Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulin-dependent protein kinases
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Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C.A critical function for Ser-282 in cardiac Myosin binding protein-C phosphorylation and cardiac functionSarcomeric protein isoform transitions in cardiac muscle: a journey to heart failureA novel, in-solution separation of endogenous cardiac sarcomeric proteins and identification of distinct charged variants of regulatory light chainRemoval of the N-terminal extension of cardiac troponin I as a functional compensation for impaired myocardial beta-adrenergic signalingAlteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscleCardiac myosin-binding protein-C phosphorylation and cardiac functionPKCβII modulation of myocyte contractile performance.Phosphorylation of yeast phosphatidylserine synthase in vivo and in vitro by cyclic AMP-dependent protein kinaseExpression of masticatory-specific isoforms of myosin heavy-chain, myosin-binding protein-C and tropomyosin in muscle fibers and satellite cell cultures of cat masticatory muscleMultiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.Autoimmune myocarditis induced in mice by cardiac C-protein. Cloning of complementary DNA encoding murine cardiac C-protein and partial characterization of the antigenic peptides.Identification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis.Myosin binding protein C interaction with actin: characterization and mapping of the binding site.Signaling and myosin-binding protein C.Mechanical unfolding of cardiac myosin binding protein-C by atomic force microscopy.Multiple forms of cardiac myosin-binding protein C exist and can regulate thick filament stabilityThe major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif.Alterations in Ca2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers.Phosphorylating Titin's Cardiac N2B Element by ERK2 or CaMKIIδ Lowers the Single Molecule and Cardiac Muscle ForceEffect of MyBP-C binding to actin on contractility in heart muscle.The multifunctional Ca(2+)/calmodulin-dependent protein kinase II delta (CaMKIIδ) phosphorylates cardiac titin's spring elements.Atrial remodelling in atrial fibrillation: CaMKII as a nodal proarrhythmic signalCardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heartCross-species mechanical fingerprinting of cardiac myosin binding protein-CBeta-adrenergic receptor signaling in the heart: role of CaMKII.Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filamentsCardiac myosin binding protein C phosphorylation in cardiac disease.Anchored protein kinase A signalling in cardiac cellular electrophysiology.Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function.Stage-specific changes in myofilament protein phosphorylation following myocardial infarction in mice.Deficient cMyBP-C protein expression during cardiomyocyte differentiation underlies human hypertrophic cardiomyopathy cellular phenotypes in disease specific human ES cell derived cardiomyocytes.The motif of human cardiac myosin-binding protein C is required for its Ca2+-dependent interaction with calmodulinBinding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay.Stability and kinetic properties of C5-domain from myosin binding protein C and its mutants.Using cAMP Sensors to Study Cardiac Nanodomains.
P2860
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P2860
Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulin-dependent protein kinases
description
1984 nî lūn-bûn
@nan
1984 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1984 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1984年の論文
@ja
1984年論文
@yue
1984年論文
@zh-hant
1984年論文
@zh-hk
1984年論文
@zh-mo
1984年論文
@zh-tw
1984年论文
@wuu
name
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@ast
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@en
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@nl
type
label
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@ast
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@en
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@nl
prefLabel
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@ast
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@en
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@nl
P1476
Phosphorylation of purified ca ...... ulin-dependent protein kinases
@en
P2093
P304
15587-15596
P407
P577
1984-12-01T00:00:00Z