about
MYBPC1, an Emerging Myopathic Gene: What We Know and What We Need to LearnSarcomeric protein isoform transitions in cardiac muscle: a journey to heart failureThe N-terminal domains of myosin binding protein C can bind polymorphically to F-actin.Loss of actomyosin regulation in distal arthrogryposis myopathy due to mutant myosin binding protein-C slow.Signaling to myosin regulatory light chain in sarcomeresA human 3' miR-499 mutation alters cardiac mRNA targeting and function.Modulation of striated muscle contraction by binding of myosin binding protein C to actin.Cardiac myosin binding protein-C: redefining its structure and function.The Phosphorylation Profile of Myosin Binding Protein-C Slow is Dynamically Regulated in Slow-Twitch Muscles in Health and Disease.Myosin Binding Protein-C Slow Phosphorylation is Altered in Duchenne Dystrophy and Arthrogryposis Myopathy in Fast-Twitch Skeletal Muscles.Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.Conserved Asp-137 is important for both structure and regulatory functions of cardiac α-tropomyosin (α-TM) in a novel transgenic mouse model expressing α-TM-D137LCharacterization of the cardiac myosin binding protein-C phosphoproteome in healthy and failing human heartsImpaired contractile function due to decreased cardiac myosin binding protein C content in the sarcomereAlterations in Multi-Scale Cardiac Architecture in Association With Phosphorylation of Myosin Binding Protein-C.Myosin binding protein-C slow: a multifaceted family of proteins with a complex expression profile in fast and slow twitch skeletal muscles.Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.Cardiac myosin binding protein-C as a central target of cardiac sarcomere signaling: a special mini review series.cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.Targeted proteomics of myofilament phosphorylation and other protein posttranslational modifications.Tri-modal regulation of cardiac muscle relaxation; intracellular calcium decline, thin filament deactivation, and cross-bridge cycling kinetics.MYBPC1 mutations impair skeletal muscle function in zebrafish models of arthrogryposisMechanical aberrations in hypetrophic cardiomyopathy: emerging concepts.Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro.
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Signaling and myosin-binding protein C.
@ast
Signaling and myosin-binding protein C.
@en
Signaling and myosin-binding protein C.
@nl
type
label
Signaling and myosin-binding protein C.
@ast
Signaling and myosin-binding protein C.
@en
Signaling and myosin-binding protein C.
@nl
prefLabel
Signaling and myosin-binding protein C.
@ast
Signaling and myosin-binding protein C.
@en
Signaling and myosin-binding protein C.
@nl
P2860
P356
P1476
Signaling and myosin-binding protein C.
@en
P2093
Jeanne James
Jeffrey Robbins
P2860
P304
P356
10.1074/JBC.R110.171801
P407
P577
2011-01-21T00:00:00Z