Cell Death & Disease最新文献

{"title":"Unravelling the impact of the chromobox proteins in human cancers.","authors":"Shabana Noreen, Nicla Simonelli, Rosaria Benedetti, Vincenzo Carafa, Michele Grieco, Concetta Ambrosino, Carmela Dell'Aversana, Angela Nebbioso, Mariarosaria Conte, Nunzio Del Gaudio, Lucia Altucci","doi":"10.1038/s41419-025-07585-1","DOIUrl":"10.1038/s41419-025-07585-1","url":null,"abstract":"<p><p>Chromobox (CBX) proteins play a crucial role in regulating epigenetic processes. They are extensively involved in various biological processes, including embryonic development, stem cell maintenance, cell proliferation and apoptosis control. The disruption and malfunction of CBXs in cancer typically results in the interference or abnormal activation of developmental pathways, which facilitate the onset, growth, and advancement of cancer. This review initially introduces the physiological properties and functions of the CBXs. Subsequently, it examines the involvement of CBXs in different cancer types. Cancer hallmarks driven by CBXs are mediated through multiple mechanisms, including changes in gene expression patterns, epigenetic dysregulation of chromatin control, disruption of intracellular signaling and alterations in cell metabolism. The study also highlights novel potential anticancer therapeutics targeting CBXs in cancer. In this review we provide novel perspectives and a solid foundation for future investigations on CBXs as promising therapeutic targets for cancer treatment.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"238"},"PeriodicalIF":8.1,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11965368/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143771216","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":"Mechanical sensing protein PIEZO1 controls osteoarthritis via glycolysis mediated mesenchymal stem cells-Th17 cells crosstalk.","authors":"Yikun Zhou, Mingzhao Li, Shuai Lin, Zilu Zhu, Zimeng Zhuang, Shengjie Cui, Liujing Chen, Ran Zhang, Xuedong Wang, Bo Shen, Chider Chen, Ruili Yang","doi":"10.1038/s41419-025-07577-1","DOIUrl":"10.1038/s41419-025-07577-1","url":null,"abstract":"<p><p>Aberrant mechanical stimuli can cause tissue attrition and activate mechanosensitive intracellular signaling, impacting the progression of osteoarthritis (OA). However, the precise relationship between mechanical loading and bone metabolism remains unclear. Here, we present evidence that Piezo1 senses the mechanical stimuli to coordinate the crosstalk between mesenchymal stem cells (MSCs) and T helper 17 (Th17) cells, leading to the deterioration of bone and cartilage in osteoarthritis (OA). Mechanical loading impaired the property of MSCs by inhibiting their osteo-chondrogenic differentiation and promoting inflammatory signaling to enhance Th17 cells. Mechanistically, mechanical stimuli activated Piezo1, thereby facilitating Ca²⁺ influx which upregulated the activity of Hexokinase 2(HK2), the rate-limiting enzyme of glycolysis. The resultant increase in glycolytic activity enhanced communication between MSCs and T cells, thus promoting Th17 cell polarization in a macrophage migration inhibitory factor (MIF) dependent manner. Functionally, Wnt1cre; Piezo1^fl/fl mice reduced bone and cartilage erosion in the temporomandibular joint condyle following mechanical loading compared to control groups. Additionally, we observed activated Piezo1 and HK2-mediated glycolysis in patients with temporomandibular joint OA, thereby confirming the clinical relevance of our findings. Overall, our results provide insights into how Piezo1 in MSCs coordinates with mechano-inflammatory signaling to regulate bone metabolism. The schema shows that mechanical sensing protein PIEZO1 in MSCs controls osteoarthritis via glycolysis mediated MSCs and Th17 cells crosstalk in a MIF dependent manner.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"231"},"PeriodicalIF":8.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11961634/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143762977","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":"SIRT7-mediated NRF2 deacetylation promotes antioxidant response and protects against chemodrug-induced liver injury.","authors":"Tingzi Yu, Cong Ding, Jinying Peng, Gaoshuang Liang, Yongyi Tang, Jinqiu Zhao, Zhuan Li","doi":"10.1038/s41419-025-07549-5","DOIUrl":"10.1038/s41419-025-07549-5","url":null,"abstract":"<p><p>NRF2 has been recognized as a central hub that neutralizes ROS and restores intracellular redox balance. In addition to KEAP1 mediated ubiquitin-proteasome degradation, post-translational modifications of NRF2 are critical for regulating its nuclear translocation and activation but precise mechanisms underly this regulation remain elusive. In this study, we found that SIRT7 was sufficient and essential for NRF2 nuclear localization and activation. Knockdown of SIRT7 significantly impaired intercellular ROS homeostasis and increased apoptosis in response to oxidative stress including chemodrug treatment. SIRT7 interacted with NRF2 and induced its deacetylation, by