Circulation research最新文献

{"title":"Mitochondrial STING Governs Glycolytic Reprogramming in Diabetic Cardiomyopathy.","authors":"Shiwu Zhang,Dechao Zhao,Mengyi Wang,Xiaorong Shen,Fan Yang,Zhen Tian,Haining Du,Fanghao Lu,Xueya Zhang,Heyu Chen,Jiaxin Kang,Mingjie Dong,Denis V Abramochkin,Huitao Fan,Jinwei Tian,Bo Yu,Shuijie Li,Weihua Zhang","doi":"10.1161/circresaha.125.327867","DOIUrl":"https://doi.org/10.1161/circresaha.125.327867","url":null,"abstract":"BACKGROUNDDiabetic cardiomyopathy, a severe complication of diabetes, is marked by mitochondrial dysfunction, metabolic inflammation, and progressive cardiac impairment. Although STING (stimulator of interferon genes) is well recognized as a central mediator of innate immunity, its noncanonical role in metabolic regulation and mitochondrial dynamics in the diabetic heart remains largely unexplored.METHODSTo elucidate the role of STING in diabetic cardiac remodeling, we used single-cell RNA sequencing, echocardiography, and transmission electron microscopy in both genetic (db/db) and chemically induced (high-fat diet [HFD] plus streptozotocin, HFD/streptozotocin) diabetic mouse models. STING knockout mice and primary neonatal mouse cardiomyocytes were used for mechanistic investigations and functional validation. Mitochondrial respiration and glycolytic flux were assessed using Seahorse extracellular flux analysis. Posttranslational modifications of STING, including S-palmitoylation and S-sulfhydration, were evaluated via acyl-biotin exchange and biotin-switch assays, respectively. ENO1 (enolase 1) enzymatic activity was measured in vitro to assess glycolytic reprogramming. Furthermore, 13C-glucose tracing-based targeted metabolomics was performed to quantify cardiac metabolic flux in db/db mice. Glycolytic metabolites, including lactate and pyruvate, were quantified in cardiac tissues and cultured cardiomyocytes to assess glycolytic activity.RESULTSExposure to high-palmitate conditions induced mitochondrial DNA leakage, thereby activating the cGAS-STING signaling pathway in cardiomyocytes. Mechanistically, STING underwent aberrant translocation to mitochondria, where it interacted with the outer membrane protein TOM (translocase of outer mitochondrial membrane) 40 to impair mitochondrial protein import and disrupt mitochondrial homeostasis. In addition, mitochondrial STING functioned as a scaffold to recruit and activate the glycolytic enzyme ENO1, thereby enhancing its enzymatic activity, accelerating glycolytic flux, and promoting lactate accumulation in diabetic cardiac tissues. Notably, diabetes-associated depletion of endogenous hydrogen sulfide reduced S-sulfhydration of STING at Cys88/91, facilitating its S-palmitoylation and mitochondrial localization. Genetic ablation of STING or pharmacological restoration of hydrogen sulfide levels with GYY4137 effectively rescued mitochondrial dysfunction, decreased lactate overproduction, and preserved cardiac contractile performance in diabetic mice.CONCLUSIONSThese findings identify STING as a spatial immunometabolic modulator that bridges mitochondrial dysfunction with metabolic imbalance in diabetic cardiomyopathy. Enhancing STING S-sulfhydration or targeting its palmitoylation through hydrogen sulfide-based interventions represents a promising therapeutic strategy for the treatment of diabetic cardiomyopathy.","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"25 1","pages":""},"PeriodicalIF":20.1,"publicationDate":"2026-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148365561","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Impaired Endothelial Cell Cholesterol Metabolism Promotes Vascular Inflammation in Sleep Apnea.","authors":"Su Gao,Vikash K Shah,Memet Emin,Audrey Chang,Riddhi Shah,Estela Area Gomez,Ying Wei,Sanja Jelic","doi":"10.1161/circresaha.126.328332","DOIUrl":"https://doi.org/10.1161/circresaha.126.328332","url":null,"abstract":"BACKGROUNDObstructive sleep apnea (OSA) is highly prevalent and triples cardiovascular risk. Intermittent hypoxia during apneas impairs endothelial cell (EC) protection against complement, which initiates endothelial inflammation and increases cardiovascular risk. This process appears to be linked