Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism. - Wikidata - awgldk - TriplyDB

Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.

Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.

http://www.wikidata.org/entity/Q37587694

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Cardiac MyBP-C regulates the rate and force of contraction in mammalian myocardium The energetic cost of contraction is higher in the myocardium of patients with hypertrophic cardiomyopathy C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.Myosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cells Effects of cardiac Myosin binding protein-C on actin motility are explained with a drag-activation-competition model Myosin-binding protein C corrects an intrinsic inhomogeneity in cardiac excitation-contraction coupling.ADP-stimulated contraction: A predictor of thin-filament activation in cardiac disease.Cardiac Myosin-binding Protein C and Troponin-I Phosphorylation Independently Modulate Myofilament Length-dependent Activation.Titin strain contributes to the Frank-Starling law of the heart by structural rearrangements of both thin- and thick-filament proteins.Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathy Site-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics.Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.Slowing of contractile kinetics by myosin-binding protein C can be explained by its cooperative binding to the thin filament.Structure, sarcomeric organization, and thin filament binding of cardiac myosin-binding protein-C.Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments Cardiac myosin binding protein-C Ser302 phosphorylation regulates cardiac β-adrenergic reserve The genetic landscape of cardiomyopathy and its role in heart failure.Thin Filament Structure and the Steric Blocking Model.The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position.The genetic basis of hypertrophic cardiomyopathy in cats and humans.Tropomyosin Structure, Function, and Interactions: A Dynamic Regulator.Myofilaments: Movers and Rulers of the Sarcomere.Myofilament protein dynamics modulate EAD formation in human hypertrophic cardiomyopathy.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 C Distinct contributions of the thin and thick filaments to length-dependent activation in heart muscle.The propensity for tropomyosin twisting in the presence and absence of F-actin.Modulation of thin filament activation of myosin ATP hydrolysis by N-terminal domains of cardiac myosin binding protein-C.Orientation of myosin binding protein C in the cardiac muscle sarcomere determined by domain-specific immuno-EM.Omecamtiv mercabil and blebbistatin modulate cardiac contractility by perturbing the regulatory state of the myosin filament.Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner.Sarcomeric protein modification during adrenergic stress enhances cross-bridge kinetics and cardiac output.Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin-Myosin Interaction Using In Vitro Motility Assay.TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions.Structural and functional effects of myosin-binding protein-C phosphorylation in heart muscle are not mimicked by serine-to-aspartate substitutions

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Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.

http://www.wikidata.org/entity/Q37587694

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 29 January 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Myosin-binding protein C displ ...... d by an independent mechanism.

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Myosin-binding protein C displ ...... d by an independent mechanism.

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Myosin-binding protein C displ ...... d by an independent mechanism.

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Myosin-binding protein C displ ...... d by an independent mechanism.

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Myosin-binding protein C displ ...... d by an independent mechanism.

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Myosin-binding protein C displ ...... d by an independent mechanism.

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PNAS.1316001111

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Proceedings of the National Academy of Sciences of the United States of America

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Myosin-binding protein C displ ...... d by an independent mechanism.

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David M Warshaw

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Hope Y Yu

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James Gulick

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Jeffrey Robbins

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Ji Young Mun

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Larry S Tobacman

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Michael J Previs

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Roger Craig

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Samantha Beck Previs

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P2860

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

The interaction of C-protein with heavy meromyosin and subfragment-2

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

Myosin Binding Protein C Positioned to Play a Key Role in Regulation of Muscle Contraction: Structure and Interactions of Domain C1

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

UCSF Chimera--a visualization system for exploratory research and analysis

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

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

Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice

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2170-2175

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scholarly article

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10.1073/PNAS.1316001111

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2014-01-29T00:00:00Z

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