which inhibited binding of NRF2 to KEAP1, enhanced NRF2 protein stability and promoted its nuclear translocation. SIRT7 induced NRF2 deacetylation at K443 and K518 sites. Lysine-arginine mutations of these sites (2KR NRF2) significantly reduced KEAP1/NRF2 binding, increased NRF2 nuclear translocation and target gene expression, decreased intercellular ROS level, whereas lysine-glutamine (2KQ) mutant showed similar subcellular localization and functions with WT. Knockdown SIRT7 in hepatocyte exacerbated Oxaliplatin (Oxa) induced hepatic injury and inflammation. While AAV8-NRF2-mediated hepatic NRF2 overexpression or NRF2 agonist significantly prevented Oxa-induced elevation of ALT levels, sinusoidal dilatation and inflammation in SIRT7^HKO mice. Our data thus uncovered previously unidentified role of SIRT7 in modulating NRF2 nuclear localization and activation via deacetylation. Activating SIRT7 might offer protection against chemodrug-induced liver injury.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"232"},"PeriodicalIF":8.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11961749/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143763053","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":"PLA2G7 promotes immune evasion of bladder cancer through the JAK-STAT-PDL1 axis.","authors":"Ding Peng, Wuping Yang, Tianyu Tang, Anbang He, Xin Xu, Taile Jing, Dan Xia","doi":"10.1038/s41419-025-07593-1","DOIUrl":"10.1038/s41419-025-07593-1","url":null,"abstract":"<p><p>Targeting immune checkpoints such as Programmed death ligand-1 (PD-L1) and Programmed cell death 1 (PD-1) has been approved for treating bladder cancer and shows promising clinical benefits. However, the relatively low response rate highlights the need to seek an alternative strategy to traditional PD-1/PD-L1 targeting immunotherapy. In this study, we found that PLA2G7 is significantly elevated in bladder cancer and correlates with worse prognosis. In vitro experiments demonstrated that knockdown of PLA2G7 does not significantly affect the proliferation, migration, and invasion of bladder cancer cells. Flow cytometry detection, as well as protein and RNA detection, showed that knockdown of PLA2G7 significantly inhibits PD-L1 expression and suppresses the growth of transplanted tumors by promoting CD8 + T-cell infiltration. Further experiments showed that PLA2G7 regulates the JAK-STAT pathway to promote PD-L1 expression by upregulating the phosphorylation of STAT1 and STAT3. Meanwhile, results from syngeneic mouse models indicated that PLA2G7 suppression and anti-CTLA4 therapy have synergistic effects on tumor burden and mouse survival. In addition, we found that ETS1 promotes PLA2G7 overexpression in bladder cancer cells. In summary, our findings provide a novel immunotherapeutic strategy against bladder cancer through targeting the ETS1-PLA2G7-STAT1/STAT3-PD-L1 axis.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"234"},"PeriodicalIF":8.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11962123/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143763005","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":"Targeting METTL3 mitigates venetoclax resistance via proteasome-mediated modulation of MCL1 in acute myeloid leukemia.","authors":"Chang-Qing Jiao, Chen Hu, Meng-Hua Sun, Yan Li, Chao Wu, Fei Xu, Lei Zhang, Fu-Rong Huang, Jun-Jie Zhou, Ji-Fei Dai, Min Ruan, Wen-Chao Wang, Qing-Song Liu, Jian Ge","doi":"10.1038/s41419-025-07560-w","DOIUrl":"10.1038/s41419-025-07560-w","url":null,"abstract":"<p><p>Venetoclax, a selective BCL2 inhibitor, is extensively utilized in clinical settings for the treatment of acute myeloid leukemia (AML). However, its efficacy is often compromised by the development of drug resistance. Hence, identification of potential venetoclax combination treatment strategies is imperative to overcome this acquired resistance. In this study, we discovered that inhibition of METTL3 can synergistically enhance the anti-leukemic efficacy of venetoclax, and is capable of overcoming venetoclax resistance in in vivo experiments and various venetoclax resistance models. Mechanistic study revealed that STM2457 augmented venetoclax activity by downregulating MCL1 and MYC, thereby increasing apoptosis in leukemia cells induced by venetoclax. Further investigation demonstrated that STM2457 promotes the ubiquitination and subsequent protein degradation of MCL1 primarily through pharmaceutically targeting METTL3. Moreover, through molecular docking-based virtual screening, we identified isoliquiritigenin as a potential novel small molecule natural product targeting METTL3, which exhibited potential effects as an anti-leukemic agent.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"233"},"PeriodicalIF":8.