S100A1 protein does not compete with calmodulin for ryanodine receptor binding but structurally alters the ryanodine receptor·calmodulin complex

S100A1 has been suggested as a therapeutic agent to enhance myocyte Ca2+ cycling in heart failure, but its molecular mode of action is poorly understood. Using FRET, we tested the hypothesis that S100A1 directly competes with calmodulin (CaM) for binding to intact, functional ryanodine receptors typ...

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Bibliographic Details
Main Authors:	Rebbeck, Robyn T. (Author) , Rohde, David (Author) , Most, Patrick (Author)
Format:	Article (Journal)
Language:	English
Published:	2016
In:	The journal of biological chemistry Year: 2016, Volume: 291, Issue: 30, Pages: 15896-15907
ISSN:	1083-351X
DOI:	10.1074/jbc.M115.713107
Online Access:	Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M115.713107 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0021925820397210
Author Notes:	Robyn T. Rebbeck, Florentin R. Nitu, David Rohde, Patrick Most, Donald M. Bers, David D. Thomas, and Razvan L. Cornea

S100A1 gene therapy in small and large animals by Most, Patrick (Author) , Raake, Philip (Author) , Weber, Christophe (Author) , Katus, Hugo (Author) , Pleger, Sven Torsten (Author) ,

in: Calcium-binding proteins and RAGE, (2013), Seite 407-420

Verlag, lizenzpflichtig, Volltext

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S100A1 protein does not compete with calmodulin for ryanodine receptor binding but structurally alters the ryanodine receptor·calmodulin complex

S100A1 gene therapy in small and large animals by Most, Patrick (Author) , Raake, Philip (Author) , Weber, Christophe (Author) , Katus, Hugo (Author) , Pleger, Sven Torsten (Author) ,

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