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• W2051058132 startingPage "9913" @default.
• W2051058132 abstract "Myosin-binding protein C (MyBP-C) is a thick filament protein consisting of 1274 amino acid residues (149 kDa) that was identified by Starr and Offer over 30 years ago as a contaminant present in a preparation of purified myosin. Since then, numerous studies have defined the muscle-specific isoforms, the structure, and the importance of the proteins in normal striated muscle structure and function. Underlying the critical role the protein plays, it is now apparent that mutations in the cardiac isoform (cMyBP-C) are responsible for a substantial proportion (30-40%) of genotyped cases of familial hypertrophic cardiomyopathy. Although generally accepted that MyBP-C can interact with all three filament systems within the sarcomere (the thick, thin, and titin filaments), the exact nature of these interactions and the functional consequences of modified binding remain obscure. In addition to these structural considerations, cMyBP-C can serve as a point of convergence for signaling processes in the cardiomyocyte via post-translational modifications mediated by kinases that phosphorylate residues in the cardiac-specific isoform sequence. Thus, cMyBP-C is a critical nodal point that has both important structural and signaling roles and whose modifications are known to cause significant human cardiac disease." @default.
• W2051058132 created "2016-06-24" @default.
• W2051058132 creator A5005272366 @default.
• W2051058132 creator A5033912758 @default.
• W2051058132 date "2011-03-01" @default.
• W2051058132 modified "2023-09-28" @default.
• W2051058132 title "Signaling and Myosin-binding Protein C" @default.
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• W2051058132 doi "https://doi.org/10.1074/jbc.r110.171801" @default.
• W2051058132 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3060544" @default.

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