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11962166/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143763091","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":"Immune evasion mechanisms in early-stage I high-grade serous ovarian carcinoma: insights into regulatory T cell dynamics.","authors":"Joanna Mikulak, Sara Terzoli, Paolo Marzano, Valentina Cazzetta, Giampaolo Martiniello, Rocco Piazza, Maria Estefania Viano, Domenico Vitobello, Rosalba Portuesi, Fabio Grizzi, Mohamed A A A Hegazi, Barbara Fiamengo, Gianluca Basso, Lara Parachini, Laura Mannarino, Maurizio D'Incalci, Sergio Marchini, Domenico Mavilio","doi":"10.1038/s41419-025-07557-5","DOIUrl":"10.1038/s41419-025-07557-5","url":null,"abstract":"<p><p>The mechanisms driving immune evasion in early-stage I high-grade serous ovarian carcinoma (HGSOC) remain poorly understood. To investigate this, we performed single-cell RNA-sequencing analysis. Our findings revealed a highly immunosuppressive HGSOC microenvironment, characterized by abundant infiltration of regulatory T cells (Tregs). Trajectory analysis uncovered differentiation pathways of naïve Tregs, which underwent either activation and proliferation or transcriptional instability. The predicted Treg-cell interaction network, including crosstalk within tumor cells, facilitates Treg mobility and maturation while reinforcing their immunosuppressive function and persistence in the tumor. Moreover, their interactions with immune cells likely inhibit CD8 T cells and antigen-presenting cells, supporting tumor immune escape. Additionally, more immunogenic tumor conditions, marked by IFNγ production, may contribute to Treg destabilization. Our findings underscore the pivotal role of Tregs in early immune evasion of HGSOC and provide insights into potential therapeutic strategies targeting their activity and differentiation fate.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"229"},"PeriodicalIF":8.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11958665/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143751384","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":"The absence of Pitx3 results in postnatal loss of dopamine neurons and is associated with an increase in the pro-apoptotic Bcl2 factor Noxa and cleaved caspase 3.","authors":"Willemieke M Kouwenhoven, Edward J Robinson, Daniek Hamberg, Lars von Oerthel, Marten P Smidt, Lars P van der Heide","doi":"10.1038/s41419-025-07552-w","DOIUrl":"10.1038/s41419-025-07552-w","url":null,"abstract":"<p><p>Mesodiencephalic dopamine neurons (mdDA) of the substantia nigra pars compacta (SNc) and ventral tegmental area (VTA) play critical roles in regulating movement and motivation. Pitx3 is an essential transcription factor required for proper embryonic development and terminal differentiation of mdDA neurons. Although Pitx3 is expressed in every mdDA neuron, its ablation results only in the absence of the SNc, not the VTA. The developmental stage at which the loss of SNc first becomes apparent, as well as the underlying mechanism, remains elusive. Here, we demonstrate, using a Pitx3 knockout GFP knock-in mouse model, that this loss does not occur during embryogenesis but rather postnatally. Quantification of GFP expression revealed a significant reduction in the total number of dopamine neurons at postnatal day 3, but not at embryonic day 14.5, 155, and 18.5. Mechanistically this reduction is accompanied by an increase in the number of cleaved caspase 3-positive GFP neurons, suggesting apoptosis. In addition, RT-PCR performed on isolated GFP neurons, one day before the loss of dopamine neurons revealed a notable elevation in the expression of the pro-apoptotic BH3-only factor Noxa. Overexpression of Noxa in dopaminergic MN9D cells dose-dependently increases the level of cleaved caspase 3 and the number of propidium iodide-positive cells, indicating that Noxa expression is sufficient to induce cell death in dopamine cells. Additionally, Noxa expression in MN9D cells, combined with a Bax-inhibiting peptide, reduces the number of cleaved caspase 3-positive and propidium iodide-positive cells, further supporting apoptosis as the mechanistic form of cell death. Overall, our study provides insights into the cell death machinery implicated in the loss of dopamine neurons, which may hold relevance for diseases affected by the loss of dopamine neurons such as Parkinson's disease, where this is a hallmark feature.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"230"},"PeriodicalIF":8.1,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11962142/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143763097","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":"Leveraging glycosylation for early detection and therapeutic target discovery in pancreatic cancer.","authors":"Tomasz Pienkowski, Katarzyna Wawrzak-Pienkowska, Anna Tankiewicz-Kwedlo, Michal Ciborowski, Krzysztof Kurek, Dariusz Pawlak","doi":"10.1038/s41419-025-07517-z","DOIUrl":"10.1038/s41419-025-07517-z","url":null,"abstract":"<p><p>Pancreatic cancer (PC) remains one of the most lethal malignancies, primarily due to late-stage diagnosis, limited biomarker specificity, and aggressive metastatic potential. Recent glycoproteomic studies have illuminated the crucial role of glycosylation in PC progression, revealing altered glycosylation patterns that impact cell adhesion, immune