Oncogenesis最新文献

{"title":"Adaptation of redox metabolism in drug-tolerant persister cells is a vulnerability to prevent relapse in pancreatic cancer.","authors":"Nadine Abdel Hadi, Gabriela Reyes-Castellanos, Tristan Gicquel, Scarlett Gallardo-Arriaga, Emma Cosialls, Emeline Boet, Jean-Emmanuel Sarry, Rawand Masoud, Juan Iovanna, Alice Carrier","doi":"10.1038/s41389-025-00591-0","DOIUrl":"10.1038/s41389-025-00591-0","url":null,"abstract":"<p><p>Pancreatic Ductal Adenocarcinoma (PDAC) remains a major unresolved disease because of its remarkable therapeutic resistance. Even patients who respond to initial therapy experience relapse in most cases. The mechanisms underlying therapy-acquired resistance supporting relapse are poorly understood. In this study, we aimed to determine the metabolic features of PDAC during relapse, specifically adaptations of mitochondrial oxidative metabolism. We used preclinical PDAC mouse models (patient-derived xenografts and murine syngeneic allografts) that present regression under initial chemotherapeutic treatment but relapse after a certain time. Relapsed tumors were analyzed ex vivo by flow cytometry to measure mitochondrial and redox characteristics. Molecular mechanisms were investigated by quantification of ATP and antioxidants levels, bulk RNA-sequencing and RT-qPCR. We show increased mitochondrial mass, ATP levels, mitochondrial superoxide anions, and total ROS levels, in relapsed compared to control tumors in both models; mitochondrial membrane potential is increased in the xenografts model only. These metabolic features are also observed in tumors during treatment-induced regression and at relapse onset. At the molecular level, antioxidant defenses are increased in relapsed tumors and during treatment. These data suggest that metabolic adaptations occurring during treatment-induced regression may favor the survival of drug-tolerant persister (DTP) cells, which persist during the subsequent minimal residual disease and are responsible for cancer relapse. Finally, the combined treatment of arsenic trioxide (ROS inducer) and buthionine sulfoximine (glutathione synthesis inhibitor) is able to completely prevent relapse in PDAC xenografts. In conclusion, redox metabolism is a vulnerability of pancreatic DTP cancer cells that can be targeted to prevent relapse.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"48"},"PeriodicalIF":6.4,"publicationDate":"2025-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12690124/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145715346","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting mitochondrial phosphatidylethanolamine alters mitochondrial metabolism and proliferation in hepatocellular carcinoma.","authors":"Melina C Mancini, Cameron P McCall, Robert C Noland, Wagner S Dantas, Timothy D Heden","doi":"10.1038/s41389-025-00593-y","DOIUrl":"10.1038/s41389-025-00593-y","url":null,"abstract":"<p><p>Mitochondrial metabolism is crucial for hepatocellular carcinoma (HCC) to thrive. Although phospholipids modulate mitochondrial metabolism, their impact on metabolism in HCC remains unknown. Here we report that the mitochondrial phospholipidome is unaltered in HCC mitochondria, suggesting HCC maintain their mitochondrial phospholipidome to enable efficient metabolism and promote thriftiness. Consistent with this, silencing phosphatidylserine decarboxylase (PISD), the inner mitochondrial membrane protein that generates mitochondrial phosphatidylethanolamine (PE), in HEPA1-6 cells impairs mitochondrial metabolism of fatty acid and glucose-derived substrates and reduces electron transport chain I and IV abundance. Moreover, PISD deficiency increased mitochondrial superoxide generation and altered mitochondria dynamics by augmenting mitochondrial fission, mitophagy, and mitochondrial extracellular efflux. Despite compensatory increases in anaerobic glycolysis and peroxisome fat oxidation, mitochondrial PE deficiency reduced DNA synthesis and cell proliferation, effects associated with reduced mTOR signaling and peptide levels. We conclude that targeting mitochondrial PE synthesis may be a viable therapy to slow HCC progression.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":" ","pages":"3"},"PeriodicalIF":6.4,"publicationDate":"2025-12-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12811616/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145708493","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"CD9, a tetraspanin in cancer: biology and therapeutic promise in acute leukemia.","authors":"Océane Guého, Elie Cousin, Jérémie Rouger-Gaudichon, Anne-Gaëlle Rio, Sébastien Corre, Virginie Gandemer, Frédéric Mazurier","doi":"10.1038/s41389-025-00590-1","DOIUrl":"10.1038/s41389-025-00590-1","url":null,"abstract":"<p><p>Tetraspanins are transmembrane proteins that organize into functional structures known as tetraspanin-enriched microdomains, where they coordinate interactions with key partner proteins and modulate cellular processes such as adhesion, signaling, and motility. Among them, CD9 is a widely expressed member, also recognized as a classical marker of exosomes. Beyond its role in development and tissue homeostasis, CD9 has emerged as a modulator of the crosstalk between