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Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibresPhosphorylation of cMyBP-C affects contractile mechanisms in a site-specific mannerKinetic and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers.Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers.Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers.The effect of partial extraction of troponin C on the elementary steps of the cross-bridge cycle in rabbit psoas muscle fibersThe 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 widthThe 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.Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles.DCM-related tropomyosin mutants E40K/E54K over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridges.Differences in the transient response of fast and slow skeletal muscle fibers. Correlations between complex modulus and myosin light chains.Cardiac myosin binding protein C phosphorylation affects cross-bridge cycle's elementary steps in a site-specific manner.Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutationsCrossbridge kinetics in chemically skinned rabbit psoas fibres when the actin-myosin lattice spacing is altered by dextran T-500.Structural and functional aspects of the myosin essential light chain in cardiac muscle contraction.High ionic strength depresses muscle contractility by decreasing both force per cross-bridge and the number of strongly attached cross-bridges.Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation.Analysis of the molecular pathogenesis of cardiomyopathy-causing cTnT mutants I79N, ΔE96, and ΔK210.Characterizations of myosin essential light chain's N-terminal truncation mutant Δ43 in transgenic mouse papillary muscles by using tension transients in response to sinusoidal length alterations.Diversity and similarity of motor function and cross-bridge kinetics in papillary muscles of transgenic mice carrying myosin regulatory light chain mutations D166V and R58QA re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Using baculovirus/insect cell expressed recombinant actin to study the molecular pathogenesis of HCM caused by actin mutation A331PThe role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Covalent cross-linking of single fibers from rabbit psoas increases oscillatory power.Comments on "Critical dependence of calcium-activated force on width in highly compressed skinned fibers of the frog".Effects of tropomyosin internal deletion Delta23Tm on isometric tension and the cross-bridge kinetics in bovine myocardium.Cardiac contractility, motor function, and cross-bridge kinetics in N47K-RLC mutant mice.Estimation of actomyosin active force maintained by tropomyosin and troponin complex under vertical forces in the in vitro motility assay system.Comparison of elementary steps of the cross-bridge cycle in rat papillary muscle fibers expressing α- and β-myosin heavy chain with sinusoidal analysis.Myosin Rod Hypophosphorylation and CB Kinetics in Papillary Muscles from a TnC-A8V KI Mouse Model.The immediate effect of HCM causing actin mutants E99K and A230V on actin-Tm-myosin interaction in thin-filament reconstituted myocardium.Correlation between cross-bridge kinetics obtained from Trp fluorescence of myofibril suspensions and mechanical studies of single muscle fibers in rabbit psoas.Stiffness and contractile properties of avian normal and dystrophic muscle bundles as measured by sinusoidal length perturbations.Nebulin increases thin filament stiffness and force per cross-bridge in slow-twitch soleus muscle fibersComparison of crossbridge dynamics between intact and skinned myocardium from ferret right ventriclesEffect of ionic strength on crossbridge kinetics as studied by sinusoidal analysis, ATP hydrolysis rate and X-ray diffraction techniques in chemically skinned rabbit psoas fibresThe role of orthophosphate in crossbridge kinetics in chemically skinned rabbit psoas fibres as detected with sinusoidal and step length alterationsThe role of collagen crosslinking in the increased stiffness of avian dystrophic muscleThe effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibersCrossbridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret
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Q28349425-D17B644E-937E-4E07-B4C1-52667B8B042BQ33634074-23217091-2895-4738-B92A-C2072F59AECBQ34018751-F0EFE79B-2895-4173-AEC5-9DC39D607C36Q34019510-1EE9E8B0-0550-4535-B88F-64824F44DE49Q34040572-10BC8570-60B5-4E0B-A675-BB7A324C96CCQ34041108-E9582B45-2386-4994-8D2D-8C8D0DFD2F99Q34092008-7922E37C-5255-4197-A2F3-646F16CAF370Q34092014-23A7B8A7-4BD0-4AEE-94A6-480741B3ED15Q34351738-0A833AB2-C379-45B4-8258-043CBA974853Q34450885-AE4C6BEE-F29F-4560-A7F3-337951B51BD5Q34535071-E60548A0-1CB9-44B3-BE9C-EDE724C421D9Q34566207-2A72390A-3BA0-482A-901C-D732D04F7F2CQ34568089-61699025-18AF-4C2D-846D-AD6AC4AF7BE5Q35024974-0D12CBBA-E4B1-4D0F-899C-8ECB9B4849E2Q35609653-12639BE7-EFC9-42F7-B17C-07D112510A4CQ35756180-EE256C52-4C83-4B95-9ED4-C1D75AB9318EQ36565792-F11E8CC2-F04F-4ACD-9B38-B755F0D0F9F8Q36824519-3B6F69D7-3ED4-4C21-B396-2CD700F0B1A5Q36851273-A255B70C-4B06-407D-BD90-68B7D29CA6E5Q37257335-83C0D088-6E3C-4BB1-B7E4-BD468DBAA285Q37539919-7437311A-409A-40E3-ACA6-916257852994Q38998926-CF703496-7CEE-4D91-9CE9-1EA754B6D55DQ39603618-93C4B87F-BF12-4C19-A2E9-5076DDF5AEB2Q39626804-37EAAD95-A786-4AE1-B9AE-B6157155608CQ43158363-CED0B633-60A2-4CA0-9D3C-DEE919229BACQ44590900-A0AD8230-6D9B-49DD-A043-424FA366D996Q47898693-567987B9-FED1-445A-87E8-704B9E93E1DEQ50053582-53B43FA8-718B-4C66-AB67-ED3EC97CDE61Q51016783-A77BC631-1F62-404F-A0F9-BBD3394DD5C5Q51033685-A21C2ADE-2923-4C47-8F23-D3DD4FFCC63BQ52783545-69B191CE-090E-4757-B023-5FA4AE7C425AQ53212341-4F04C4A2-86BC-441E-97B9-CB34F0242513Q54447200-5023053D-C734-49C3-9028-B71170ED89BBQ57290201-E588511D-D6A7-4F42-831C-0F3EB7907E21Q67762072-5372C014-AA52-4932-ACC7-D7635C369B9BQ68641724-73F462C7-D211-4818-8511-78D8E0F259ABQ68811185-0D4C050A-2A70-482C-A31A-E38B914E6CD2Q69617544-168F28B6-6431-40B8-A4F3-1F7F661B49B6Q69763322-25371734-BD8C-4256-BCB0-66198FC713EAQ70753477-8C038B41-5914-4977-B802-ED98CF04F22F
P50
description
researcher ORCID ID = 0000-0002-3219-3527
@en
wetenschapper
@nl
name
Masataka Kawai
@ast
Masataka Kawai
@en
Masataka Kawai
@es
Masataka Kawai
@nl
type
label
Masataka Kawai
@ast
Masataka Kawai
@en
Masataka Kawai
@es
Masataka Kawai
@nl
prefLabel
Masataka Kawai
@ast
Masataka Kawai
@en
Masataka Kawai
@es
Masataka Kawai
@nl
P106
P1153
7403311803
P31
P496
0000-0002-3219-3527