Myosin head orientation: a structural determinant for the Frank-Starling relationship - Wikidata - awgldk - TriplyDB

Myosin head orientation: a structural determinant for the Frank-Starling relationship

Myosin head orientation: a structural determinant for the Frank-Starling relationship

http://www.wikidata.org/entity/Q35056950

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The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C Perturbed length-dependent activation in human hypertrophic cardiomyopathy with missense sarcomeric gene mutations In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation.Deletion of the titin N2B region accelerates myofibrillar force development but does not alter relaxation kinetics Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics Familial hypertrophic cardiomyopathy related cardiac troponin C L29Q mutation alters length-dependent activation and functional effects of phosphomimetic troponin I*The interaction of Ca2+ with sarcomeric proteins: role in function and dysfunction of the heart Magnitude of length-dependent changes in contractile properties varies with titin isoform in rat ventricles.Cardiac myosin binding protein-C: redefining its structure and function.Myofilament length-dependent activation develops within 5 ms in guinea-pig myocardium Deletion of 1-43 amino acids in cardiac myosin essential light chain blunts length dependency of Ca(2+) sensitivity and cross-bridge detachment kinetics.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.Titin stiffness modifies the force-generating region of muscle sarcomeres.Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filaments Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips.Myosin heads are displaced from actin filaments in the in situ beating rat heart in early diabetes Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Historical perspective on heart function: the Frank-Starling Law.The Frank-Starling Law: a jigsaw of titin proportions.Distinct contributions of the thin and thick filaments to length-dependent activation in heart muscle.Cardiac muscle mechanics: Sarcomere length matters.Impact of titin isoform on length dependent activation and cross-bridge cycling kinetics in rat skeletal muscle.Cross-talk, cross-bridges, and calcium activation of cardiac contraction.Update on innovative initiatives for the American Journal of Physiology-Heart and Circulatory Physiology.N-terminal phosphorylation of cardiac troponin-I reduces length-dependent calcium sensitivity of contraction in cardiac muscle.Altered myofilament structure and function in dogs with Duchenne muscular dystrophy cardiomyopathy.Functional significance of C-terminal mobile domain of cardiac troponin I.Left ventricular strain modifications after maximal exercise in athletes: a speckle tracking study.Role of the C-terminus mobile domain of cardiac troponin I in the regulation of thin filament activation in skinned papillary muscle strips.

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P2860

Myosin head orientation: a structural determinant for the Frank-Starling relationship

http://www.wikidata.org/entity/Q35056950

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Myosin head orientation: a structural determinant for the Frank-Starling relationship

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Myosin head orientation: a structural determinant for the Frank-Starling relationship

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Myosin head orientation: a structural determinant for the Frank-Starling relationship

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Myosin head orientation: a structural determinant for the Frank-Starling relationship

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Myosin head orientation: a structural determinant for the Frank-Starling relationship

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Myosin head orientation: a structural determinant for the Frank-Starling relationship

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AJPHEART.01221.2010

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American Journal of Physiology - Heart and Circulatory Physiology

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Myosin head orientation: a structural determinant for the Frank-Starling relationship

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P2093

David Gore

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Edward Allen

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Gerrie P Farman

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Kelly Schoenfelt

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Pieter P de Tombe

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Thomas C Irving

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P2860

The effect of myosin light chain 2 dephosphorylation on Ca2+ -sensitivity of force is enhanced in failing human hearts

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

Three-dimensional structure of vertebrate cardiac muscle myosin filaments.

X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle

Sarcomere-length dependence of lattice volume and radial mass transfer of myosin cross-bridges in rat papillary muscle.

Myofilament length dependent activation

Increased phosphorylation of tropomyosin, troponin I, and myosin light chain-2 after stretch in rabbit ventricular myocardium under physiological conditions.

Phosphorylation-dependent power output of transgenic flies: an integrated study.

Calcium sensitivity and the Frank-Starling mechanism of the heart are increased in titin N2B region-deficient mice

The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. II. Elementary steps affected by the spacing change.

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10.1152/AJPHEART.01221.2010

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3119094

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