Molecular Cancer Research最新文献

{"title":"Mutational Signatures and Hypermutation Phenotypes Define Bladder Cancers Arising in Waterpipe and Cigarette Smokers.","authors":"Ali Shamseddine, Noura Abbas, Jordan Eichholz, Walid K Chatila, Henry Walch, Rami Mahfouz, Merve Basar, Nikolaus Schultz, David Solit, Layal Al Mahmasani, Maya Charafeddine, Monita Al Darazi, Jonathan E Rosenberg, Gopa Iyer, Bernard H Bochner, Eugene J Pietzak, Victor E Reuter, Ghazi Zaatari, Ghassan K Abou-Alfa, Hikmat Al-Ahmadie","doi":"10.1158/1541-7786.MCR-26-0157","DOIUrl":"https://doi.org/10.1158/1541-7786.MCR-26-0157","url":null,"abstract":"<p><p>Bladder cancer is a major malignancy worldwide. Although cigarette smoking is the leading modifiable risk factor, the contribution of waterpipe smoking (WPS), which is increasingly popular globally and often misperceived as safer, remains unclear. In 2019, Lebanese males had the highest bladder cancer incidence in the Arab world (five times the global average), prompting investigation of WPS as a potential carcinogen. We performed a cross-sectional genomic analysis of patients with exclusive WPS and urothelial carcinoma treated at the American University of Beirut Medical Center (n=250 screened; 14 exclusively WPS), integrating targeted sequencing (MSK-IMPACT®) and whole-exome sequencing (TEMPO pipeline). Tumor mutational burden (TMB), microsatellite instability, mutational signatures, and oncogenic alterations were assessed. Previously profiled bladder cancer tumors from cigarette smokers and non-smokers at Memorial Sloan Kettering Cancer Center (n=751) served as comparators. MSK-IMPACT® successfully profiled 13 tumors. WPS-associated tumors exhibited a numerically higher median TMB than cigarette (20 vs. 10 mut/Mb; p=0.10, q=0.2), with 38.5% classified as MSS-hypermutated, a phenotype associated with elevated mutational load despite microsatellite stability. Common mutations included TERT promoter (62%), TP53 and FGFR3 (46%), and PIK3CA (38%). APOBEC mutational signatures predominated across all cohorts, suggesting shared mutagenic processes, while chromatin-modifying gene alterations were less frequent. PD-L1 expression was generally low. Implications: Exclusive WPS induces bladder tumors with overall genomic features resembling cigarette-associated disease, yet with numerically higher TMB and enrichment of MSS-hypermutated phenotypes. These findings provide novel mechanistic evidence of tobacco-related carcinogenesis beyond cigarettes and highlight potential biomarker relevance for immunotherapy in a globally rising exposure group.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":""},"PeriodicalIF":5.8,"publicationDate":"2026-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149228340","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PAX3::FOXO1 and the INO80 complex sustain replication fork progression in fusion positive rhabdomyosarcoma.","authors":"Pushpendra Kumar Sahu, Yue Pan, Matthew Watson, Colette G Sands, Sinead Carse, Kristen Kwong, Alex G Lee, Leanne C Sayles, E Alejandro Sweet-Cordero, Amit J Sabnis","doi":"10.1158/1541-7786.MCR-26-0205","DOIUrl":"10.1158/1541-7786.MCR-26-0205","url":null,"abstract":"<p><p>Transcription factor fusions are recurrent drivers of sarcomas and other cancers, but their oncogenic reorganization of chromatin is difficult to target. One such fusion, PAX3::FOXO1, drives an aggressive subset of pediatric rhabdomyosarcoma (RMS) through chromatin remodeling, blocking terminal differentiation and sustaining proliferation. We hypothesized that identifying PAX3::FOXO1 genetic dependencies would reveal new facets of transcription factor fusion biology. We report an unexpected role for PAX3::FOXO1 in driving DNA replication fork progression, uncovered by its dependence on the INO80 chromatin remodeling complex (INO80c). Loss of the INO80c member UCHL5 reduces the competitive fitness of fusion positive (FP), but not fusion negative (FN) RMS cell lines, and is accompanied by reduced DNA replication