Hypercontractile properties of cardiac muscle fibers in a knock-in mouse model of cardiac myosin-binding protein-C
about
Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo.Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2.Myosin binding protein C: implications for signal-transductionThe N-terminal domains of myosin binding protein C can bind polymorphically to F-actin.MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerMyosin binding protein C: structural abnormalities in familial hypertrophic cardiomyopathy.Cardiac myosin binding protein-C: redefining its structure and function.Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.Myofibrillar remodeling in cardiac hypertrophy, heart failure and cardiomyopathies.Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathyBuild it up-Tear it down: protein quality control in the cardiac sarcomere.Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins.In vivo definition of cardiac myosin-binding protein C's critical interactions with myosinMolecular basis of hereditary cardiomyopathy: abnormalities in calcium sensitivity, stretch response, stress response and beyond.Increased myofilament Ca2+-sensitivity and arrhythmia susceptibility.Cardiac slices as a predictive tool for arrhythmogenic potential of drugs and chemicals.Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Mendelian forms of structural cardiovascular disease.Normal cardiac contraction in mice lacking the proline-alanine rich region and C1 domain of cardiac myosin binding protein CCardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay.Differential contribution of cardiac sarcomeric proteins in the myofibrillar force response to stretch.Orientation of myosin binding protein C in the cardiac muscle sarcomere determined by domain-specific immuno-EM.Hypertrophic cardiomyopathy mutations increase myofilament Ca2+ buffering, alter intracellular Ca2+ handling and stimulate Ca2+ dependent signalling.
P2860
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P2860
Hypercontractile properties of cardiac muscle fibers in a knock-in mouse model of cardiac myosin-binding protein-C
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hypercontractile properties of ...... rdiac myosin-binding protein-C
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Hypercontractile properties of ...... rdiac myosin-binding protein-C
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Hypercontractile properties of ...... rdiac myosin-binding protein-C
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Hypercontractile properties of ...... rdiac myosin-binding protein-C
@ast
Hypercontractile properties of ...... rdiac myosin-binding protein-C
@en
Hypercontractile properties of ...... rdiac myosin-binding protein-C
@nl
prefLabel
Hypercontractile properties of ...... rdiac myosin-binding protein-C
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Hypercontractile properties of ...... rdiac myosin-binding protein-C
@en
Hypercontractile properties of ...... rdiac myosin-binding protein-C
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P2093
P2860
P3181
P356
P1476
Hypercontractile properties of ...... rdiac myosin-binding protein-C
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P2093
P2860
P304
P3181
P356
10.1074/JBC.M008691200
P407
P577
2001-02-16T00:00:00Z