Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?
about
Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein CMolecular pathology of familial hypertrophic cardiomyopathy caused by mutations in the cardiac myosin binding protein C gene.Identification of a new missense mutation in MyBP-C associated with hypertrophic cardiomyopathyNovel splice donor site mutation in the cardiac myosin-binding protein-C gene in familial hypertrophic cardiomyopathy. Characterization Of cardiac transcript and proteinPost-translational control of cardiac hemodynamics through myosin binding protein CMyosin binding protein C: implications for signal-transductionCardiac 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 C1Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C.A critical function for Ser-282 in cardiac Myosin binding protein-C phosphorylation and cardiac functionTop-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation stateSarcomeric protein isoform transitions in cardiac muscle: a journey to heart failureDistinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cyclingGSK3β phosphorylates newly identified site in the proline-alanine-rich region of cardiac myosin-binding protein C and alters cross-bridge cycling kinetics in human: short communicationUnderstanding the organisation and role of myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscleNovel role for p90 ribosomal S6 kinase in the regulation of cardiac myofilament phosphorylationIn the thick of it: HCM-causing mutations in myosin binding proteins of the thick filamentDilated cardiomyopathy in homozygous myosin-binding protein-C mutant miceCardiac myosin binding protein C phosphorylation is cardioprotectiveAlteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscleCardiac myosin-binding protein-C phosphorylation and cardiac functionDirect visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle.The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.Translation elongation factor eEF1A binds to a novel myosin binding protein-C-like protein.Adverse events in families with hypertrophic or dilated cardiomyopathy and mutations in the MYBPC3 geneProtein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific mannerFunctional differences between the N-terminal domains of mouse and human myosin binding protein-C.The molecular genetic basis for 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.The origins of hypertrophic cardiomyopathy-causing mutations in two South African subpopulations: a unique profile of both independent and founder eventsSurviving the infarct: A profile of cardiac myosin binding protein-C pathogenicity, diagnostic utility, and proteomics in the ischemic myocardium.Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerIdentification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis.Myosin binding protein C interaction with actin: characterization and mapping of the binding site.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.Identifying sarcomere gene mutations in hypertrophic cardiomyopathy: a personal history
P2860
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P2860
Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1995年の論文
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1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Phosphorylation switches speci ...... ulator of cardiac contraction?
@ast
Phosphorylation switches speci ...... ulator of cardiac contraction?
@en
Phosphorylation switches speci ...... ulator of cardiac contraction?
@nl
type
label
Phosphorylation switches speci ...... ulator of cardiac contraction?
@ast
Phosphorylation switches speci ...... ulator of cardiac contraction?
@en
Phosphorylation switches speci ...... ulator of cardiac contraction?
@nl
prefLabel
Phosphorylation switches speci ...... ulator of cardiac contraction?
@ast
Phosphorylation switches speci ...... ulator of cardiac contraction?
@en
Phosphorylation switches speci ...... ulator of cardiac contraction?
@nl
P2093
P2860
P3181
P1433
P1476
Phosphorylation switches speci ...... ulator of cardiac contraction?
@en
P2093
P2860
P304
P3181
P407
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1995-05-01T00:00:00Z