ArticleProceedings. Biological sciences2010
A kinetic model that explains the effect of inorganic phosphate on the mechanics and energetics of isometric contraction of fast skeletal muscle.
Article in Proceedings. Biological sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Cross-bridge model-based quantification of muscle metabolite alterations leading to fatigue during all-out knee extension exercise.Frontiers in physiology · 2026Article
- A human skeletal muscle cross-bridge model to characterize the role of metabolite accumulation in muscle fatigue.Experimental physiology · 2025Article
- Theoretical treatment of tension transients in muscle following sudden changes in orthophosphate concentration: implications for energy transduction.Journal of muscle research and cell motility · 2025Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- 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
- Considering the effect of Pi rebinding on myosin dynamics based on the distinct functions of cardiac and skeletal myosin.Frontiers in physiology · 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
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.Frontiers in physiology · 2025Article
- Stochastic force generation in an isometric binary mechanical system.The Journal of general physiology · 2024Article
- A novel kinetic model to demonstrate the independent effects of ATP and ADP/Pi concentrations on sarcomere function.PLoS computational biology · 2024Article
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Maximal muscular power: lessons from sprint cycling.Sports medicine - open · 2021Review
- The Location and Rate of the Phosphate Release Step in the Muscle Cross-Bridge Cycle.Biophysical journal · 2020Article
- Orthophosphate increases the efficiency of slow muscle-myosin isoform in the presence of omecamtiv mecarbil.Nature communications · 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
- Bioenergetic basis of skeletal muscle fatigue.Current opinion in physiology · 2019Article
- Effects of elevated HThe Journal of physiology · 2018Article
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3 authors.
Funding
Abstract
A conventional five-step chemo-mechanical cycle of the myosin-actin ATPase reaction, which implies myosin detachment from actin upon release of hydrolysis products (ADP and phosphate, Pi) and binding of a new ATP molecule, is able to fit the [Pi] dependence of the force and number of myosin motors during isometric contraction of skeletal muscle. However, this scheme is not able to explain why the isometric ATPase rate of fast skeletal muscle is decreased by an increase in [Pi] much less than the number of motors. The question can be solved assuming the presence of a branch in the cycle: in isometric contraction, when the force generation process by the myosin motor is biased at the start of the working stroke, the motor can detach at an early stage of the ATPase cycle, with Pi still bound to its catalytic site, and then rapidly release the hydrolysis products and bind another ATP. In this way, the model predicts that in fast skeletal muscle the energetic cost of isometric contraction increases with [Pi]. The large dissociation constant of the product release in the branched pathway allows the isometric myosin-actin reaction to fit the equilibrium constant of the ATPase.
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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.