ReviewJournal of muscle research and cell motility2025
The elementary step that generates force and sinusoidal analysis in striated muscle fibers.
Review in Journal of muscle research and cell motility, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- 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
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.Frontiers in physiology · 2025Article
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The elementary step that generates force by cross-bridges (CBs) in striated muscles is reviewed. A literature search focused on models with validating data to verify a CB scheme; models without substantiating data were briefly mentioned or not included. Experimental data include those carried out under the isometric condition in muscle fibers and single myofibrils, along with results from single molecule and stopped-flow studies. These results suggest that force is generated before phosphate (Pi) is released, and the same force is maintained after Pi is released. These studies assumed that Pi is released from myosin. Some results from isotonic experiments are also reviewed, but the data lack the effect of Pi (or a weak effect). Studies with X-ray crystallography and cryo-electron microscopy suggested that force is generated after Pi release from the active site, and Pi is trapped at the secondary site before it is released to the solution. Thus, the difference in the definition of the "Pi release step" must have caused a controversy. It can be concluded that the results from physiological/single molecule studies and cryo-EM/crystal studies complement each other quite well. With isometric experiments, several perturbations are used to generate force transients: length change, chemical change, pressure release, and temperature increase. A small length change includes sinusoidal waveforms, and a large length change includes 10-20% release/restretch. Chemical perturbation includes [Pi] changes. With temperature studies it was shown that the force generation step is endothermic, indicating heat is absorbed. This is qualitatively explained by a hydrophobic interaction between actin and myosin, and by a cleft closure of myosin.
Indexed as
Identifiers
What OpenQuestion holds
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.