{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Doh CY"],"funding":["National Heart, Lung, and Blood Institute","NHLBI NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["14189-14202"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9089392"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(16)"],"pubmed_abstract":["Cardiac myosin binding protein C (cMyBPC) is a critical multidomain protein that modulates myosin cross bridge behavior and cardiac contractility. cMyBPC is principally regulated by phosphorylation of the residues within the M-domain of its N-terminus. However, not much is known about the phosphorylation or other post-translational modification (PTM) landscape of the central C4C5 domains. In this study, the presence of phosphorylation outside the M-domain was confirmed in vivo using mouse models expressing cMyBPC with nonphosphorylatable serine (S) to alanine substitutions. Purified recombinant mouse C4C5 domain constructs were incubated with 13 different kinases, and samples from the 6 strongest kinases were chosen for mass spectrometry analysis. A total of 26 unique phosphorylated peptid"],"journal":["ACS omega"],"pubmed_title":["Identification of Phosphorylation and Other Post-Translational Modifications in the Central C4C5 Domains of Murine Cardiac Myosin Binding Protein C."],"pmcid":["PMC9089392"],"funding_grant_id":["R01GM121583","R01 HL146676","R01 HL114770","2R01HL114770","1R01HL146676","R01 GM121583"],"pubmed_authors":["Stelzer JE","Swanberg CE","Ramachandran R","Dominic KL","Doh CY","Bharambe N","Li L","Willard BB"],"additional_accession":[]},"is_claimable":false,"name":"Identification of Phosphorylation and Other Post-Translational Modifications in the Central C4C5 Domains of Murine Cardiac Myosin Binding Protein C.","description":"Cardiac myosin binding protein C (cMyBPC) is a critical multidomain protein that modulates myosin cross bridge behavior and cardiac contractility. cMyBPC is principally regulated by phosphorylation of the residues within the M-domain of its N-terminus. However, not much is known about the phosphorylation or other post-translational modification (PTM) landscape of the central C4C5 domains. In this study, the presence of phosphorylation outside the M-domain was confirmed in vivo using mouse models expressing cMyBPC with nonphosphorylatable serine (S) to alanine substitutions. Purified recombinant mouse C4C5 domain constructs were incubated with 13 different kinases, and samples from the 6 strongest kinases were chosen for mass spectrometry analysis. A total of 26 unique phosphorylated peptid","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-10T04:11:00.787Z","creation":"2024-11-20T17:22:56.536Z"},"accession":"S-EPMC9089392","cross_references":{"pubmed":["35573219"],"doi":["10.1021/acsomega.2c00799"]}}