fork speed. UCHL5 is required to maintain the N-terminal subdomain of INO80c, but a catalytically dead UCHL5 is sufficient to rescue complex formation, fork progression, and FP-RMS fitness. Similarly, loss of PAX3::FOXO1 rapidly leads to RPA32 foci and slows DNA fork progression. These findings demonstrate that PAX3::FOXO1 and INO80c are each critical to maintain replication fork progression in FP-RMS, a novel function for this transcription factor fusion. Implications: PAX3::FOXO1 and the N-terminal INO80 complex are both required to drive replication fork progression in FP-RMS, offering a counterpoint to models in which fusion oncogenes drive replication stress, and identifying INO80 complex members as a genetic dependency in FP-RMS cells.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":""},"PeriodicalIF":5.8,"publicationDate":"2026-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149183538","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functional Characterization of Breast Cancer-Associated Histone Mutations.","authors":"Andrea D Edwards, Yangyang Dai, Siddharth Singh, Micah Thornton, Tulip Nandu, Ralf Kittler, Cristel V Camacho, Dan Huang, W Lee Kraus","doi":"10.1158/1541-7786.MCR-25-0982","DOIUrl":"10.1158/1541-7786.MCR-25-0982","url":null,"abstract":"<p><p>Cancer-related somatic histone mutants are present in 4% of diverse tumor types and display a similar genomic prevalence to other somatic mutations in cancer, but they are not well characterized. We curated and characterized 17 of the most frequently recurring missense mutations in histone H2A, H2B, and H3 genes in breast cancers occurring at glutamate (E), aspartate (D), serine (S), and arginine (R) residues. Many of these mutants co-occur with PIK3CA mutations in breast cancers. We expressed these breast cancer-associated histone mutants in MCF-7 and MDA-MB-468 breast cancer cells, or MCF-10A mammary epithelial cells, and screened them for effects on oncogenic phenotypes in a variety of cell- and tumor-based assays (i.e., proliferation, migration, invasion, competitive outgrowth, transformation). In addition, we examined the effects of selected mutants on DNA damage, gene expression, and histone modifications. We observed varying phenotypic and functional effects. Some of the histone mutants promoted cancer-related phenotypes, with H2B-E76Q, H3-E97K, and H3-E105K eliciting strong oncogenic phenotypes, alterations in gene expression, and context-dependent growth enhancement in a PI3K-activated background. We further showed that the H2B-E76Q and H3-E105K mutants exhibit reduced ADP-ribosylation compared to their cognate wild-type histones, resulting in altered H3-S10 phosphorylation and H3-K27 acetylation in cells. Our results indicate that some histone mutants can promote oncogenic effects in breast cancers, contributing to cancer pathogenesis and tumor progression. Implications: These findings identify a subset of breast cancer-associated histone variants with oncogenic activity, highlighting the role of histone mutations in promoting tumor phenotypes through epigenomic alterations and signaling crosstalk.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":""},"PeriodicalIF":5.8,"publicationDate":"2026-10-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149183535","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"tRF-3021a Promotes Apoptosis Resistance and Global Protein Synthesis in Cancer Cell Lines.","authors":"Fatemeh Esmaeili, Kumarjeet Banerjee, Ajay Chatrath, Divya Sahu, Yoshiyuki Shibata, Shekhar Saha, Pankaj Kumar, Zhangli Su, Anindya Dutta","doi":"10.1158/1541-7786.MCR-26-0126","DOIUrl":"https://doi.org/10.1158/1541-7786.MCR-26-0126","url":null,"abstract":"<p><p>tRNA-derived fragments (tRFs) are a relatively recently discovered class of small RNAs implicated in gene-regulation, particularly behaving as microRNA to degrade target mRNAs with seed-sequence matches, but there have been very few reports of a clear phenotypic role of these small RNAs in