ArticleThe Journal of physiology2002
The size and the speed of the working stroke of muscle myosin and its dependence on the force.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 127 citations in OpenAlex.
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- Resolving the kinetics of an ensemble of muscle myosin motors via a temperature-dependent fitting procedure.Journal of the Royal Society, Interface · 2025Article
- Nanometer scale difference in myofilament lattice structure of muscle alters muscle function in a spatially explicit model.PLoS computational biology · 2025Article
- The Mechanism of Modulation of Cardiac Force by Temperature.International journal of molecular sciences · 2025Article
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Cooperativity of myosin II motors in the non-regulated and regulated thin filaments investigated with high-speed AFM.The Journal of general physiology · 2023Article
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Article
- Cross-bridge mechanics estimated from skeletal muscles' work-loop responses to impacts in legged locomotion.Scientific reports · 2021Article
- Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin.Biophysical journal · 2021Article
- Straightening Out the Elasticity of Myosin Cross-Bridges.Biophysical journal · 2020Review
- Exhaustion of Skeletal Muscle Fibers Within Seconds: Incorporating Phosphate Kinetics Into a Hill-Type Model.Frontiers in physiology · 2020Article
- The load dependence and the force-velocity relation in intact myosin filaments from skeletal and smooth muscles.American journal of physiology. Cell physiology · 2020Article
- The force and stiffness of myosin motors in the isometric twitch of a cardiac trabecula and the effect of the extracellular calcium concentration.The Journal of physiology · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit.The Journal of physiology · 2018Article
- Strain in shock-loaded skeletal muscle and the time scale of muscular wobbling mass dynamics.Scientific reports · 2017Article
- Robust mechanobiological behavior emerges in heterogeneous myosin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Auxotonic to isometric contraction transitioning in a beating heart causes myosin step-size to down shift.PloS one · 2017Article
- Effects of cross-bridge compliance on the force-velocity relationship and muscle power output.PloS one · 2017Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin II is the motor protein that produces force and shortening in muscle by ATP-driven cyclic interactions of its globular portion, the head, with the actin filament. During each interaction the myosin head undergoes a conformational change, the working stroke, which, depending on the mechanical conditions, can generate a force of several piconewtons or an axial displacement of the actin filament toward the centre of the sarcomere of several nanometres. However, the sizes of the elementary force and length steps and their dependence on the mechanical conditions are still under question. Due to the small fraction of the ATPase cycle time myosin II spends attached to actin, single molecule mechanics failed to produce definitive measurements of the individual events. In intact frog muscle fibres, however, myosin II's working stroke can be synchronised in the few milliseconds following a step reduction in either force or length superimposed on the isometric contraction. Here we show that with 150 micros force steps it is possible to separate the elastic response from the subsequent early rapid component of filament sliding due to the working stroke in the attached myosin heads. In this way we determine how the size and the speed of the working stroke depend on the clamped force. The relation between mechanical energy and force provides a molecular basis for muscle efficiency and an estimate of the isometric force exerted by a myosin head.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.