A Critical Function for Ser-282 in Cardiac Myosin Binding Protein-C Phosphorylation and Cardiac Function | Zendy

Sakthivel Sadayappan | Zendy; James Gulick | Zendy; Hanna Osińska | Zendy; David Y. Barefield | Zendy; Friederike Cuello | Zendy; Metin Avkiran | Zendy; Valerie M. Lasko | Zendy; John N. Lorenz | Zendy; Marjorie Maillet | Zendy; Joel W. Martin | Zendy; Joan Heller Brown | Zendy; Donald M. Bers | Zendy; Jeffery D. Molkentin | Zendy; Jeanne James | Zendy; Jeffrey Robbins | Zendy

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A Critical Function for Ser-282 in Cardiac Myosin Binding Protein-C Phosphorylation and Cardiac Function

Author(s) -

Sakthivel Sadayappan,

James Gulick,

Hanna Osińska,

David Y. Barefield,

Friederike Cuello,

Metin Avkiran,

Valerie M. Lasko,

John N. Lorenz,

Marjorie Maillet,

Joel W. Martin,

Joan Heller Brown,

Donald M. Bers,

Jeffery D. Molkentin,

Jeanne James,

Jeffrey Robbins

Publication year - 2011

Publication title -

circulation research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.899

H-Index - 336

eISSN - 1524-4571

pISSN - 0009-7330

DOI - 10.1161/circresaha.111.242560

Subject(s) - phosphorylation , protein phosphorylation , biology , protein kinase a , calmodulin , kinase , serine , microbiology and biotechnology , biochemistry , enzyme

Cardiac myosin-binding protein-C (cMyBP-C) phosphorylation at Ser-273, Ser-282, and Ser-302 regulates myocardial contractility. In vitro and in vivo experiments suggest the nonequivalence of these sites and the potential importance of Ser-282 phosphorylation in modulating the protein's overall phosphorylation and myocardial function.

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