Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod
about
The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle.Loss of actomyosin regulation in distal arthrogryposis myopathy due to mutant myosin binding protein-C slow.Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes.Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Signaling and myosin-binding protein C.Muscle giants: molecular scaffolds in sarcomerogenesis.Cardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and functionA hypertrophic cardiomyopathy-associated MYBPC3 mutation common in populations of South Asian descent causes contractile dysfunctionMechanical unfolding of cardiac myosin binding protein-C by atomic force microscopy.Myosin binding protein-C: a regulator of actomyosin interaction in striated muscleEffects of pathogenic proline mutations on myosin assembly.Myosin binding protein-C phosphorylation is the principal mediator of protein kinase A effects on thick filament structure in myocardium.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Cross-species mechanical fingerprinting of cardiac myosin binding protein-CCardiac myosin-binding protein C decorates F-actin: implications for cardiac function.Molecular modulation of actomyosin function by cardiac myosin-binding protein C.MYBPC3's alternate ending: consequences and therapeutic implications of a highly prevalent 25 bp deletion mutationHeavy and light roles: myosin in the morphogenesis of the heart.Structural implications of β-cardiac myosin heavy chain mutations in human disease.Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Normal cardiac contraction in mice lacking the proline-alanine rich region and C1 domain of cardiac myosin binding protein CCardiomyopathy mutations in the tail of β-cardiac myosin modify the coiled-coil structure and affect integration into thick filaments in muscle sarcomeres in adult cardiomyocytes.An evolutionary analysis of flightin reveals a conserved motif unique and widespread in Pancrustacea.A mutation in the beta-myosin rod associated with hypertrophic cardiomyopathy has an unexpected molecular phenotype.Association of cardiac myosin-binding protein-C with the ryanodine receptor channel - putative retrograde regulation?
P2860
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P2860
Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod
description
2007 nî lūn-bûn
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2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2007 թվականի հունվարին հրատարակված գիտական հոդված
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年學術文章
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name
Localization of the binding si ...... ng protein-C on the myosin rod
@ast
Localization of the binding si ...... ng protein-C on the myosin rod
@en
Localization of the binding si ...... ng protein-C on the myosin rod
@nl
type
label
Localization of the binding si ...... ng protein-C on the myosin rod
@ast
Localization of the binding si ...... ng protein-C on the myosin rod
@en
Localization of the binding si ...... ng protein-C on the myosin rod
@nl
prefLabel
Localization of the binding si ...... ng protein-C on the myosin rod
@ast
Localization of the binding si ...... ng protein-C on the myosin rod
@en
Localization of the binding si ...... ng protein-C on the myosin rod
@nl
P2860
P356
P1433
P1476
Localization of the binding si ...... ng protein-C on the myosin rod
@en
P2093
Charles Redwood
P2860
P304
P356
10.1042/BJ20060500
P407
P577
2007-01-01T00:00:00Z