Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24.
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The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin CLength-dependent activation is modulated by cardiac troponin I bisphosphorylation at Ser23 and Ser24 but not by Thr143 phosphorylationPhosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.Computational studies of the effect of the S23D/S24D troponin I mutation on cardiac troponin structural dynamics.Effects of HCM cTnI mutation R145G on troponin structure and modulation by PKA phosphorylation elucidated by molecular dynamics simulationsCardiac Myosin-binding Protein C and Troponin-I Phosphorylation Independently Modulate Myofilament Length-dependent Activation.Titin strain contributes to the Frank-Starling law of the heart by structural rearrangements of both thin- and thick-filament proteins.Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filamentsMolecule specific effects of PKA-mediated phosphorylation on rat isolated heart and cardiac myofibrillar functionPathomechanisms in heart failure: the contractile connection.Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility.Historical perspective on heart function: the Frank-Starling Law.The Frank-Starling Law: a jigsaw of titin proportions.Myosin filament activation in the heart is tuned to the mechanical task.Restrictive Cardiomyopathy Troponin I R145W Mutation Does Not Perturb Myofilament Length-dependent Activation in Human Cardiac Sarcomeres.Cardiac troponin I phosphorylation and the force-length relationship.The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform.
P2860
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P2860
Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24.
description
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name
Length dependence of striated ...... tion of cTnI at serines 23/24.
@en
Length dependence of striated ...... tion of cTnI at serines 23/24.
@nl
type
label
Length dependence of striated ...... tion of cTnI at serines 23/24.
@en
Length dependence of striated ...... tion of cTnI at serines 23/24.
@nl
prefLabel
Length dependence of striated ...... tion of cTnI at serines 23/24.
@en
Length dependence of striated ...... tion of cTnI at serines 23/24.
@nl
P2860
P1476
Length dependence of striated ...... tion of cTnI at serines 23/24.
@en
P2093
Brandon J Biesiadecki
Laurin M Hanft
P2860
P304
P356
10.1113/JPHYSIOL.2013.258400
P407
P577
2013-07-08T00:00:00Z