evasion, and tumor invasiveness. Biomarkers such as CA19-9 remain the clinical standard, yet limitations in sensitivity and specificity, especially in early disease stages, necessitate the exploration of alternative markers. Emerging glycoproteins-such as mesothelin, thrombospondin-2, and glycan modifications like sialyl-Lewis x-offer diagnostic promise when combined with CA19-9 or used in profiling panels. Furthermore, therapeutic strategies targeting glycosylation processes, including sialylation, and fucosylation, have shown potential in curbing PC metastasis and enhancing immune response. Translational platforms, such as patient-derived xenografts and advanced in vitro models, are pivotal in validating these findings and assessing glycosylation potential therapeutic impact. Continued exploration of glycosylation-driven mechanisms and biomarker discovery in PC can significantly advance early detection and treatment efficacy, offering new hope in the management of this challenging disease.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"227"},"PeriodicalIF":8.1,"publicationDate":"2025-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11958638/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143751386","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":"Modulation of CREB3L2-ATF4 heterodimerization via proteasome inhibition and HRI activation in Alzheimer's disease pathology.","authors":"Krystal Herline-Killian, Michaela M Pauers, Jessica E Lipponen, Michael A Zrzavy, Cláudio Gouveia Roque, Ethan P McCurdy, Kyung Min Chung, Ulrich Hengst","doi":"10.1038/s41419-025-07586-0","DOIUrl":"10.1038/s41419-025-07586-0","url":null,"abstract":"<p><p>Alzheimer's disease (AD) pathology includes transcriptional changes in the neurons, which are in part caused by the heterodimerization of two stress response transcription factors, CREB3L2 and ATF4. We investigated the role of proteasome inhibition and the eIF2α-kinase HRI in the formation of CREB3L2-ATF4 in neurons exposed to soluble oligomeric Aβ₄₂. While HRI activation increased ATF4 expression, it decreased CREB3L2 and CREB3L2-ATF4 levels. Proteasome inhibition, induced by Aβ₄₂, leads to increased levels of both transcription factors in the nucleus. These findings suggest that CREB3L2 levels are normally kept low due to rapid degradation, but proteasome inhibition in response to Aβ₄₂ disrupts this balance, increasing CREB3L2 and heterodimer levels. Activation of HRI not only reduced CREB3L2 and heterodimer levels but also prevented the transcriptional dysregulation of a CREB3L2-ATF4 target, SNX3. Our results suggest that manipulating the HRI pathway during proteasome inhibition could help restore normal gene expression in the context of AD-related protein accumulation.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"225"},"PeriodicalIF":8.1,"publicationDate":"2025-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11958753/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143751388","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":"NUB1 reduction promotes PCNA-mediated tumor growth by disturbing the PCNA polyubiquitination/NEDDylation in hepatocellular carcinoma cells.","authors":"Dongnian Du, Wenming Zhang, Dandan Zhang, Lingpeng Liu, Jiajuan Li, Zehao Chen, Xuzhe Yu, Miao Ye, Wei Wang, Zijing Li, Jianghua Shao","doi":"10.1038/s41419-025-07567-3","DOIUrl":"10.1038/s41419-025-07567-3","url":null,"abstract":"<p><p>Negative regulator of ubiquitin-like protein 1 (NUB1), an inhibitor of neural precursor cells expressed developmentally downregulated 8 (NEDD8), is implicated in tumor growth. However, the expression of NUB1 in hepatocellular carcinoma (HCC) and its effects on HCC growth remain unclear. In this study, our findings revealed reduced NUB1 protein expression in HCC tissues and cells, leading to increased proliferating cell nuclear antigen (PCNA) protein stability through upregulating NEDD8 to promote HCC cell growth. Mechanistically, NUB1 reduction upregulated NEDD8 to promote PCNA NEDDylation at lysine 164 (Lys164), in turn, antagonized PCNA K48-linked polyubiquitination, thereby increasing the stability of PCNA in HCC cells. Finally, the results of the in vitro and in vivo experiments revealed that the NEDDylation inhibitor TAS4464 could inhibit PCNA NEDDylation to decrease PCNA protein expression, thereby suppressing HCC cell growth. Collectively, our results identified NUB1 as a negative regulator of HCC proliferation and confirmed that PCNA NEDDylation promotes PCNA protein stability by antagonizing PCNA polyubiquitination. This study provides a new perspective on the specific mechanism of HCC growth. It expands our understanding of the role of NEDDylation in the regulation of substrate proteins and their functions.</p>","PeriodicalId":9734,"journal":{"name":"Cell Death & Disease","volume":"16 1","pages":"228"},"PeriodicalIF":8.1,"publicationDate":"2025-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11958677/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143751390","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}