cancer cell growth and other properties. Here we report that in three different cancer cell lineages, tRF-3009a, tRF-3021a and tRF-3030a are required for cell invasion and migration. Of the three tRFs, tRF-3021a was uniquely required for cell proliferation and suppression of apoptosis. Interestingly, tRF-3021a knockdown decreases global protein synthesis prior to and independent of apoptosis in a number of cancer cell lines of different lineages. Mutation of tRF-3021a shows that the effect on protein synthesis is very dependent on specific sequences in the tRF. RNA-seq reveals that the results cannot be explained by tRF-3021a decreasing the levels of target mRNAs that carry seed sequence matches with the tRF. These data indicate that tRF-3021a supports cancer cell survival and particularly protein synthesis while promoting cellular invasion and migration. Implications: tRF-3021a promotes malignant cell phenotypes, sustains global protein synthesis and prevents spontaneous apoptosis.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":""},"PeriodicalIF":5.8,"publicationDate":"2026-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149137893","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction: BRAFV600E-Driven Lung Adenocarcinoma Requires Copper to Sustain Autophagic Signaling and Processing.","authors":"Tiffany Tsang, Xingxing Gu, Caroline I Davis, Jessica M Posimo, Zoey A Miller, Donita C Brady","doi":"10.1158/1541-7786.MCR-26-0652","DOIUrl":"https://doi.org/10.1158/1541-7786.MCR-26-0652","url":null,"abstract":"","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":"24 10","pages":"870"},"PeriodicalIF":5.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13631495/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149112656","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":"Editor's Note: AURKA Governs Self-Renewal Capacity in Glioma-Initiating Cells via Stabilization/Activation of β-catenin/Wnt Signaling.","authors":"Zhibo Xia, Ping Wei, Heng Zhang, Zhiming Ding, Lixuan Yang, Zhengsong Huang, Nu Zhang","doi":"10.1158/1541-7786.MCR-26-0648","DOIUrl":"https://doi.org/10.1158/1541-7786.MCR-26-0648","url":null,"abstract":"","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":"24 10","pages":"871"},"PeriodicalIF":5.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149112666","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"CELF2 Is a Tumor Suppressor That Modulates SLC7A11 and Promotes Ferroptosis in Stomach Adenocarcinoma.","authors":"Shoucai Zhang, Shichao Liu, Zeyu Zhang, Yingjie Liu, Maopeng Yin, Xueyan Geng, Helgi B Schioth, Yi Zhang","doi":"10.1158/1541-7786.MCR-25-1017","DOIUrl":"10.1158/1541-7786.MCR-25-1017","url":null,"abstract":"<p><p>Stomach adenocarcinoma is among the most prevalent malignant gastrointestinal tumors worldwide. Ferroptosis, a relatively new form of programmed cell death, has garnered significant attention for its role in cancer molecular mechanisms and therapeutic strategies. Therefore, it is particularly important to explore the mechanism of key molecules in ferroptosis in stomach adenocarcinoma. In our study, CUGBP Elav-like family member 2 (CELF2) was identified as being lowly expressed in stomach adenocarcinoma tumor tissues at both the mRNA and protein levels. Next, CELF2 effectively inhibited the growth and migration of stomach adenocarcinoma cells both in vitro and in vivo. RNA sequencing (RNA-seq) analysis of AGSCELF2 and AGSNC cells showed that the functions of differentially expressed genes were enriched in the glutathione metabolism and ferroptosis pathways. CELF2 increased the levels of key ferroptosis markers, including reactive oxygen species, malondialdehyde, Fe2+, and 4-hydroxynonenal, while reducing glutathione levels. Furthermore, CELF2 enhanced the susceptibility of stomach adenocarcinoma tumor cells to ferroptosis. Interestingly, the expression levels of CELF2 and solute carrier family 7 member 11 (SLC7A11) were negatively correlated in RNA-seq data and The Cancer Genome Atlas database. RNA immunoprecipitation and RNA pull-down assays confirmed the interaction between CELF2 and SLC7A11. Overexpression (OE) of SLC7A11 reversed the effects of CELF2 on stomach adenocarcinoma growth and ferroptosis levels. Moreover, the ferroptosis inhibitor ferrostatin-1 effectively rescued the inhibitory effect of CELF2 OE on the proliferation of tumor cells. CELF2 is a tumor suppressor that promotes the level and susceptibility of ferroptosis in stomach adenocarcinoma cells by targeting SLC7A11.