Cardiac myosin binding protein-C phosphorylation in a {beta}-myosin heavy chain background - Wikidata - wikimedia - TriplyDB

Cardiac myosin binding protein-C phosphorylation in a {beta}-myosin heavy chain background

Cardiac myosin binding protein-C phosphorylation in a {beta}-myosin heavy chain background

http://www.wikidata.org/entity/Q37130118

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Novel control of cardiac myofilament response to calcium by S-glutathionylation at specific sites of myosin binding protein C Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C Post-translational control of cardiac hemodynamics through myosin binding protein C Myosin binding protein C: implications for signal-transduction Molecular mechanisms of cardiomyopathy phenotypes associated with myosin light chain mutations A critical function for Ser-282 in cardiac Myosin binding protein-C phosphorylation and cardiac function 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 Novel role for p90 ribosomal S6 kinase in the regulation of cardiac myofilament phosphorylation In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament Determination of the critical residues responsible for cardiac myosin binding protein C's interactions Myosin binding protein C1: a novel gene for autosomal dominant distal arthrogryposis type 1 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.Remodeling of the heart in hypertrophy in animal models with myosin essential light chain mutations.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded 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.Independent modulation of contractile performance by cardiac troponin I Ser43 and Ser45 in the dynamic sarcomere.Two novel mutations in myosin binding protein C slow causing distal arthrogryposis type 2 in two large Han Chinese families may suggest important functional role of immunoglobulin domain C2.Synergistic effects between phosphorylation of phospholamban and troponin I promote relaxation at higher heart rate Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle Myosin binding protein-C slow is a novel substrate for protein kinase A (PKA) and C (PKC) in skeletal muscle.Cardiac myosin binding protein-C is a potential diagnostic biomarker for myocardial infarction.Cardiac myosin binding protein-C: redefining its structure and function.Knockout of p21-activated kinase-1 attenuates exercise-induced cardiac remodelling through altered calcineurin signalling Dissociation of structural and functional phenotypes in cardiac myosin-binding protein C conditional knockout mice.Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.Molecular mechanics of cardiac myosin-binding protein C in native thick filaments.Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.Increase in cardiac myosin binding protein-C plasma levels is a sensitive and cardiac-specific biomarker of myocardial infarction.A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin.An endogenously produced fragment of cardiac myosin-binding protein C is pathogenic and can lead to heart failure MYBPC3's alternate ending: consequences and therapeutic implications of a highly prevalent 25 bp deletion mutation cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.Cardiac myosin binding protein C phosphorylation in cardiac disease.A change of heart: oxidative stress in governing muscle function?Phosphoregulation of Cardiac Inotropy via Myosin Binding Protein-C During Increased Pacing Frequency or β1-Adrenergic Stimulation.β-adrenergic effects on cardiac myofilaments and contraction in an integrated rabbit ventricular myocyte model.

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Cardiac myosin binding protein-C phosphorylation in a {beta}-myosin heavy chain background

http://www.wikidata.org/entity/Q37130118

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 23 February 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Cardiac myosin binding protein ...... -myosin heavy chain background

@en

Cardiac myosin binding protein ...... myosin heavy chain background.

@nl

type

label

Cardiac myosin binding protein ...... -myosin heavy chain background

@en

Cardiac myosin binding protein ...... myosin heavy chain background.

@nl

prefLabel

Cardiac myosin binding protein ...... -myosin heavy chain background

@en

Cardiac myosin binding protein ...... myosin heavy chain background.

@nl

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CIRCULATIONAHA.108.798983

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Cardiac myosin binding protein ...... -myosin heavy chain background

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James Gulick

http://www.w3.org/2001/XMLSchema#string

Jeffrey Robbins

http://www.w3.org/2001/XMLSchema#string

John N Lorenz

http://www.w3.org/2001/XMLSchema#string

Michelle Sargent

http://www.w3.org/2001/XMLSchema#string

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

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

Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy

Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C

Cardiac myosin-binding protein C (MyBP-C): identification of protein kinase A and protein kinase C phosphorylation sites

Length and protein kinase A modulations of myocytes in cardiac myosin binding protein C-deficient mice

Decreased phosphorylation levels of cardiac myosin-binding protein-C in human and experimental heart failure

Dilated cardiomyopathy in homozygous myosin-binding protein-C mutant mice

Cardiac myosin binding protein C phosphorylation is cardioprotective

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1253-1262

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scholarly article

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10.1161/CIRCULATIONAHA.108.798983

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9

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119

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Jeffery D. Molkentin

Sakthivel Sadayappan

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2009-02-23T00:00:00Z

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19237661

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phosphorylation

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2656413

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