked inhibitor of apoptosis (XIAP) inhibits caspases 3, 7, and 9, thereby preventing cell apoptosis. Endogenous Second mitochondria-derived activator of caspase (Smac) competes out the binding of caspases with XIAP and causes apoptosis, so that Smac mimetics are under clinical trials for anti-cancer chemotherapy. We demonstrated by selectively alkylating caspase 7 (CASP7) to release the active CASP7 for killing the drug-resistant cancer cells with accumulated XIAP:CASP7 resulted from caspase-3 down-regulation (CASP3/DR). However, finding a reversible inhibitor of the protein-protein interaction (PPI) poses a significant challenge. Here, we identified a reversible XIAP:CASP7 inhibitor, 643943, through a multiple-mode virtual screening strategy. In vitro experiments revealed that 643943 bound to CASP7, released the linker-BIR2 domain of XIAP, and activated the caspase. Removing an essential hydroxyl group on 643943 or replacing the OH-interacting Asp93 on CASP7 caused loss of 643943 cytotoxicity, revealing the binding mode. This compound thus selectively killed MCF-7 and other CASP3/DR triple-negative breast cancer cell lines, but not the cancer and normal cell lines expressing higher levels of CASP3 in vitro and in vivo. Moreover, 643943 overcame chemoresistance via down-regulating β-catenin and its associated ABC transporters in paclitaxel-resistant MCF-7 cells. Our studies not only serve as a proof-of-concept for using XIAP:CASP7 as a drug target, but also provide the first reversible XIAP:CASP7 inhibitor for cancer therapy of CASP3/DR malignancies.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"459"},"PeriodicalIF":8.1,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12177060/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144324536","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":"PI3K-dependent GAB1/Erk phosphorylation renders head and neck squamous cell carcinoma sensitive to PI3Kα inhibitors.","authors":"Xu Zhang, Jiao Xu, Xuan Wang, Lan Xu, Xi Zhang, Yi Wang, Shujuan Jiang, Yixiang Zhang, Jian Ding, Chen Qing, Linghua Meng","doi":"10.1038/s41419-025-07767-x","DOIUrl":"10.1038/s41419-025-07767-x","url":null,"abstract":"<p><p>The hyperactivation of the PI3K pathway in head and neck squamous cell carcinoma (HNSCC) suggests that targeting PI3K is a potential therapeutic strategy. CYH33 is a novel PI3Kα-selective inhibitor discovered by our group, which is currently undergoing a phase I clinical trial (NCT03544905) for the treatment of advanced solid tumors including HNSCC. However, there is an urgent need to elucidate its mechanism of action and improve its efficacy against HNSCC. In this study, we found that CYH33 displayed promising but variable therapeutic activity against HNSCC. Inhibition of PI3K/Akt pathway by CYH33 was not sufficient for its activity against HNSCC. Tandem-Mass-Tag (TMT) phosphoproteomics were performed to reveal comprehensive regulation of kinome by CYH33. Particularly, attenuation of Erk phosphorylation was associated with the sensitivity of HNSCC cells to CYH33. Mechanistically, inhibition of PI3K by CYH33 blocked the PIP3 production and attenuated the membrane localization and phosphorylation of GAB1, resulting in reduced Erk phosphorylation and ultimately inhibition of cell proliferation in sensitive HNSCC cells. Meanwhile, activation of EGFR induced GAB1 phosphorylation independent of PI3K in HNSCC cells. Concurrent inhibition of EGFR synergistically potentiated the activity of CYH33 against HNSCC. These findings revealed the insight mechanism of CYH33 against HNSCC and provided rational combination regimen for HNSCC treatment.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"457"},"PeriodicalIF":8.1,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12177050/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144324538","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":"N6-methyladenosine-modified GPX2 impacts cancer cell stemness and TKI resistance through regulating of redox metabolism.","authors":"Xu Yang, Long Yu, Miaomiao Shao, Huiling Yang, Kangwei Qi, Gaofei He, Lanxin Wang, Di Kong, Jianxin Gu, Xiaolin Xu, Lan Wang","doi":"10.1038/s41419-025-07764-0","DOIUrl":"10.1038/s41419-025-07764-0","url":null,"abstract":"<p><p>As a predominant oncogenic driver in non-small cell lung cancer (NSCLC), EGFR frequently undergoes amplification or mutation, with EGFR-tyrosine kinase inhibitors (EGFR-TKIs) like gefitinib and erlotinib