</p><p><strong>Implications: </strong>This study offers valuable molecular insights for the development of ferroptosis-targeted therapies for stomach adenocarcinoma.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":"809-820"},"PeriodicalIF":5.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148265236","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comprehensive Multi-Omic Profiling of Desmoplastic Small Round Cell Tumors Identifies Targetable Pathways with Therapeutic Opportunities.","authors":"Jamie M Keck, Limin Zhu, Jayne M Stommel, Jay A Egger, Tugba Y Ozmen, Furkan Ozmen, Jinho Lee, Benjamin Tate, Matthew J Rames, Allison L Creason, Christopher G Suciu, Joanna Pucilowska, Gordon B Mills, Lara E Davis","doi":"10.1158/1541-7786.MCR-25-1134","DOIUrl":"10.1158/1541-7786.MCR-25-1134","url":null,"abstract":"<p><p>Desmoplastic small round cell tumor (DSRCT) is a rare, aggressive, fusion-driven sarcoma with poor outcomes despite intensive chemotherapy. Utilization of targeted therapies in DSRCT remains limited, underscoring the need for deeper characterization of patient tumors. To address this, we performed multi-omic profiling on nine patient-derived tumor biopsies from five patients enrolled in a precision oncology program. We consistently observed elevated mRNA and protein expression of human epidermal growth factor receptor 2, androgen receptor, and DNA damage response (DDR) markers, and characterized these molecular features using an integrated assay suite including bulk and single-cell RNA sequencing, protein profiling, immunohistochemistry, immune analyses, and functional homologous recombination deficiency (HRD) testing. We define a replication stress-associated DNA damage landscape and identify functional HRD in a subset of tumors lacking genomic HRD scar signatures. Single-cell analyses reveal intratumoral and intertumoral heterogeneity, whereas longitudinal sampling uncovers treatment-dependent shifts in expression and activity that may contribute to adaptive resistance. The immune microenvironment is characterized by dysfunctional T-cell states and sparse antigen-presenting cells. Collectively, these analyses delineate recurrent, biologically targetable features and patient-specific vulnerabilities, establishing a foundation for biomarker-guided therapeutic strategies in DSRCT. These findings support the investigation of rational combination approaches informed by sensitive detection methods and functional testing to address resistance in ultra-rare cancers.</p><p><strong>Implications: </strong>Integrative multi-omic profiling combined with functional testing in DSRCTs reveals patient-specific vulnerabilities and biologically targetable receptor and DDR dependencies while defining immune states that may inform therapeutic response and rational combination strategies in this rare, fusion-driven cancer.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":"849-869"},"PeriodicalIF":5.