PKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosin
about
Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein CDistinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cyclingNew insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin IIn vivo left ventricular functional capacity is compromised in cMyBP-C null miceAblation of myosin-binding protein-C accelerates force development in mouse myocardiumAblation of the cardiac-specific gene leucine-rich repeat containing 10 (Lrrc10) results in dilated cardiomyopathyProtein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Cycling cross-bridges increase myocardial stiffness at submaximal levels of Ca2+ activation.Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle.Protein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosin-binding protein CEffects of low-level α-myosin heavy chain expression on contractile kinetics in porcine myocardiumLKB1/Mo25/STRAD uniquely impacts sarcomeric contractile function and posttranslational modification.A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Magnitude of length-dependent changes in contractile properties varies with titin isoform in rat ventricles.Activation dependence of stretch activation in mouse skinned myocardium: implications for ventricular functionPost-translational modifications of myofilament proteins involved in length-dependent prolongation of relaxation in rabbit right ventricular myocardiumSex dimorphisms of crossbridge cycling kinetics in transgenic hypertrophic cardiomyopathy miceStriated muscle tropomyosin isoforms differentially regulate cardiac performance and myofilament calcium sensitivity.Instability in the central region of tropomyosin modulates the function of its overlapping ends.Cardiac tissue structure, properties, and performance: a materials science perspective.Peroxisome proliferator-activated receptor-α expression induces alterations in cardiac myofilaments in a pressure-overload model of hypertrophy.β-adrenergic effects on cardiac myofilaments and contraction in an integrated rabbit ventricular myocyte model.Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I.Altered Right Ventricular Mechanical Properties Are Afterload Dependent in a Rodent Model of Bronchopulmonary Dysplasia.The inotropic effect of nitric oxide on mammalian papillary muscle is dependent on the level of beta1-adrenergic stimulation.Protein kinase C and A sites on troponin I regulate myofilament Ca2+ sensitivity and ATPase activity in the mouse myocardium.Cardiac myofibrillar contractile properties during the progression from hypertension to decompensated heart failure.Rate of tension redevelopment is not modulated by sarcomere length in permeabilized human, murine, and porcine cardiomyocytes.Monophosphorylation of cardiac troponin-I at Ser23/24 is sufficient to regulate cardiac myofibrillar Ca2+ sensitivity and calpain-induced proteolysis.Differential roles of regulatory light chain and myosin binding protein-C phosphorylations in the modulation of cardiac force development.
P2860
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P2860
PKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosin
description
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2001
@ast
im Juni 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/06/01)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/06/01)
@nl
наукова стаття, опублікована в червні 2001
@uk
مقالة علمية (نشرت في يونيو 2001)
@ar
name
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@ast
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@en
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@nl
type
label
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@ast
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@en
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@nl
prefLabel
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@ast
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@en
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@nl
P2093
P2860
P1476
PKA accelerates rate of force ...... ing alpha- or beta-tropomyosin
@en
P2093
D. F. Wieczorek
D. P. Fitzsimons
J. R. Patel
M. Muthuchamy
R. L. Moss
S. H. Buck
P2860
P304
H2732–2739
P356
10.1152/AJPHEART.2001.280.6.H2732
P577
2001-06-01T00:00:00Z