Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit
about
Perturbed length-dependent activation in human hypertrophic cardiomyopathy with missense sarcomeric gene mutationsDirect measurement of cortical force generation and polarization in a living parasiteClinically Divergent Mutation Effects on the Structure and Function of the Human Cardiac Tropomyosin Overlap.Loop 2 of myosin is a force-dependent inhibitor of the rigor bondForce spectroscopy reveals multiple "closed states" of the muscle thin filament.Direct regulation of striated muscle myosins by nitric oxide and endogenous nitrosothiolsIncreased phosphorylation of tropomyosin, troponin I, and myosin light chain-2 after stretch in rabbit ventricular myocardium under physiological conditions.Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Recent insights into muscle fatigue at the cross-bridge level.The role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres.Isolation and characterisation of tropomyosin from shrimp (Penaeus vannamei Boone) and its association property at high ionic strength.A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.Modifications of myofilament protein phosphorylation and function in response to cardiac arrest induced in a swine modelMuscle weakness in TPM3-myopathy is due to reduced Ca2+-sensitivity and impaired acto-myosin cross-bridge cycling in slow fibres.Post-translational modifications of myofilament proteins involved in length-dependent prolongation of relaxation in rabbit right ventricular myocardiumNew insights into the regulation of the actin cytoskeleton by tropomyosin.A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Phosphorylation of Ser283 enhances the stiffness of the tropomyosin head-to-tail overlap domain.Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation.Expression of tropomyosin-κ induces dilated cardiomyopathy and depresses cardiac myofilament tension by mechanisms involving cross-bridge dependent activation and altered tropomyosin phosphorylation.HCM and DCM cardiomyopathy-linked α-tropomyosin mutations influence off-state stability and crossbridge interaction on thin filaments.Phosphorylation of myofibrillar proteins in post-mortem ovine muscle with different tenderness.
P2860
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P2860
Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@ast
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@en
type
label
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@ast
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@en
prefLabel
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@ast
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@en
P2860
P356
P1433
P1476
Phosphorylation of tropomyosin ...... eyond a single regulatory unit
@en
P2093
Ellisha N Marongelli
Vijay S Rao
P2860
P356
10.1002/CM.20321
P577
2009-01-01T00:00:00Z