Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle.
about
Airway and Extracellular Matrix Mechanics in COPDCardiac myofilament regulation by protein phosphatase type 1alpha and CapZEffect of Ca2+ on weak cross-bridge interaction with actin in the presence of adenosine 5'-[gamma-thio]triphosphate).Rotational dynamics of actin-bound intermediates of the myosin adenosine triphosphatase cycle in myofibrils.Mutation of the myosin converter domain alters cross-bridge elasticity.Cooperativity in F-actin: chemical modifications of actin monomers affect the functional interactions of myosin with unmodified monomers in the same actin filament.Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels.Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin adenosine triphosphatase cycle.Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap.Cross-linker dynamics determine the mechanical properties of actin gels.Kinetic mechanism of myofibril ATPase.Prolonged space flight-induced alterations in the structure and function of human skeletal muscle fibres.Distinct molecular processes associated with isometric force generation and rapid tension recovery after quick release.Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force genThe effect of thin filament activation on the attachment of weak binding cross-bridges: A two-dimensional x-ray diffraction study on single muscle fibers.Structural features of cross-bridges in isometrically contracting skeletal muscle.Mechanokinetics of rapid tension recovery in muscle: the Myosin working stroke is followed by a slower release of phosphate.The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Dynamics of cross-bridge cycling, ATP hydrolysis, force generation, and deformation in cardiac muscleDetermination of the myosin step size from mechanical and kinetic dataOn the regeneration of the actin-myosin power stroke in contracting muscle.High ionic strength and low pH detain activated skinned rabbit skeletal muscle crossbridges in a low force state.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Myosin V is a biological Brownian machine.Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding.Instabilities in the transient response of muscle.A new perspective on muscle contraction.Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance.Cargo-binding makes a wild-type single-headed myosin-VI move processively.Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers.Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.Direct inhibition of the actomyosin motility by local anesthetics in vitro.Synergistic role of ADP and Ca(2+) in diastolic myocardial stiffness.Force enhancement without changes in cross-bridge turnover kinetics: the effect of EMD 57033.Effect of an ADP analog on isometric force and ATPase activity of active muscle fibers.Force Responses and Sarcomere Dynamics of Cardiac Myofibrils Induced by Rapid Changes in [Pi].Mechanical and kinetic properties of β-cardiac/slow skeletal muscle myosin.Differences in Contractile Function of Myofibrils within Human Embryonic Stem Cell-Derived Cardiomyocytes vs. Adult Ventricular Myofibrils Are Related to Distinct Sarcomeric Protein Isoforms.Radial stiffness characteristics of the overlap regions of sarcomeres in isolated skeletal myofibrils in pre-force generating state.Cross-bridges in slow skeletal muscle: not only slow but also soft.
P2860
Q26773109-F7C8005A-2A7A-4843-B8EC-9D8236A7ED9FQ28273888-6322602C-12EC-48C7-8C6C-E482301D52E7Q33973089-8050981B-A0A9-41B7-B3F4-3DB3F5647645Q34018203-0D006977-56A3-448D-BA35-352044B6887BQ34019053-6DF89FDC-DB7C-49CC-8C13-309E67FA2E93Q34019306-17F7B161-1987-414F-BAC4-367CB7B88381Q34019344-06AD0B7B-AEF1-4610-80AD-0206E4808098Q34092104-B1EF9769-B453-41CE-8876-87E6C1F3F00FQ34115011-59B9693C-A706-46F9-B2A5-570B9A839FCEQ34115021-C5BF8E98-398B-45AC-8DFC-708CD56A847AQ34115321-92C3A1B8-447E-4846-B671-2D78BB46F16FQ34128050-E93AC67E-5F6C-43EB-AD00-D82438FDB9C7Q34128880-86FDF2E5-5119-414A-B9AA-9E7CB657E81AQ34129658-50B00190-9F28-4691-A0E8-01394977EFB4Q34169992-6825D733-3516-446F-B1A0-DD989C458FACQ34177857-250D0EEC-AA48-4044-A7E1-05B5CC56B823Q34186301-51CA47AF-64A7-4AA3-A12B-49017F9047EDQ34187343-62FF1A6D-EE18-4E07-AE8F-BABD17B08D15Q35940982-E642BDBC-8D5F-4C81-ACB4-E84F53BD6F59Q36176059-CA62EE40-372C-4C55-8640-AE1A7DEBD6E6Q36340072-B1E48517-F311-47C6-B9F7-B5B1F78A3C86Q36411385-307B304E-1728-4E31-98F9-799C5D1F2B2EQ36483549-6FD555B7-A48C-4472-8439-B7C69C1620E2Q38919352-E056F057-F4A8-4C19-AB99-76A4B8DDA889Q40160176-B5D02CF4-2EAC-4000-8065-A1FD7284EAF4Q40246912-744C0E75-C77D-4117-A207-270D14CFEC80Q40918583-D27985AA-FCB0-4971-AEB0-DB158B9EDBBBQ41929173-EA601931-25C4-4783-810D-427C1052D0B5Q42128939-26D8B22B-D2B3-47C9-9E65-AC9D7311F5CFQ42180929-94FC9B9A-DC27-4480-A60F-6E69BE62DBF4Q42183431-8C26F16F-B376-4D5E-83E1-069AF1B66FB7Q42184420-095C0F00-93E5-4CF6-88BD-7996F87FA6DCQ42478668-6DC80E0F-B80B-4192-BD9D-B1C128A65A50Q42933494-38F79FBA-5696-40E6-A557-8FA1A305F3AFQ44232459-68022FB3-8376-48E2-BC71-00CC5CAF0BA9Q46334789-38E0C6D9-2520-46E4-9137-C78C05102EF2Q47322365-BC541518-4DA9-456B-9E18-C344364D5967Q49185907-81E6F6DD-BACE-49A3-8F9A-F284FF8B4981Q49507277-CB68E34A-4899-43E6-B1C9-9715E9113378Q50088372-7D748815-D2D6-4450-84C4-B6CD87047D47
P2860
Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@en
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@nl
type
label
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@en
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@nl
prefLabel
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@en
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@nl
P2860
P356
P1476
Rapid dissociation and reassoc ...... cross-bridge action in muscle.
@en
P2093
P2860
P304
10490-10494
P356
10.1073/PNAS.88.23.10490
P407
P577
1991-12-01T00:00:00Z