to altered cellular cholesterol metabolism. However, whether and how intermittent hypoxia alters endothelial cholesterol homeostasis and whether those changes affect endothelial inflammation in patients with OSA are unclear.METHODSECs were harvested from the forearm vein from patients with OSA (n=24; age, 44±14 years; 38% female; body mass index, 36±10 kg/m2) and OSA-free controls (n=19; age, 39±14 years; 74% female; body mass index, 29±9 kg/m2). Cultured human umbilical vein ECs exposed to intermittent hypoxia (alternating 30-minute 21% O2 for normoxia/30-minute 2% O2 for hypoxia for 8 hours), 2% O2 for 8 hours (continuous hypoxia), or normoxia were used as the in vitro model.RESULTSIntermittent hypoxia-induced endoplasmic reticulum stress increases interaction of endoplasmic reticulum-bound VAP-B (vesicle-associated membrane protein-associated protein B) with Derlin-1 (degradation in endoplasmic reticulum protein 1), which, in turn, impairs VAP-B interaction with endolysosomal compartment-bound ORP1L (oxysterol-binding protein-related protein 1 long form), leading to retention of cholesterol in the endolysosomal compartment in ECs in OSA. The consequent increase in cholesterol content in the EC plasma membrane promotes internalization of the complement inhibitor CD59, thereby increasing deposition of the terminal complement membrane attack complex on ECs and initiating inflammation. Low levels of positive airway pressure therapy reversed OSA-induced alteration in interactions of VAP-B with both Derlin-1 and ORP1L in patients with OSA.CONCLUSIONSUsing a direct approach to study endothelium, we have identified altered endothelial intracellular cholesterol trafficking and metabolism as mechanisms underlying reduced protection against complement activity and increased endothelial inflammation, which, over time, increases cardiovascular risk in OSA.","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"96 1","pages":""},"PeriodicalIF":20.1,"publicationDate":"2026-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148349110","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Engineered Heart Tissues Facilitate Noncoding Variant Studies in Cardiomyopathy.","authors":"Zachary T Weber,Tanner O Monroe,Cory Holgren,Robert M Mitchell,Li Zhang,Alexis G Thornburg,Isabella M Salamone,Ivana A Chychula,Felix Karthik,Dominic E Fullenkamp,Megan J Puckelwartz,Xuanyao Liu,Elizabeth M McNally,Marcelo A Nóbrega","doi":"10.1161/circresaha.125.327506","DOIUrl":"https://doi.org/10.1161/circresaha.125.327506","url":null,"abstract":"BACKGROUNDCardiomyopathies frequently arise from rare, highly penetrant coding variants with variable clinical expressivity. Genome-wide association studies (GWAS) suggest significant polygenic contributions to cardiovascular diseases, including cardiomyopathy. Most GWAS loci map to poorly conserved noncoding regions, requiring human genome context for experimental validation.METHODSWe created engineered heart tissues (EHTs) from human induced pluripotent stem cell-derived cardiomyocytes and primary cardiac fibroblasts. We assayed single-cell gene expression and chromatin accessibility to generate comprehensive genome-wide regulatory maps. Open chromatin regions were integrated with chromatin contact information and used to fine-map cardiomyopathy GWAS single-nucleotide polymorphisms. Single-nucleotide polymorphisms and their associated open chromatin regions were assessed using reporter assays, genome editing, and expression profiling.RESULTSEHT Single-cell RNA-seq recapitulated major cardiac cell types, with advanced cardiomyocyte maturation compared with monolayer human induced pluripotent stem cell cardiomyocytes. More than 400 000 open chromatin regions were resolved to cell types and assayed for transcription factor motifs. Functional fine-mapping of GWAS loci prioritized 5817 variants, and reporter assays validated allele-specific enhancer activity. We identified an intergenic chr3p25.1 locus harboring significant GWAS signals from both dilated cardiomyopathy and left ventricular ejection fraction. Several of these variants lie in open chromatin regions participating in long-range chromatin interactions with SLC6A6 and