Activation dependence of stretch activation in mouse skinned myocardium: implications for ventricular function - Wikidata - awgldk - TriplyDB

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

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

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Acceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chain Myofilament length dependent activation Distorting the sarcomere Model representation of the nonlinear step response in cardiac muscle.Altered in vivo left ventricular torsion and principal strains in hypothyroid rats Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.Interaction between troponin and myosin enhances contractile activity of myosin in cardiac muscle.The effects of force inhibition by sodium vanadate on cross-bridge binding, force redevelopment, and Ca2+ activation in cardiac muscle.Cardiac myosin binding protein C insufficiency leads to early onset of mechanical dysfunction.The interaction of Ca2+ with sarcomeric proteins: role in function and dysfunction of the heart Functions of stretch activation in heart muscle Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-C Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent Activation In vivo cardiac myosin binding protein C gene transfer rescues myofilament contractile dysfunction in cardiac myosin binding protein C null mice Impaired contractile function due to decreased cardiac myosin binding protein C content in the sarcomere 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.Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion Dilated Cardiomyopathy Mutation (R134W) in Mouse Cardiac Troponin T Induces Greater Contractile Deficits against α-Myosin Heavy Chain than against β-Myosin Heavy Chain.Electromechanical coupling in the cardiac myocyte; stretch-arrhythmia feedback.The 3-state model of muscle regulation revisited: is a fourth state involved?Changes in dynamic embryonic heart wall motion in response to outflow tract banding measured using video densitometry.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 Contributions of stretch activation to length-dependent contraction in murine myocardium.Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin Cooperative regulation of myosin-S1 binding to actin filaments by a continuous flexible Tm-Tn chain.N-terminal phosphorylation of cardiac troponin-I reduces length-dependent calcium sensitivity of contraction in cardiac muscle.Transmural variation in myosin heavy chain isoform expression modulates the timing of myocardial force generation in porcine left ventricle.Stretch activation properties of Drosophila and Lethocerus indirect flight muscle suggest similar calcium dependent mechanisms.Omecamtiv Mecarbil Abolishes Length-Mediated Increase in Guinea Pig Cardiac Myofiber Ca2+ Sensitivity.Heart Failure-Related Hyperphosphorylation in the Cardiac Troponin I C Terminus Has Divergent Effects on Cardiac Function In Vivo.Hypertrophic cardiomyopathy mutation in cardiac troponin T (R95H) attenuates length-dependent activation in guinea pig cardiac muscle fibers.The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type.Dynamic left ventricular elastance: a model for integrating cardiac muscle contraction into ventricular pressure-volume relationships.Coupling Langevin Dynamics With Continuum Mechanics: Exposing the Role of Sarcomere Stretch Activation Mechanisms to Cardiac Function.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

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

http://www.wikidata.org/entity/Q36295575

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The Journal of General Physiology

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Daniel P Fitzsimons

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Julian E Stelzer

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Lars Larsson

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Richard L Moss

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P2860

The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation

Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament

Basal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force development

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

PKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosin

Regulation of contraction in striated muscle

SLControl: PC-based data acquisition and analysis for muscle mechanics.

Indirect coupling of phosphate release to de novo tension generation during muscle contraction.

Phase transition in force during ramp stretches of skeletal muscle.

Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction.

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