Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing. - Wikidata - wikimedia - TriplyDB

Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.

Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.

http://www.wikidata.org/entity/Q44300159

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Integration of troponin I phosphorylation with cardiac regulatory networks Cardiac thin filament regulation and the Frank-Starling mechanism Phosphorylation of protein kinase C sites Ser42/44 decreases Ca(2+)-sensitivity and blunts enhanced length-dependent activation in response to protein kinase A in human cardiomyocytes Cardiac thin filament regulation Perturbed length-dependent activation in human hypertrophic cardiomyopathy with missense sarcomeric gene mutations Length-dependent activation is modulated by cardiac troponin I bisphosphorylation at Ser23 and Ser24 but not by Thr143 phosphorylation Troponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle.Cardiac myosin-binding protein-C phosphorylation and cardiac function A novel phosphorylation site, Serine 199, in the C-terminus of cardiac troponin I regulates calcium sensitivity and susceptibility to calpain-induced proteolysis Sites of intra- and intermolecular cross-linking of the N-terminal extension of troponin I in human cardiac whole troponin complex.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Desensitization of myofilaments to Ca2+ as a therapeutic target for hypertrophic cardiomyopathy with mutations in thin filament proteins.Myofilament length dependent activation Genotype-specific pathogenic effects in human dilated cardiomyopathy.Deletion of the titin N2B region accelerates myofibrillar force development but does not alter relaxation kinetics Troponin I phosphorylation in human myocardium in health and disease.Neonatal gene transfer of Serca2a delays onset of hypertrophic remodeling and improves function in familial hypertrophic cardiomyopathy.Protein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosin-binding protein C Functional effects of a tropomyosin mutation linked to FHC contribute to maladaptation during acidosis Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.A mathematical model of the mouse ventricular myocyte contraction.Familial hypertrophic cardiomyopathy related cardiac troponin C L29Q mutation alters length-dependent activation and functional effects of phosphomimetic troponin I*The regulation of troponins I, C and ANP by GATA4 and Nkx2-5 in heart of hibernating thirteen-lined ground squirrels, Ictidomys tridecemlineatus.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.AMP-activated protein kinase phosphorylates cardiac troponin I at Ser-150 to increase myofilament calcium sensitivity and blunt PKA-dependent function.Length and PKA Dependence of Force Generation and Loaded Shortening in Porcine Cardiac Myocytes Mechanisms of the Frank-Starling law of the heart: the beat goes on.Enhanced Ca2+ binding of cardiac troponin reduces sarcomere length dependence of contractile activation independently of strong crossbridges.Myosin binding protein-C phosphorylation is the principal mediator of protein kinase A effects on thick filament structure in myocardium.ADP-stimulated contraction: A predictor of thin-filament activation in cardiac disease.Cardiac Myosin-binding Protein C and Troponin-I Phosphorylation Independently Modulate Myofilament Length-dependent Activation.Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner.Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle Cardiac Myosin Binding Protein-C Phosphorylation Modulates 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.Calcium sensitivity and myofilament lattice structure in titin N2B KO mice.Cardiac function and modulation of sarcomeric function by length.The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation.Sarcomere length dependence of power output is increased after PKA treatment in rat cardiac myocytes

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Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.

http://www.wikidata.org/entity/Q44300159

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

Troponin I in the murine myoca ...... ion and interfilament spacing.

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Troponin I in the murine myoca ...... ion and interfilament spacing.

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type

label

Troponin I in the murine myoca ...... ion and interfilament spacing.

@en

Troponin I in the murine myoca ...... ion and interfilament spacing.

@nl

prefLabel

Troponin I in the murine myoca ...... ion and interfilament spacing.

@en

Troponin I in the murine myoca ...... ion and interfilament spacing.

@nl

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JPHYSIOL.2002.038117

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The Journal of Physiology

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Troponin I in the murine myoca ...... ion and interfilament spacing.

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Anne F Martin

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Beata M Wolska

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Eias E Jweied

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John P Konhilas

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Pieter P de Tombe

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R John Solaro

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Thomas C Irving

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P2860

Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band

Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2

The mechanism of muscular contraction

Expression of slow skeletal troponin I in adult transgenic mouse heart muscle reduces the force decline observed during acidic conditions

Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation

In vivo modeling of myosin binding protein C familial hypertrophic cardiomyopathy

Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle

The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. I. Proportionality between the lattice spacing and the fiber width

Proposed mechanism of force generation in striated muscle.

Equatorial x-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing.

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Pt 3

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547

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2003-01-24T00:00:00Z

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10921071

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12562915

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