GRIP2. Haplotype-resolved and synthetic reporter assays confirmed enhancer activity and narrowed candidate single-nucleotide polymorphisms. CRISPR-deletion of this region reduced expression of both SLC6A6 and GRIP2, indicating the enhancer regulates the expression of multiple genes. EHTs with the enhancer deletion displayed markedly reduced contractile function, confirming that this enhancer region contributes to myocardial function.CONCLUSIONSEHTs are an experimentally tractable platform for testing the function of noncoding variants as modifiers of cardiomyopathy. Variants fine-mapped from cardiomyopathies using EHT regulatory maps have functional consequences and provide a set of prioritized sites to advance the study of polygenic heart failure.","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"72 1","pages":""},"PeriodicalIF":20.1,"publicationDate":"2026-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148342219","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"NUAK1 Inhibition Alleviates Ischemia-Reperfusion Injury via SYNE1-YAP1.","authors":"Yangjinming Bai,Tingting Zhao,Qian Wang,Rui Zhang,Zhixing Wei,Yudong Fei,Xingxing Cai,Zhengyang Wu,Ji Yan,Yichao Zhang,Kaiyan Chen,Yuepeng Wang,Yi-Gang Li","doi":"10.1161/circresaha.126.328256","DOIUrl":"https://doi.org/10.1161/circresaha.126.328256","url":null,"abstract":"BACKGROUNDMechanosensitive nuclear signaling contributes to myocardial ischemia-reperfusion injury, but the substrates and mechanisms of NUAK1 (AMPK-related kinase 5) remain unclear. We investigated whether NUAK1 regulates SYNE1 (Nesprin-1)/linker of nucleoskeleton and cytoskeleton-dependent nuclear gating of YAP1 (Yes-associated protein 1) during hypoxia/reoxygenation and ischemia-reperfusion injury.METHODS AND RESULTSQuantitative phosphoproteomics identified a conserved NUAK1-dependent phosphorylation site in striated muscle-enriched Nesprin1-α2/SYNE1 (S434; S8284 in nesprin-1 giant). Coimmunoprecipitation and in vitro kinase assays supported direct SYNE1 phosphorylation by NUAK1. In neonatal mouse ventricular myocytes, genetic or pharmacological inhibition of NUAK1 decreased apoptotic signaling, reduced SYNE1 stability, enhanced YAP1 nuclear localization, and altered nuclear YAP1 dynamics. SYNE1 phosphosite mutants and nuclear/cytoplasmic fractionation supported a NUAK1-SYNE1 axis that restrains YAP1 nuclear accumulation under stress. Atomic force microscopy linked this pathway to nuclear mechanical remodeling. In a mouse model of ischemia-reperfusion injury, NUAK1 inhibition reduced acute myocardial damage and improved remodeling indices.CONCLUSIONSNUAK1-dependent SYNE1 phosphorylation shapes nuclear mechanosignaling during ischemic stress. NUAK1 downregulation promotes cardiomyocyte YAP1 nuclear activity and attenuates injury responses.","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"13 1","pages":""},"PeriodicalIF":20.1,"publicationDate":"2026-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148286799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Adipose-Derived FAM19A5 Inhibits Both Vascular Calcification and Osteoporosis in Mice.","authors":"Zhao Dong, Shiyu Yang, Huan Wang, Jiazi Zhang, Nan Xie, Rongbo Dai, Siting Zhang, Zeyu Cai, Zhiqing Li, Shirong Zhu, Jinwei Wang, Biao Zhou, Jihong Kang, Fang Yu, Hua Meng, Yi Fu, Luxia Zhang, Lu Zhang, Chunli Song, Wei Kong","doi":"10.1161/CIRCRESAHA.125.327708","DOIUrl":"10.1161/CIRCRESAHA.125.327708","url":null,"abstract":"<p><strong>Background: </strong>Vascular calcification and osteoporosis often co-occur during postmenopause, end-stage renal disease, advancing age, and diabetes, leading to increased mortality and significant challenges in therapy. FAM19A5 (family with sequence similarity 19 [chemokine (C-C motif)-like], member A5), as a novel protective adipokine, has been identified to suppress postinjury neointima formation. However, the involvement of adipose-derived FAM19A5 in vascular calcification and osteoporosis remains unclear.