ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2000
Mechanics and models of the myosin motor.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 103 citations in OpenAlex.
- Validation of the energetics of a Huxley muscle-tendon complex model using experimental data obtained from mouse soleus muscle.The Journal of experimental biology · 2025Article
- Endurance exercise-induced histone methylation modification involved in skeletal muscle fiber type transition and mitochondrial biogenesis.Scientific reports · 2024Article
- Into the dynamics of rotaxanes at atomistic resolution.Chemical science · 2023Article
- NIMA-related kinase 9 regulates the phosphorylation of the essential myosin light chain in the heart.Nature communications · 2022Article
- FRET and optical trapping reveal mechanisms of actin activation of the power stroke and phosphate release in myosin V.The Journal of biological chemistry · 2020Article
- Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.International journal of molecular sciences · 2018Review
- Multiscale and Multiaxial Mechanics of Vascular Smooth Muscle.Biophysical journal · 2017Article
- Local heating of molecular motors using single carbon nanotubes.Biophysical reviews · 2016Review
- The endothermic ATP hydrolysis and crossbridge attachment steps drive the increase of force with temperature in isometric and shortening muscle.The Journal of physiology · 2015Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- A cross-bridge cycle with two tension-generating steps simulates skeletal muscle mechanics.Biophysical journal · 2013Article
- Theoretical Hill-type muscle and stability: numerical model and application.Computational and mathematical methods in medicine · 2013Article
- From cycling between coupled reactions to the cross-bridge cycle: mechanical power output as an integral part of energy metabolism.Metabolites · 2012Article
- The interrelation between mechanical characteristics of contracting muscle, cross-bridge internal structure, and the mechanism of chemomechanical energy transduction.European biophysics journal : EBJ · 2012Article
- Is titin a 'winding filament'? A new twist on muscle contraction.Proceedings. Biological sciences · 2012Article
- Theory of muscle contraction mechanism with cooperative interaction among crossbridges.Biophysics (Nagoya-shi, Japan) · 2012Review
- Axial and radial forces of cross-bridges depend on lattice spacing.PLoS computational biology · 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
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- 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
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In striated muscles, shortening comes about by the sliding movement of thick filaments, composed mostly of myosin, relative to thin filaments, composed mostly of actin. This is brought about by cyclic action of 'cross-bridges' composed of the heads of myosin molecules projecting from a thick filament, which attach to an adjacent thin filament, exert force for a limited time and detach, and then repeat this cycle further along the filament. The requisite energy is provided by the hydrolysis of a molecule of adenosine triphosphate to the diphosphate and inorganic phosphate, the steps of this reaction being coupled to mechanical events within the cross-bridge. The nature of these events is discussed. There is good evidence that one of them is a change in the angle of tilt of a 'lever arm' relative to the 'catalytic domain' of the myosin head which binds to the actin filament. It is suggested here that this event is superposed on a slower, temperature-sensitive change in the orientation of the catalytic domain on the actin filament. Many uncertainties remain.
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Registered trials
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.