Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle
about
Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein CDissecting the N-terminal myosin binding site of human cardiac myosin-binding protein C. Structure and myosin binding of domain C2Contractile apparatus dysfunction early in the pathophysiology of diabetic cardiomyopathyUnderstanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motorCardiac MyBP-C regulates the rate and force of contraction in mammalian myocardiumMyosin Binding Protein C Positioned to Play a Key Role in Regulation of Muscle Contraction: Structure and Interactions of Domain C1Hypercontractile properties of cardiac muscle fibers in a knock-in mouse model of cardiac myosin-binding protein-CTop-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation stateIn vivo left ventricular functional capacity is compromised in cMyBP-C null miceRadial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-CAblation of ventricular myosin regulatory light chain phosphorylation in mice causes cardiac dysfunction in situ and affects neighboring myofilament protein phosphorylationCardiac myosin binding protein C phosphorylation is cardioprotectiveCardiac myosin-binding protein-C phosphorylation and cardiac functionPKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosinProteomic signature of muscle fibre hyperplasia in response to faba bean intake in grass carp.The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Expression of masticatory-specific isoforms of myosin heavy-chain, myosin-binding protein-C and tropomyosin in muscle fibers and satellite cell cultures of cat masticatory muscleRegulation of contraction in mammalian striated muscles--the plot thick-ens.Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.Top-down mass spectrometry of cardiac myofilament proteins in health and disease.GENETIC CAUSES OF DILATED CARDIOMYOPATHY.Roles for cardiac MyBP-C in maintaining myofilament lattice rigidity and prolonging myosin cross-bridge lifetime.Constitutive phosphorylation of cardiac myosin regulatory light chain in vivoMyosin binding protein C: structural abnormalities in familial hypertrophic cardiomyopathy.Phosphorylation of contractile proteins in response to alpha- and beta-adrenergic stimulation in neonatal cardiomyocytesCardiac myosin binding protein-C: redefining its structure and function.Multiple forms of cardiac myosin-binding protein C exist and can regulate thick filament stabilityAnchoring proteins as regulators of signaling pathways.Effect of MyBP-C binding to actin on contractility in heart muscle.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Ablation of cardiac myosin-binding protein-C accelerates contractile kinetics in engineered cardiac tissue.Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathyCardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heartSite-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics.Cardiac myosin-binding protein C: A protein once at loose ends finds its regulatory groove.Human heart beta-adrenoceptors: beta1-adrenoceptor diversification through 'affinity states' and polymorphism.Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function.
P2860
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P2860
Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle
description
1996 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans les Procee ...... f the United States of America
@fr
artículu científicu espublizáu en 1996
@ast
im August 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1996/08/20)
@sk
vědecký článek publikovaný v roce 1996
@cs
wetenschappelijk artikel (gepubliceerd op 1996/08/20)
@nl
наукова стаття, опублікована в серпні 1996
@uk
name
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@ast
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@en
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@nl
type
label
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@ast
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@en
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@nl
prefLabel
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@ast
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@en
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@nl
P2860
P3181
P356
P1476
Alteration of myosin cross bri ...... ng protein C in cardiac muscle
@en
P2093
A. Weisberg
S. Winegrad
P2860
P304
P3181
P356
10.1073/PNAS.93.17.8999
P407
P577
1996-08-20T00:00:00Z