</p><p><strong>Methods: </strong>A cross-sectional study was conducted to assess the relationship among circulating FAM19A5, coronary artery calcification, and osteoporosis. Adipose-specific FAM19A5 transgenic mice and AAV8 (adeno-associated virus serum type 8)-adipo-shFAM19A5 were employed to study gain or loss of function of FAM19A5 in 2 distinct mouse models: ovariectomy followed by Vitamin D3 overload (OVX-VitD3) and adenine diet. Calcium assays, micro-CT, Western blot, RT-qPCR, luciferase reporter assays, and ChIP-qPCR were performed to clarify the phenotype and elucidate the molecular mechanisms. Finally, administration of AAV8-adipoq-FAM19A5 and S1PR2 (sphingosine 1-phosphate receptor 2) global knockout mice was used to investigate their therapeutic effects.</p><p><strong>Results: </strong>Circulating FAM19A5 was negatively correlated with coronary artery calcification and osteoporosis in patients and mouse models. Adipose-specific FAM19A5 transgenic mice exhibited milder aortic calcification and preserved bone mass via S1PR2 in both OVX-VitD3 and adenine diet models. Although adipose-specific knockdown of FAM19A5 aggravates aortic calcification and bone mass loss. Interestingly, FAM19A5 mitigated vascular smooth muscle cells' calcification by activating S1PR2-Gi-PKA signaling and promoted mice osteoblasts differentiation by triggering S1PR2-Gq-PKCδ (protein kinase C delta isoform) signaling. Finally, administration of AAV8-adipoq-FAM19A5 effectively rescued vascular calcification and osteoporosis, but exerted no beneficial effects in S1PR2 knockout mice.</p><p><strong>Conclusions: </strong>Adipose-derived FAM19A5 plays an essential role in orchestrating vascular calcification and osteoporosis through the selective activation of S1PR2. Our findings provide novel insight into the previously unexplored role of adipose tissue in maintaining vascular-bone homeostasis. FAM19A5-S1PR2 may be considered as a potential therapeutic strategy for vascular calcification and osteoporosis.</p>","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":" ","pages":"e327708"},"PeriodicalIF":18.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834411","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editors and Editorial Board.","authors":"","doi":"10.1161/RES.0000000000000758","DOIUrl":"https://doi.org/10.1161/RES.0000000000000758","url":null,"abstract":"","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"139 1","pages":"e000758"},"PeriodicalIF":18.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276235","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polycystin-1 and Cardiac Remodeling: From Mechanotransduction to Clinical Consequences.","authors":"Magda C Díaz-Vesga, Luiz Fernando Onuchic, Thomas G Gillette, Sergio Lavandero, Joseph A Hill, Zully Pedrozo","doi":"10.1161/CIRCRESAHA.125.327266","DOIUrl":"10.1161/CIRCRESAHA.125.327266","url":null,"abstract":"<p><p>PC1 (polycystin-1), traditionally viewed through the lens of renal pathophysiology in autosomal dominant polycystic kidney disease, has emerged as a central regulator of cardiovascular mechanobiology. Recent structural elucidation of the PC1/PC2 (polycystin-2) complex provides a molecular framework emphasizing its mechanically sensitive ectodomain, regulated proteolytic cleavage, and functional coupling with PC2, framing PC1 as a versatile integrator of biomechanical cues, extracellular matrix interactions, and Ca²⁺ signaling across cardiovascular cell types. This review synthesizes evidence demonstrating that PC1 plays a direct and primary role in the cardiovascular system, independent of renal decline, regulating vascular homeostasis, endothelial shear stress responsiveness, smooth muscle phenotype, and myocardial mechanotransduction. We describe the molecular mechanisms whereby PC1 dysfunction perturbs nitric oxide signaling, cytoskeletal remodeling, excitation-contraction coupling, and hypertrophic transcriptional programs, and highlight tissue-specific roles in cardiac morphogenesis and adult myocardial integrity. By integrating structural biology with cardiovascular physiology, this review provides a unified framework for understanding PC1 as a master mechanosensor linking biomechanical forces to pathological remodeling. Critical knowledge gaps, emerging therapeutic opportunities, and the potential role of artificial intelligence in PC1-targeted drug discovery are also discussed.