Phospholamban: a major determinant of the cardiac force-frequency relationship
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Calcium sensitivity, force frequency relationship and cardiac troponin I: critical role of PKA and PKC phosphorylation sitesPhospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex.CaMKII inhibition targeted to the sarcoplasmic reticulum inhibits frequency-dependent acceleration of relaxation and Ca2+ current facilitation.A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Toward an integrative computational model of the Guinea pig cardiac myocyte.Computational analysis of the regulation of Ca(2+) dynamics in rat ventricular myocytesDeterminants of frequency-dependent contraction and relaxation of mammalian myocardium.Endocardial endothelium is a key determinant of force-frequency relationship in rat ventricular myocardiumThe role of CaMKII regulation of phospholamban activity in heart disease.CaMKII effects on inotropic but not lusitropic force frequency responses require phospholamban.Calmodulin kinase II, sarcoplasmic reticulum Ca2+ leak, and atrial fibrillation.The heart in Duchenne muscular dystrophy: early detection of contractile performance alteration.Contractility Measurements on Isolated Papillary Muscles for the Investigation of Cardiac Inotropy in Mice.Characterization of calumenin-SERCA2 interaction in mouse cardiac sarcoplasmic reticulum.Abnormal contractile activity and calcium cycling in cardiac myocytes isolated from DMPK knockout mice.Frequency-dependent acceleration of relaxation in mammalian heart: a property not relying on phospholamban and SERCA2a phosphorylation.Reduced oxygen supply explains the negative force-frequency relation and the positive inotropic effect of adenosine in buffer-perfused hearts.Differential effects of phospholamban and Ca2+/calmodulin-dependent kinase II on [Ca2+]i transients in cardiac myocytes at physiological stimulation frequencies.ATP splitting by half the cross-bridges can explain the twitch energetics of mouse papillary muscle.Roles of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics.An analysis of deformation-dependent electromechanical coupling in the mouse heart.
P2860
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P2860
Phospholamban: a major determinant of the cardiac force-frequency relationship
description
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artikull shkencor
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artículu científicu espublizáu en 2000
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im Januar 2000 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
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wetenschappelijk artikel
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наукова стаття, опублікована в січні 2000
@uk
مقالة علمية (نشرت عام 2000)
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name
Phospholamban: a major determinant of the cardiac force-frequency relationship
@ast
Phospholamban: a major determinant of the cardiac force-frequency relationship
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Phospholamban: a major determinant of the cardiac force-frequency relationship
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type
label
Phospholamban: a major determinant of the cardiac force-frequency relationship
@ast
Phospholamban: a major determinant of the cardiac force-frequency relationship
@en
Phospholamban: a major determinant of the cardiac force-frequency relationship
@nl
prefLabel
Phospholamban: a major determinant of the cardiac force-frequency relationship
@ast
Phospholamban: a major determinant of the cardiac force-frequency relationship
@en
Phospholamban: a major determinant of the cardiac force-frequency relationship
@nl
P2093
P2860
P1476
Phospholamban: a major determinant of the cardiac force-frequency relationship
@en
P2093
E. G. Kranias
W. F. Bluhm
W. H. Dillmann
P2860
P304
P356
10.1152/AJPHEART.2000.278.1.H249
P577
2000-01-01T00:00:00Z