cancer cells and their microenvironment. It can contribute to processes such as cell migration, invasion, and resistance to therapy. Mechanistically, CD9 interacts with many partners including integrins, metalloproteinases, and signaling receptors to influence cell behavior. However, its functional contribution to tumor progression remains controversial. While CD9 expression is associated with enhanced dissemination in certain cancers, it appears to restrain motility and invasion in others. This likely reflects the complexity of its context-dependent functions, influenced by cell type, microenvironmental cues, and molecular partners. A deeper understanding of the regulatory mechanisms is therefore essential. In this review, we overview the tetraspanin family and summarize current knowledge on CD9 regulation and function across cancers, with a focus on leukemia. While its role in tumorigenesis remains debated, CD9 is a reliable biomarker of leukemic cells and can be used for diagnosis and MRD monitoring in acute lymphoblastic and myeloid leukemia, particularly in patients lacking molecular markers. We also discuss emerging therapeutic strategies that aim to target CD9 in cancer. CD9 gene regulation in cancer, and biological implication in acute lymphoblastic leukemia. Created with BioRender.com.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"47"},"PeriodicalIF":6.4,"publicationDate":"2025-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12680759/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145687743","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Stabilization of FASN by USP5-mediated deubiquitination promotes hepatocellular carcinoma progression.","authors":"Qinliang Fang, Changhong Luo, Yuyan Lu, Xijun Chen, Ping Zhan, Qin Yao, Huita Wu, Fuqiang Wang, Zhenyu Yin, Chengrong Xie","doi":"10.1038/s41389-025-00589-8","DOIUrl":"10.1038/s41389-025-00589-8","url":null,"abstract":"<p><p>The deubiquitinating enzyme Ubiquitin specific peptidase 5 (USP5) has attracted substantial notice for its vital role in cancer progression. However, the USP5-mediated deubiquitination of corresponding protein substrates and its functional role in hepatocellular carcinoma (HCC) have not been fully investigated. Here, we demonstrated that USP5 expression was significantly elevated in HCC tissues. The overexpression of USP5 was closely associated with larger tumor sizes, more satellite nodules and tumor emboli, and predicted unfavorable clinical outcome in HCC patients as well. Functionally, USP5 facilitated cell proliferation, migration, and invasion, and induced lipid accumulation in vitro, along with enhanced tumor growth in vivo. Moreover, knockdown of USP5 expression showed a profound effect on lipidomic profiling, specially reduced the content of palmitic acid (PA). Treatment of PA could partially rescue the suppression of HCC mediated by USP5 knockdown. Further mechanistic investigation uncovered that Fatty acid synthase (FASN), the crucial enzyme catalyzing PA synthesis, was a downstream target of USP5. USP5 interacted with FASN, repressing the ubiquitination modification of FASN and preventing its degradation. Notably, the positive correlation between USP5 and FASN expression in HCC tissues was observed, and USP5 exerted oncogenic effects partly via FASN. Our findings revealed that USP5 promotes HCC progression through deubiquitinating FASN, and targeting the USP5-FASN-PA axis could potentially serve as a strategic approach for the therapy of HCC.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"46"},"PeriodicalIF":6.4,"publicationDate":"2025-11-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12663548/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145637112","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"RNA m5C methylation in cancer: mechanisms and biological impact.","authors":"Zhenyu Guan, Wendong Li, Yuting He, Wenzhi Guo","doi":"10.1038/s41389-025-00587-w","DOIUrl":"10.1038/s41389-025-00587-w","url":null,"abstract":"<p><p>RNA modification, a prominent epigenetic mechanism, has been implicated in regulating RNA function, stability, processing, and interactions, including pseudouridylation, acetylation, and methylation. Recent evidence highlights that 5-methylcytosine (m5C) influences key cellular processes such as proliferation, differentiation, apoptosis, and stress responses by modulating RNA stability, translation, transcription, nuclear export, and cleavage. This review consolidates current insights into the role and mechanisms of m5C methylation across various tumor types, underscoring its pivotal involvement in post-transcriptional regulation and its profound effects on gene expression, cellular dynamics, and tumor biology. The mechanisms through which m5C methylation impacts tumor progression, including modulation of glucose and iron metabolism, as well as resistance to therapeutic agents, are also discussed. Finally, the review identifies critical future research avenues, focusing on elucidating the underlying mechanisms, developing targeted therapies, and advancing personalized medicine approaches to leverage m5C methylation in cancer treatment.