{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Turner KL"],"funding":["American Heart Association-American Stroke Association","NHLBI NIH HHS","National Institutes of Health","NIH HHS"],"pagination":["e202213250"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9930131"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["155(4)"],"pubmed_abstract":["Hypertrophic cardiomyopathy (HCM) is the leading genetic cause of heart disease. The heart comprises several proteins that work together to properly facilitate force production and pump blood throughout the body. Cardiac myosin binding protein-C (cMyBP-C) is a thick-filament protein, and mutations in cMyBP-C are frequently linked with clinical cases of HCM. Within the sarcomere, the N-terminus of cMyBP-C likely interacts with the myosin regulatory light chain (RLC); RLC is a subunit of myosin located within the myosin neck region that modulates contractile dynamics via its phosphorylation state. Phosphorylation of RLC is thought to influence myosin head position along the thick-filament backbone, making it more favorable to bind the thin filament of actin and facilitate force production. H"],"journal":["The Journal of general physiology"],"pubmed_title":["RLC phosphorylation amplifies Ca2+ sensitivity of force in myocardium from cMyBP-C knockout mice."],"pmcid":["PMC9930131"],"funding_grant_id":["R01 HL149164","19TPA34860008"],"pubmed_authors":["Tanner BCW","Fitzsimons DP","Awinda PO","Turner KL","Morris HS"],"additional_accession":[]},"is_claimable":false,"name":"RLC phosphorylation amplifies Ca2+ sensitivity of force in myocardium from cMyBP-C knockout mice.","description":"Hypertrophic cardiomyopathy (HCM) is the leading genetic cause of heart disease. The heart comprises several proteins that work together to properly facilitate force production and pump blood throughout the body. Cardiac myosin binding protein-C (cMyBP-C) is a thick-filament protein, and mutations in cMyBP-C are frequently linked with clinical cases of HCM. Within the sarcomere, the N-terminus of cMyBP-C likely interacts with the myosin regulatory light chain (RLC); RLC is a subunit of myosin located within the myosin neck region that modulates contractile dynamics via its phosphorylation state. Phosphorylation of RLC is thought to influence myosin head position along the thick-filament backbone, making it more favorable to bind the thin filament of actin and facilitate force production. H","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2025-04-04T20:04:22.464Z","creation":"2025-04-04T20:04:22.464Z"},"accession":"S-EPMC9930131","cross_references":{"pubmed":["36715675"],"doi":["10.1085/jgp.202213250"]}}