Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
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Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein CCounteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein PhosphatasesContractile apparatus dysfunction early in the pathophysiology of diabetic cardiomyopathyMyosin binding protein C: implications for signal-transductionStructural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAINMYBPC1, an Emerging Myopathic Gene: What We Know and What We Need to LearnDiastolic dysfunctionA critical function for Ser-282 in cardiac Myosin binding protein-C phosphorylation and cardiac functionAdrenergic stress reveals septal hypertrophy and proteasome impairment in heterozygous Mybpc3-targeted knock-in miceIncreased myofilament Ca2+ sensitivity and diastolic dysfunction as early consequences of Mybpc3 mutation in heterozygous knock-in micePathogenic properties of the N-terminal region of cardiac myosin binding protein-C in vitroProtein kinase D increases maximal Ca2+-activated tension of cardiomyocyte contraction by phosphorylation of cMyBP-C-Ser315Tetrahydrobiopterin improves diastolic dysfunction by reversing changes in myofilament propertiesRescue of cardiomyopathy through U7snRNA-mediated exon skipping in Mybpc3-targeted knock-in miceNovel role for p90 ribosomal S6 kinase in the regulation of cardiac myofilament phosphorylationMyocardial infarction-induced N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardiumIn the thick of it: HCM-causing mutations in myosin binding proteins of the thick filamentDirect visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle.Protein Kinases as Drug Development Targets for Heart Disease TherapyNext-generation sequencing identifies pathogenic and modifier mutations in a consanguineous Chinese family with hypertrophic cardiomyopathy.Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.Surviving the infarct: A profile of cardiac myosin binding protein-C pathogenicity, diagnostic utility, and proteomics in the ischemic myocardium.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerImpact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue.FHL2 expression and variants in hypertrophic cardiomyopathy.Top-down mass spectrometry of cardiac myofilament proteins in health and disease.Cardiac myosin binding protein C phosphorylation affects cross-bridge cycle's elementary steps in a site-specific manner.Signaling and myosin-binding protein C.Redox signaling and cardiac sarcomeresSignaling to myosin regulatory light chain in sarcomeresMyosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cellsEffects of cardiac Myosin binding protein-C on actin motility are explained with a drag-activation-competition modelCardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and functionAltered interactions between cardiac myosin binding protein-C and α-cardiac actin variants associated with cardiomyopathiesPKCα-specific phosphorylation of the troponin complex in human myocardium: a functional and proteomics analysis.A hypertrophic cardiomyopathy-associated MYBPC3 mutation common in populations of South Asian descent causes contractile dysfunctionRoles for cardiac MyBP-C in maintaining myofilament lattice rigidity and prolonging myosin cross-bridge lifetime.Biochemical and myofilament responses of the right ventricle to severe pulmonary hypertension.Ca²⁺ sensitization of cardiac myofilament proteins contributes to exercise training-enhanced myocardial function in a porcine model of chronic occlusion.
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P2860
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 03 December 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
@en
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
@nl
type
label
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
@en
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
@nl
prefLabel
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
@en
Phosphorylation and function of cardiac myosin binding protein-C in health and disease.
@nl
P1476
Phosphorylation and function of cardiac myosin binding protein-C in health and disease
@en
P2093
David Barefield
Sakthivel Sadayappan
P304
P356
10.1016/J.YJMCC.2009.11.014
P577
2009-12-03T00:00:00Z