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"44"},"PeriodicalIF":6.4,"publicationDate":"2025-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12639029/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145573912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ACSL6 modulates docosahexaenoic acid-induced cytotoxicity to potentiate chemotherapy response in colorectal and breast cancer.","authors":"I-Sung Chen, Chi-Che Hsieh, Chun-Chun Li, You-Lin Wei, Chao-Chun Cheng, Sheng-Wei Feng, Hsin-Lun Lee, Nai-Jung Chiang, Che-Hung Shen, Hui-Ping Hsu","doi":"10.1038/s41389-025-00588-9","DOIUrl":"10.1038/s41389-025-00588-9","url":null,"abstract":"<p><p>Docosahexaenoic acid (DHA), an omega-3 polyunsaturated fatty acid, exhibits anticancer properties by modulating cell membrane composition, inducing oxidative stress, and triggering ferroptosis. Acyl-CoA synthetase long chain family member 6 (ACSL6) catalyzes DHA activation, yet its role in tumor growth and tumor sensitivity to DHA treatment remains unclear. We characterized the role of ACSL6 in regulating cell growth and DHA sensitivity in vitro cancer cells and in vivo xenograft tumors. ACSL6 expression was positively associated DHA sensitivity and enhanced chemotherapy efficacy in both colorectal and breast cancer cell lines, as well as with improved responsiveness to standard treatments in patients with these cancers. ACSL6 suppressed cell growth, inhibited AKT/ERK signaling, reduced ATP production, and activated AMPK signaling, supporting its tumor-suppressive role. Importantly, ACSL6 knockdown increased GPX4 expression and colony growth, partially rescuing DHA-induced suppression, whereas ACSL6 overexpression enhanced DHA-mediated GPX4 reduction and colony inhibition, effects reversible by RSL3 or ferrostatin-1. Moreover, ACSL6 enhances DHA-induced lipid peroxidation. These support that ACSL6 enhances DHA-induced ferroptosis, leading to growth suppression. In vivo, DHA supplementation potentiated oxaliplatin-suppressed tumor growth in tumors with upregulated ACSL6 expression, accompanied by GPX4 reduction. Together, these findings highlight ACSL6 as a critical determinant of DHA sensitivity in cancer, underscoring its potential as a predictive biomarker for chemotherapy-DHA combination strategies. By modulating key metabolic and signaling pathways, ACSL6 could influence cellular susceptibility to ferroptosis and may guide therapeutic approaches that enhance chemotherapy through DHA supplementation.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"45"},"PeriodicalIF":6.4,"publicationDate":"2025-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12638798/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145573882","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sphingosine 1-phosphate signalling in cancer stem cells.","authors":"Jason A Powell, Stuart M Pitson","doi":"10.1038/s41389-025-00585-y","DOIUrl":"10.1038/s41389-025-00585-y","url":null,"abstract":"<p><p>Cancer stem cells (CSCs) are considered the head of a hierarchical organisation of carcinogenesis, exhibiting heightened cell survival properties, an ability to endlessly self-renew and undergo attenuated differentiation to maintain the bulk tumour population. The acquisition of cancer stem cell properties including dysregulated self-renewal and differentiation trajectories, is a dynamic disease-specific process underpinned by numerous genetic changes and signalling network aberrations. The bioactive sphingolipid, sphingosine 1-phosphate (S1P), has emerged as a key regulator of CSC biology. Historically, S1P has been associated with maintaining tissue homeostasis and immune responses, but recent studies have revealed that dysregulation of S1P-mediated cellular signalling plays important roles in CSC biology. This review provides an overview of the role of S1P in stem cell biology in both normal physiology and disease. It also describes approaches to target this signalling pathway, where aberrant, with the goal of eradicating the CSC population responsible for cancer initiation and progression, and importantly, patient relapse to many clinical therapeutics.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"42"},"PeriodicalIF":6.4,"publicationDate":"2025-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12627456/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145550178","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pannexin 1 induces Rhabdomyosarcoma cell fusion by downregulating APOBEC2.","authors":"Alexandra Welten, Amit Bera, Stéphanie Langlois, Xiao Xiang, Keshav Gupta, Emily Freeman, Kyle N Cowan","doi":"10.1038/s41389-025-00586-x","DOIUrl":"10.1038/s41389-025-00586-x","url":null,"abstract":"<p><p>Rhabdomyosarcoma (RMS) is an aggressive cancer thought to arise from impaired myogenesis. This can be substantially overcome by increasing the levels of pannexin 1 (PANX1), a critical component of the myogenic program, but the mechanism involved is unknown. Using RNA-seq, we have previously found that overexpression of PANX1 dramatically reshapes the transcriptomic landscape of RMS including downregulation of a myogenic modulator, APOBEC2 (apolipoprotein B mRNA editing enzyme catalytic subunit 2). Following this clue, we investigated the role of APOBEC2 in the PANX1-mediated suppression of RMS malignancy. Here