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Cardiac myosin-binding protein-C phosphorylation and cardiac function

Cardiac myosin-binding protein-C phosphorylation and cardiac function

http://www.wikidata.org/entity/Q28584863

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Post-translational control of cardiac hemodynamics through myosin binding protein C Myosin binding protein C: implications for signal-transduction Cardiac MyBP-C regulates the rate and force of contraction in mammalian myocardium Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAIN MYBPC1, an Emerging Myopathic Gene: What We Know and What We Need to Learn A critical function for Ser-282 in cardiac Myosin binding protein-C phosphorylation and cardiac function Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state How do MYBPC3 mutations cause hypertrophic cardiomyopathy?Adrenergic stress reveals septal hypertrophy and proteasome impairment in heterozygous Mybpc3-targeted knock-in mice Pathogenic properties of the N-terminal region of cardiac myosin binding protein-C in vitro Protein kinase D increases maximal Ca2+-activated tension of cardiomyocyte contraction by phosphorylation of cMyBP-C-Ser315 Distinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cycling In vivo left ventricular functional capacity is compromised in cMyBP-C null mice Tetrahydrobiopterin improves diastolic dysfunction by reversing changes in myofilament properties Rescue of cardiomyopathy through U7snRNA-mediated exon skipping in Mybpc3-targeted knock-in mice Tropomyosin de-phosphorylation in the heart: what are the consequences?Novel role for p90 ribosomal S6 kinase in the regulation of cardiac myofilament phosphorylation Ablation of ventricular myosin regulatory light chain phosphorylation in mice causes cardiac dysfunction in situ and affects neighboring myofilament protein phosphorylation Myocardial infarction-induced N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardium In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament Cardiac myosin binding protein C phosphorylation is cardioprotective Determination of the critical residues responsible for cardiac myosin binding protein C's interactions Diastolic dysfunction in spontaneous type 2 diabetes rhesus monkeys: a study using echocardiography and magnetic resonance imaging.Removal of the cardiac troponin I N-terminal extension improves cardiac function in aged mice.Quantitative comparison of sarcomeric phosphoproteomes of neonatal and adult rat hearts.Protein 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 manner Myosin binding protein C1: a novel gene for autosomal dominant distal arthrogryposis type 1 The curious role of sarcomeric proteins in control of diverse processes in cardiac myocytes.Cardiac remodeling in fish: strategies to maintain heart function during temperature Change 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.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 manner Protein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosin-binding protein C Identification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis.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.Kinetics of cardiac myosin isoforms in mouse myocardium are affected differently by presence of myosin binding protein-C Signaling and myosin-binding protein C.Myosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cells

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Cardiac myosin-binding protein-C phosphorylation and cardiac function

http://www.wikidata.org/entity/Q28584863

description

2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2005

@ast

im November 2005 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2005/11/25)

@sk

vědecký článek publikovaný v roce 2005

@cs

wetenschappelijk artikel (gepubliceerd op 2005/11/25)

@nl

наукова стаття, опублікована в листопаді 2005

@uk

مقالة علمية (نشرت في 25-11-2005)

@ar

name

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@ast

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@en

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@nl

type

label

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@ast

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@en

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@nl

prefLabel

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@ast

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@en

Cardiac myosin-binding protein-C phosphorylation and cardiac function

@nl

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01.RES.0000190605.79013.4D

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Circulation Research

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Cardiac myosin-binding protein-C phosphorylation and cardiac function

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P2093

Christine E Seidman

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Gerald W Dorn

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Hanna Osinska

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Harvey S Hahn

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James Gulick

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Jeffrey Robbins

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Jonathan G Seidman

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Lisa A Martin

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Raisa Klevitsky

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P2860

Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C

Protein kinase Calpha negatively regulates systolic and diastolic function in pathological hypertrophy

Cardiac myosin binding protein C: its role in physiology and disease

Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy

Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?

Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2

Cardiac myosin binding protein C

Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins

A calcineurin-dependent transcriptional pathway for cardiac hypertrophy

Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulin-dependent protein kinases

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1156-1163

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10.1161/01.RES.0000190605.79013.4D

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11

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97

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Sakthivel Sadayappan

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2005-10-13T00:00:00Z

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16224063

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Myosin-binding protein C, cardiac-type

phosphorylation

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1343494

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