constituting frontline therapy for advanced EGFR-mutant cases. However, both primary and acquired resistance significantly limit clinical efficacy. Here, we revealed that glutathione metabolic pathway controlled by glutathione peroxidase GPX2 was abnormally activated in gefitinib-resistant A549 and HCC827-GR cell lines. Mechanistically, GPX2 triggers Hedgehog signaling activation through releasing GLI transcriptional regulator, promoting cancer stem cell (CSC) characteristics and TKI resistance. Notably, N6-methyladenosine (m⁶A) modification on GPX2 mRNA mediated by METTL14 diminished its stability. In vivo, GPX2 deletion constrained glutathione metabolism and boosted the effectiveness of TKI in cell line-derived xenograft models. Collectively, these findings demonstrate that GPX2 serves as a positive regulator of both primary and acquired EGFR-TKI resistance and could be a promising therapeutic target for precise treatment of NSCLC.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"458"},"PeriodicalIF":8.1,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12177039/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144324537","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":"Repurposing MDM2 inhibitor RG7388 for TP53-mutant NSCLC: a p53-independent pyroptotic mechanism via ROS/p-p38/NOXA/caspase-3/GSDME axis.","authors":"Gaoyan Tang, Xuelei Cao, Jiaqi Chen, Fu Hui, Na Xu, Yiqing Jiang, Hongmin Lu, Haifeng Xiao, Xiuming Liang, Mingzhe Ma, Yu Qian, Dongli Liu, Zhenlu Wang, Shuzhen Liu, Guohua Yu, Lei Sun","doi":"10.1038/s41419-025-07770-2","DOIUrl":"10.1038/s41419-025-07770-2","url":null,"abstract":"<p><p>Non-small cell lung cancer (NSCLC) is highly malignant with limited treatment options, largely due to the inherent tumoral heterogeneity and acquired resistance towards chemotherapy and immunotherapy. RG7388, a known MDM2 inhibitor, exhibited anticancer activity in TP53-wild-type (TP53^WT) NSCLC by triggering the p53/PUMA axis-dependent apoptosis. However, our study uncovered previously unrecognized p53-independent anticancer effects of RG7388 in TP53-mutant (TP53^mutant) NSCLC, although the underlying mechanisms remained elusive. Here, we demonstrated that RG7388 specifically induced the NOXA/caspase-3 axis-dependent apoptosis and gasdermin E (GSDME)-mediated secondary pyroptosis in TP53^mutant NSCLC, as validated through in silico analyses and multiple biological assays. Mechanically, we identified reactive oxygen species (ROS) as the critical mediator in NOXA upregulation and p38 MAPK pathway activation in RG7388 treated TP53^mutant NSCLC. This was further supported by the use of ROS scavengers, N-acetylcysteine (NAC), and Ferrostatin-1 (Fer-1), which attenuated these effects. Pharmacologic inhibition of p38 MAPK signaling by SB203580 rescued RG7388-induced ROS-dependent NOXA accumulation and subsequent apoptosis and pyroptosis, highlighting the central role of the ROS/phosphorylated p38 MAPK (p-p38)/NOXA/caspase-3 axis in RG7388-induced TP53^mutant NSCLC cell death. Our findings revealed a novel mechanism for selectively targeting mutant p53-derived cancer through ROS/p-p38-mediated NOXA accumulation, offering potential therapeutic implications given the current lack of direct mutant p53 targeting strategies in cancer. Furthermore, immunohistochemical (IHC) analysis of an NSCLC tissue microarray confirmed a strong positive correlation between p-p38 and NOXA expression. Clinical data analysis further suggested that the p-p38/NOXA axis might be a potential prognostic biomarker for overall survival (OS) in NSCLC patients.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"452"},"PeriodicalIF":8.1,"publicationDate":"2025-06-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12170848/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144309613","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: Mutant Runx2 regulates amelogenesis and osteogenesis through a miR-185-5p-Dlx2 axis.","authors":"Huaiguang Chang, Yue Wang, Haochen Liu, Xu Nan, Singwai Wong, Saihui Peng, Yajuan Gu, Hongshan Zhao, Hailan Feng","doi":"10.1038/s41419-025-07762-2","DOIUrl":"10.1038/s41419-025-07762-2","url":null,"abstract":"","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"455"},"PeriodicalIF":8.1,"publicationDate":"2025-06-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12174338/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144315968","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}