we show that, using a panel of patient-derived RMS cell lines and tumor specimens, APOBEC2 is expressed in RMS, but that its levels are lower than those in both differentiating myoblasts and skeletal muscle. In most RMS cell lines examined, APOBEC2 accumulates during proliferation and sustains their stem-like characteristics, as evidenced by its ability to promote the growth of spheroids upon increased expression. Yet, ectopic PANX1 expression led to a marked downregulation of APOBEC2 across a large proportion of RMS cell lines assessed. Strikingly, these were the same cells in which PANX1 triggers multinucleation. We further reveal that, like healthy myoblasts progressing through myogenesis, the multinucleation observed here in RMS cells results from cell fusion. Importantly, in RMS cells engineered to overexpress APOBEC2, PANX1 no longer enhances cell fusion, but its other anti-tumorigenic properties are still preserved. Collectively, our data indicate that PANX1 promotes RMS cell fusion by downregulating APOBEC2 expression, driving these tumor cells further into the myogenic program.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"43"},"PeriodicalIF":6.4,"publicationDate":"2025-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12627423/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145550144","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"YTHDF3 promotes breast cancer osteolytic bone metastasis by enhancing the translation of ZEB1 and SMAD5.","authors":"Lun Xu, Qian Yu, Xu Peihang, Kun Li, Bingnan Wang, Yang Shao, Mo Cheng, Wending Huang, Qianlan Yao, Xu Feng, Shaoli Song, Shuoer Wang, Wangjun Yan","doi":"10.1038/s41389-025-00583-0","DOIUrl":"10.1038/s41389-025-00583-0","url":null,"abstract":"<p><p>Bone metastsis in advanced breast cancer patients are usually osteolytic. A better understanding of the mechanisms in osteolytic metastasis is critical for the development of new therapies. YTH domain-containing family protein 3 (YTHDF3) has been reported to function as an N6-methyladenosine (m6A)-modified mRNA regulator. In this study, we found YTDHF3 expression was associated with clinical characteristics of breast cancer patients. YTHDF3 expression influenced the migration and invasion capacity of breast cancer cells in vitro and in vivo, and low expression of YTHDF3 suppressed cancer cell-induced osteoclast differentiation and osteolytic bone destruction. Moreover, we found YTHDF3 enhanced the translation of zinc finger E-box-binding protein 1 (ZEB1) and SMAD family member 5 (SMAD5) by reading the m6A modification sites in their mRNAs and further promoted the epithelial-mesenchymal transition (EMT) of breast cancer cells. Enhanced expression of ZEB1 promoted the transcription of bone morphogenetic protein inhibitors such as NOG, FST and CCN2, which boosts osteolytic metastasis. Furthermore, we newly found Wnt family member 5B (WNT5B) expression was regulated by ZEB1, also involved in osteolytic process. In conclusion, YTHDF3 plays an important role in osteolytic metastasis and it may serve as a potential prognostic biomarker and therapeutic target for breast cancer bone metastasis.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"41"},"PeriodicalIF":6.4,"publicationDate":"2025-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12623997/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145541551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"CMKLR1/PKA signaling reinforces sonic hedgehog pathway to promote medulloblastoma pathogenesis.","authors":"Shan Wang, Tongtong Jiang, Tao Wang, Zhiwei Yang, Ting Wang, Xiao Zhang, Xingchun Gou, Lintao Jia, Liang Wang, Yang Song","doi":"10.1038/s41389-025-00582-1","DOIUrl":"10.1038/s41389-025-00582-1","url":null,"abstract":"<p><p>Aberrant Hedgehog signaling is a key driver of malignancies like medulloblastoma (MB), the most common pediatric brain tumor originating from cerebellar granule neuron progenitors with largely uncharacterized mechanisms. We found here that the G protein-coupled receptor, chemokine-like receptor 1 (CMKLR1), is upregulated and correlates with the development of Sonic Hedgehog (SHH)-subtype MB. SHH and the downstream transcription factor Gli2 license the expression of CMKLR1, which promotes the growth and migration of cells by activating Gα(i)βγ and subsequently the PI3K/Akt signal pathway. SHH/Gli also transcriptionally represses Regulator of G Protein Signaling 16 (RGS16), a known suppressor of Gα(i). Meanwhile, CMKLR1/Gα(i) signaling inactivates protein kinase A (PKA), reduces PKA-catalyzed phosphorylation of Gli2, and circumvents its proteasomal degradation, thus forming a feedback circuit in medulloblastoma cells. Consistently, CMKLR1 ablation suppresses the in vivo development of SHH subtype MB, which is counteracted by further silencing of the PKA catalytic subunit. These findings provide novel insights into the oncogenic network of Hedgehog pathway-driven cancer.</p>","PeriodicalId":19489,"journal":{"name":"Oncogenesis","volume":"14 1","pages":"40"},"PeriodicalIF":6.4,"publicationDate":"2025-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12624127/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145541560","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}