ArticleBiophysical journal2005
Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Cellular and molecular contractile function in aged human skeletal muscle is altered by phosphate and acidosis and partially reversed with an ATP analog.American journal of physiology. Cell physiology · 2025Article
- Research reviews on myosin head interactions with F-actin.Applied microscopy · 2024Review
- Mechanisms of Frank-Starling law of the heart and stretch activation in striated muscles may have a common molecular origin.Journal of muscle research and cell motility · 2021Article
- Phosphate has dual roles in cross-bridge kinetics in rabbit psoas single myofibrils.The Journal of general physiology · 2021Article
- Nebulin increases thin filament stiffness and force per cross-bridge in slow-twitch soleus muscle fibers.The Journal of general physiology · 2018Article
- Article
- Molecular determinants of force production in human skeletal muscle fibers: effects of myosin isoform expression and cross-sectional area.American journal of physiology. Cell physiology · 2015Article
- A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Journal of muscle research and cell motility · 2013Article
- Age-related slowing of myosin actin cross-bridge kinetics is sex specific and predicts decrements in whole skeletal muscle performance in humans.Journal of applied physiology (Bethesda, Md. : 1985) · 2013Article
- ATP binding and cross-bridge detachment steps during full Ca²⁺ activation: comparison of myofibril and muscle fibre mechanics by sinusoidal analysis.The Journal of physiology · 2012Article
- Actomyosin kinetics of pure fast and slow rat myosin isoforms studied by in vitro motility assay approach.Experimental physiology · 2012Article
- Chronic heart failure decreases cross-bridge kinetics in single skeletal muscle fibres from humans.The Journal of physiology · 2010Article
- The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle.Biophysical journal · 2010Article
- Mechanistic role of movement and strain sensitivity in muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2009Article
- Unloaded speed of shortening in voltage-clamped intact skeletal muscle fibers from wt, mdx, and transgenic minidystrophin mice using a novel high-speed acquisition system.Biophysical journal · 2008Article
- Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis.Biophysical journal · 2007Article
- Force transients and minimum cross-bridge models in muscular contraction.Journal of muscle research and cell motility · 2007Review
- Mathematical simulation of muscle cross-bridge cycle and force-velocity relationship.Biophysical journal · 2006Article
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3 authors.
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Abstract
To understand the molecular mechanism underlying the diversity of mammalian skeletal muscle fibers, the elementary steps of the cross-bridge cycle were investigated in three fast-twitch fiber types from rabbit limb muscles. Skinned fibers were maximally Ca(2+)-activated at 20 degrees C and the effects of MgATP, phosphate (P, P(i)), and MgADP were studied on three exponential processes by sinusoidal analysis. The fiber types (IIA, IID, and IIB) were determined by analyzing the myosin heavy-chain isoforms after mechanical experiments using high-resolution SDS-PAGE. The results were consistent with the following cross-bridge scheme: where A is actin, M is myosin, D is MgADP, and S is MgATP. All states except for those in brackets are strongly bound states. All rate constants of elementary steps (k(2), 198-526 s(-1); k(-2), 51-328 s(-1); k(4), 13.6-143 s(-1); k(-4), 13.6-81 s(-1)) were progressively larger in the order of type IIA, type IID, and type IIB fibers. The rate constants of a transition from a weakly bound state to a strongly bound state (k(-2), k(4)) varied more among fiber types than their reversals (k(2), k(-4)). The equilibrium constants K(1) (MgATP affinity) and K(2) (=k(2)/k(-2), ATP isomerization) were progressively less in the order IIA, IID, and IIB. K(4) (=k(4)/k(-4), force generation) and K(5) (P(i) affinity) were larger in IIB than IIA and IID fibers. K(1) showed the largest variation indicating that the myosin head binds MgATP more tightly in the order IIA (8.7 mM(-1)), IID (4.9 mM(-1)), and IIB (0.84 mM(-1)). Similarly, the MgADP affinity (K(0)) was larger in type IID fibers than in type IIB fibers.
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