ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004
Coupling between phosphate release and force generation in muscle actomyosin.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
63 citing papers in PubMed, 113 citations in OpenAlex.
- Physical confinement modulates the rate-limiting transition in the release of phosphate from actin filaments.Science advances · 2026Article
- Physical Confinement Modulates the Rate-Limiting Transition in the Release of Phosphate from Actin Filaments.bioRxiv : the preprint server for biology · 2026Article
- A human skeletal muscle cross-bridge model to characterize the role of metabolite accumulation in muscle fatigue.Experimental physiology · 2025Article
- Stretch activation combats force loss from fatigue in fast-contracting mouse skeletal muscle fibers.The Journal of general physiology · 2025Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Considering the effect of Pi rebinding on myosin dynamics based on the distinct functions of cardiac and skeletal myosin.Frontiers in physiology · 2025Article
- Switch-2 determines MgFrontiers in physiology · 2024Article
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- Creatine Kinase Equilibration and ΔGInternational journal of molecular sciences · 2023Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Recent insights into the relative timing of myosin's powerstroke and release of phosphate.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin.Biophysical journal · 2021Article
- Phosphate has dual roles in cross-bridge kinetics in rabbit psoas single myofibrils.The Journal of general physiology · 2021Article
- The Location and Rate of the Phosphate Release Step in the Muscle Cross-Bridge Cycle.Biophysical journal · 2020Article
- Exhaustion of Skeletal Muscle Fibers Within Seconds: Incorporating Phosphate Kinetics Into a Hill-Type Model.Frontiers in physiology · 2020Article
- A myosin-based mechanism for stretch activation and its possible role revealed by varying phosphate concentration in fast and slow mouse skeletal muscle fibers.American journal of physiology. Cell physiology · 2019Article
- Exploring the Link between Serum Phosphate Levels and Low Muscle Strength, Dynapenia, and Sarcopenia.Scientific reports · 2018Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Energetic, kinetic and oxygen exchange experiments in the mid-1980s and early 1990s suggested that phosphate (Pi) release from actomyosin-adenosine diphosphate Pi (AM.ADP.Pi) in muscle fibres is linked to force generation and that Pi release is reversible. The transition leading to the force-generating state and subsequent Pi release were hypothesized to be separate, but closely linked steps. Pi shortens single force-generating actomyosin interactions in an isometric optical clamp only if the conditions enable them to last 20-40 ms, enough time for Pi to dissociate. Until 2003, the available crystal forms of myosin suggested a rigid coupling between movement of switch II and tilting of the lever arm to generate force, but they did not explain the reciprocal affinity myosin has for actin and nucleotides. Newer crystal forms and other structural data suggest that closing of the actin-binding cleft opens switch I (presumably decreasing nucleotide affinity). These data are all consistent with the order of events suggested before: myosin.ADP.Pi binds weakly, then strongly to actin, generating force. Then Pi dissociates, possibly further increasing force or sliding.
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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.