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148272129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PPP1CA drives osteosarcoma tumorigenesis by promoting PKM2 dephosphorylation and tetramerization.","authors":"Guangjian Bai, Zhao Li, Tianxiang Shao, Dingbang Chen, Zhitao Han, Zhenhua Zhou, Haoming Wang, Xiangzhi Ni, Baoquan Xin, Xinghai Yang, Tielong Liu, Jianru Xiao, Qi Jia","doi":"10.1158/1541-7786.MCR-25-1256","DOIUrl":"https://doi.org/10.1158/1541-7786.MCR-25-1256","url":null,"abstract":"<p><p>Osteosarcoma (OS) is a highly aggressive malignant tumor with no effective targeted therapies at present. Aerobic glycolysis represents a hallmark metabolic feature of OS, wherein the glycolytic rate-limiting enzyme pyruvate kinase M2 isozyme (PKM2) exhibits high enzymatic activity in OS cells. However, the regulatory mechanisms underlying PKM2 hyperactivation in OS remain poorly understood. PKM2 expression was measured by agarose gel electrophoresis and quantitative real-time reverse transcription polymerase chain reaction (qRT-PCR). Proteomic analysis, coimmunoprecipitation (co-IP), and proximity ligation assay (PLA) were used to identify PKM2-interacting proteins. Protein cross-linking, blue native PAGE (BN-PAGE), and extracellular acidification rate (ECAR)/oxygen consumption rate (OCR) assays were performed to determine the effect of PPP1CA on PKM2 tetramer formation and glycolytic capacity. Functional assays were conducted in vitro and in vivo to assess the biological consequences of PPP1CA-mediated PKM2 activation on proliferation, migration, cell cycle, apoptosis, and in vivo tumor growth. Mechanistically, PPP1CA specifically binds to PKM2 and dephosphorylates it, promoting the conversion of PKM2 from dimers to tetramers. PPP1CA-mediated PKM2 tetramer activation enhanced glycolytic capacity and drove malignant behaviors including proliferation, migration, cell cycle progression, dysregulated apoptosis, and in vivo tumor growth. In clinical specimens, PPP1CA was aberrantly upregulated in OS tissues and inversely correlated with both PKM2 phosphorylation level and patient prognosis. Collectively, these results demonstrate that PPP1CA promotes PKM2 tetramerization through dephosphorylation, thereby enhancing glycolytic capacity and driving malignant progression in OS, highlighting PPP1CA as a potential therapeutic target. Implications: This study reveals that PPP1CA drives osteosarcoma progression by promoting PKM2 tetramerization and glycolysis.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":""},"PeriodicalIF":5.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149112669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MYC-Mediated USP39 Upregulation Stabilizes SRSF1 in Pancreatic Cancer.","authors":"Benteng Ma, Xin Zhang, Alexander J Kral, Neelu Singh, Astrid Deschênes, Paolo Cifani, Youngkyu Park, David A Tuveson, Adrian R Krainer, Ledong Wan","doi":"10.1158/1541-7786.MCR-25-1104","DOIUrl":"10.1158/1541-7786.MCR-25-1104","url":null,"abstract":"<p><p>Pancreatic ductal adenocarcinoma (PDAC) is a highly lethal malignancy primarily driven by oncogenic KRAS signaling. The splicing factor serine/arginine-rich splicing factor 1 (SRSF1) plays a key oncogenic role in PDAC through reciprocal cross-interactions with KRAS signaling. However, the mechanisms regulating SRSF1 protein stability remain poorly understood. In this study, we identify the deubiquitinase USP39 as a critical regulator of SRSF1 stability. It interacts with SRSF1 in an RNA-independent manner and suppresses its ubiquitination. USP39 is upregulated in PDAC and correlates with poor patient prognosis. Functional analyses demonstrate that USP39 promotes PDAC cell progression, in part through the stabilization of SRSF1. Mechanistically, MYC activates USP39 transcription through direct promoter binding. These findings define a MYC-USP39-SRSF1 regulatory axis that integrates transcriptional and posttranslational mechanisms in PDAC and suggest USP39 as a potential therapeutic target.</p><p><strong>Implications: </strong>USP39 functions as a central regulator that integrates transcriptional and posttranslational regulation in pancreatic cancer through the MYC-USP39-SRSF1 axis and represents a potential therapeutic target.</p>","PeriodicalId":19095,"journal":{"name":"Molecular Cancer Research","volume":" ","pages":"837-848"},"PeriodicalIF":5.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13355883/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148218866","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}