Cooperative cross-bridge activation of thin filaments contributes to the Frank-Starling mechanism in cardiac muscle.
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Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridgesFilament compliance influences cooperative activation of thin filaments and the dynamics of force production in skeletal muscleTransgenic overexpression of ribonucleotide reductase improves cardiac performance.Axial and radial forces of cross-bridges depend on lattice spacing.Myofilament length dependent activationIn situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation.The role of thin filament cooperativity in cardiac length-dependent calcium activation.Mechanistic heterogeneity in contractile properties of α-tropomyosin (TPM1) mutants associated with inherited cardiomyopathies.A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Thick-to-thin filament surface distance modulates cross-bridge kinetics in Drosophila flight muscleEnhanced Ca2+ binding of cardiac troponin reduces sarcomere length dependence of contractile activation independently of strong crossbridges.Deletion of 1-43 amino acids in cardiac myosin essential light chain blunts length dependency of Ca(2+) sensitivity and cross-bridge detachment kinetics.Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips.Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm (20ΔRRM) Mice.Modeling to link regional myocardial work, metabolism and blood flows.Exploring cardiac biophysical properties.Distinct contributions of the thin and thick filaments to length-dependent activation in heart muscle.The effect of cardiomyopathy mutation (R97L) in mouse cardiac troponin T on the muscle length-mediated recruitment of crossbridges is modified divergently by α- and β-myosin heavy chain.Omecamtiv Mecarbil Abolishes Length-Mediated Increase in Guinea Pig Cardiac Myofiber Ca2+ Sensitivity.The length-tension curve in muscle depends on lattice spacing.Myosin MgADP release rate decreases at longer sarcomere length to prolong myosin attachment time in skinned rat myocardium.Cardiomyopathy mutation (F88L) in troponin T abolishes length dependency of myofilament Ca sensitivity
P2860
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P2860
Cooperative cross-bridge activation of thin filaments contributes to the Frank-Starling mechanism in cardiac muscle.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年學術文章
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2009年學術文章
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name
Cooperative cross-bridge activ ...... g mechanism in cardiac muscle.
@ast
Cooperative cross-bridge activ ...... g mechanism in cardiac muscle.
@en
type
label
Cooperative cross-bridge activ ...... g mechanism in cardiac muscle.
@ast
Cooperative cross-bridge activ ...... g mechanism in cardiac muscle.
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prefLabel
Cooperative cross-bridge activ ...... g mechanism in cardiac muscle.
@ast
Cooperative cross-bridge activ ...... g mechanism in cardiac muscle.
@en
P2860
P1433
P1476
Cooperative cross-bridge activ ...... ng mechanism in cardiac muscle
@en
P2093
P2860
P304
P356
10.1016/J.BPJ.2009.02.018
P407
P577
2009-05-01T00:00:00Z