Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?
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Novel control of cardiac myofilament response to calcium by S-glutathionylation at specific sites of myosin binding protein CCardiac MyBP-C regulates the rate and force of contraction in mammalian myocardiumGSK3β phosphorylates newly identified site in the proline-alanine-rich region of cardiac myosin-binding protein C and alters cross-bridge cycling kinetics in human: short communicationCardiac 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-CMyosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cellsThe myosin mesa and a possible unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathyMyosin-binding protein C corrects an intrinsic inhomogeneity in cardiac excitation-contraction coupling.Cardiac myosin binding protein C regulates postnatal myocyte cytokinesis.Cardiac Myosin-binding Protein C and Troponin-I Phosphorylation Independently Modulate Myofilament Length-dependent Activation.Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent ActivationObscurin is required for ankyrinB-dependent dystrophin localization and sarcolemma integrity.Titin strain contributes to the Frank-Starling law of the heart by structural rearrangements of both thin- and thick-filament proteins.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.S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.Impaired contractile function due to decreased cardiac myosin binding protein C content in the sarcomereMolecular modulation of actomyosin function by cardiac myosin-binding protein C.Cardiac myosin binding protein-C as a central target of cardiac sarcomere signaling: a special mini review series.Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filamentsCardiac myosin-binding protein C: hypertrophic cardiomyopathy mutations and structure-function relationships.Myofilaments: Movers and Rulers of the Sarcomere.Phosphorylation of Ser283 enhances the stiffness of the tropomyosin head-to-tail overlap domain.Historical perspective on heart function: the Frank-Starling Law.Normal cardiac contraction in mice lacking the proline-alanine rich region and C1 domain of cardiac myosin binding protein COrientation of the N- and C-terminal lobes of the myosin regulatory light chain in cardiac muscle.Myosin filament activation in the heart is tuned to the mechanical task.Distinct contributions of the thin and thick filaments to length-dependent activation in heart muscle.Orientation of myosin binding protein C in the cardiac muscle sarcomere determined by domain-specific immuno-EM.Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.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.Force generation by skeletal muscle is controlled by mechanosensing in myosin filaments.Thick Filament Mechano-Sensing in Skeletal and Cardiac Muscles: A Common Mechanism Able to Adapt the Energetic Cost of the Contraction to the Task.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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Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
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artikull shkencor
@sq
artículo científico
@es
name
Structure, interactions and fu ...... what, with what, and to whom?
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type
label
Structure, interactions and fu ...... what, with what, and to whom?
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prefLabel
Structure, interactions and fu ...... what, with what, and to whom?
@en
P2860
P1476
Structure, interactions and fu ...... what, with what, and to whom?
@en
P2093
Mathias Gautel
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P2888
P356
10.1007/S10974-012-9291-Z
P577
2012-04-20T00:00:00Z
P6179
1019621013