Model representation of the nonlinear step response in cardiac muscle. - Wikidata - awgldk - TriplyDB

Model representation of the nonlinear step response in cardiac muscle.

Model representation of the nonlinear step response in cardiac muscle.

http://www.wikidata.org/entity/Q34028229

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A mathematical model of muscle containing heterogeneous half-sarcomeres exhibits residual force enhancement Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.The functional effect of dilated cardiomyopathy mutation (R144W) in mouse cardiac troponin T is differently affected by α- and β-myosin heavy chain isoforms A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Alanine or aspartic acid substitutions at serine23/24 of cardiac troponin I decrease thin filament activation, with no effect on crossbridge detachment kinetics The N-terminal extension of cardiac troponin T stabilizes the blocked state of cardiac thin filament Effects of R92 mutations in mouse cardiac troponin T are influenced by changes in myosin heavy chain isoform.Rat cardiac troponin T mutation (F72L)-mediated impact on thin filament cooperativity is divergently modulated by α- and β-myosin heavy chain isoforms.Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-C Deletion of 1-43 amino acids in cardiac myosin essential light chain blunts length dependency of Ca(2+) sensitivity and cross-bridge detachment kinetics.Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent Activation Interplay Between the Effects of Dilated Cardiomyopathy Mutation (R206L) and the Protein Kinase C Phosphomimic (T204E) of Rat Cardiac Troponin T Are Differently Modulated by α- and β-Myosin Heavy Chain Isoforms.Divergent effects of α- and β-myosin heavy chain isoforms on the N terminus of rat cardiac troponin T.Dilated Cardiomyopathy Mutation (R134W) in Mouse Cardiac Troponin T Induces Greater Contractile Deficits against α-Myosin Heavy Chain than against β-Myosin Heavy Chain.Cardiac myosin binding protein-C Ser302 phosphorylation regulates cardiac β-adrenergic reserve L71F mutation in rat cardiac troponin T augments crossbridge recruitment and detachment dynamics against α-myosin heavy chain, but not against β-myosin heavy chain.Cardiomyopathy-related mutation (A30V) in mouse cardiac troponin T divergently alters the magnitude of stretch activation in α- and β-myosin heavy chain fibers.Interplay between the effects of a Protein Kinase C phosphomimic (T204E) and a dilated cardiomyopathy mutation (K211Δ or R206W) in rat cardiac troponin T blunts the magnitude of muscle length-mediated crossbridge recruitment against the β-myosin hea Length-dependent effects on cardiac contractile dynamics are different in cardiac muscle containing α- or β-myosin heavy chain.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.The contribution of cardiac myosin binding protein-c Ser282 phosphorylation to the rate of force generation and in vivo cardiac contractility.Omecamtiv Mecarbil Abolishes Length-Mediated Increase in Guinea Pig Cardiac Myofiber Ca2+ Sensitivity.Hypertrophic cardiomyopathy mutation in cardiac troponin T (R95H) attenuates length-dependent activation in guinea pig cardiac muscle fibers.Effects of pseudo-phosphorylated rat cardiac troponin T are differently modulated by α- and β-myosin heavy chain isoforms.Cardiomyopathy mutation (F88L) in troponin T abolishes length dependency of myofilament Ca sensitivity Impact of the Myosin Modulator Mavacamten on Force Generation and Cross-Bridge Behavior in a Murine Model of Hypercontractility

P2860

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P2860

Model representation of the nonlinear step response in cardiac muscle.

http://www.wikidata.org/entity/Q34028229

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Model representation of the nonlinear step response in cardiac muscle.

@ast

Model representation of the nonlinear step response in cardiac muscle.

@en

Model representation of the nonlinear step response in cardiac muscle.

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type

label

Model representation of the nonlinear step response in cardiac muscle.

@ast

Model representation of the nonlinear step response in cardiac muscle.

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Model representation of the nonlinear step response in cardiac muscle.

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prefLabel

Model representation of the nonlinear step response in cardiac muscle.

@ast

Model representation of the nonlinear step response in cardiac muscle.

@en

Model representation of the nonlinear step response in cardiac muscle.

@nl

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P1433

The Journal of General Physiology

P1476

Model representation of the nonlinear step response in cardiac muscle.

@en

P2093

Kenneth B Campbell

http://www.w3.org/2001/XMLSchema#string

Murali Chandra

http://www.w3.org/2001/XMLSchema#string

Ranganath Mamidi

http://www.w3.org/2001/XMLSchema#string

Steven J Ford

http://www.w3.org/2001/XMLSchema#string

Wenji Dong

http://www.w3.org/2001/XMLSchema#string

P2860

Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T

Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity

Interpreting cardiac muscle force-length dynamics using a novel functional model

Troponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle.

Proposed mechanism of force generation in striated muscle.

Activation dependence of stretch activation in mouse skinned myocardium: implications for ventricular function

Force transients and minimum cross-bridge models in muscular contraction.

Tension responses to sudden length change in stimulated frog muscle fibres near slack length.

Temperature and amplitude dependence of tension transients in glycerinated skeletal and insect fibrillar muscle.

Transmural variation in myosin heavy chain isoform expression modulates the timing of myocardial force generation in porcine left ventricle.

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159-177

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scholarly article

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10.1085/JGP.201010467

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2

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136

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2010-08-01T00:00:00Z

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45366265

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20660660

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2912065

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