</p>","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"139 1","pages":"e327266"},"PeriodicalIF":18.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13286233/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276287","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editors and Editorial Board.","authors":"","doi":"10.1161/RES.0000000000000758","DOIUrl":"https://doi.org/10.1161/RES.0000000000000758","url":null,"abstract":"","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"139 1","pages":"e000758"},"PeriodicalIF":18.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148863739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Atherosclerosis Profiling Reveals BHLHE40 as a Candidate Modulator of VSMC.","authors":"Chinyere O Ibikunle, Enrique J Garcia, Chenyi Xue, Eunyoung Kim, Hanying Yan, Johana Coronel, Lucie Y Zhu, Jian Cui, Allen Chung, Lauren E Fries, Nadja Sachs, Robert C Bauer, Lars Maegdefessel, Mingyao Li, Alan R Tall, Alexander C Bashore, Muredach P Reilly","doi":"10.1161/CIRCRESAHA.125.326821","DOIUrl":"10.1161/CIRCRESAHA.125.326821","url":null,"abstract":"<p><strong>Background: </strong>Vascular smooth muscle cells (VSMCs) play a central role in atherosclerosis by undergoing phenotypic modulation from a quiescent, contractile state to a range of synthetic phenotypes, including fibroblast-like, macrophage-like, and lipid-laden foam cell-like states. However, a comprehensive multimodal characterization and understanding of the transcriptional programs driving these transitions remain incomplete.</p><p><strong>Methods: </strong>To comprehensively define the phenotypic diversity of VSMCs during atherosclerosis progression, we performed in-depth profiling using cellular indexing of transcriptomes and epitopes by sequencing and bulk RNA sequencing in a VSMC-lineage-tracing atherosclerotic mouse model. Insights from these data sets guided the design of targeted in vitro experiments to investigate candidate regulatory mechanisms.</p><p><strong>Results: </strong>Single-cell multiomics revealed extensive cellular heterogeneity within atherosclerotic plaques, including a rare population of VSMC-derived macrophage-like cells, whose presence was confirmed by histological analysis. These studies also identified a large population of VSMC-derived foam cells that exhibited activation of gene programs associated with lipid metabolism, proliferation, and tumor-like features. The transcription factor BHLHE40 (basic helix-loop-helix family member e40) emerged as a candidate regulator of this phenotypic transition, with elevated expression and activity in VSMC-derived foam cells during disease progression and expression in modulated VSMC in human carotid atherosclerosis. Functional knockdown of <i>Bhlhe40</i> reprogrammed immune, cell cycle, and lipid homeostasis genes in cultured VSMC and suppressed VSMC phenotypic switching and foam cell characteristics, consistent with a potential regulatory role in VSMC modulation.</p><p><strong>Conclusions: </strong>These findings advance our understanding of VSMC phenotypic modulation in atherosclerosis and implicate BHLHE40 as a candidate transcriptional regulator of this process. Elucidating mechanisms governing VSMC plasticity may offer new therapeutic opportunities to reduce cardiovascular risk by targeting disease-driving cellular transitions.</p>","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":" ","pages":"e326821"},"PeriodicalIF":18.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13274727/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147927156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction to: Athlete's Heart Revisited: Historical, Clinical, and Molecular Perspectives.","authors":"Paishiun Nelson Hsieh, Siman Shen, Marius I Chukwurah, Timothy W Churchill, Katie M Stewart, Eugene H Chung, Rory B Weiner, Haobo Li, James Sawalla Guseh","doi":"10.1161/RES.0000000000000757","DOIUrl":"https://doi.org/10.1161/RES.0000000000000757","url":null,"abstract":"","PeriodicalId":10147,"journal":{"name":"Circulation research","volume":"139 1","pages":"e000757"},"PeriodicalIF":18.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276256","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}