ArticleThe Journal of physiology2005
Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- The working stroke of the myosin II motor in muscle is not tightly coupled to release of orthophosphate from its active site.The Journal of physiology · 2013Article
- Orthovanadate and orthophosphate inhibit muscle force via two different pathways of the myosin ATPase cycle.Biophysical journal · 2011Article
- A kinetic model that explains the effect of inorganic phosphate on the mechanics and energetics of isometric contraction of fast skeletal muscle.Proceedings. Biological sciences · 2010Article
- Time course and strain dependence of ADP release during contraction of permeabilized skeletal muscle fibers.Biophysical journal · 2009Article
- Effects of solution tonicity on crossbridge properties and myosin lever arm disposition in intact frog muscle fibres.The Journal of physiology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We measured the effects of ionic strength (IS), 200 (standard) and 400 mmol l(-1) (high), on force and ATP hydrolysis during isometric contractions of permeabilized white fibres from dogfish myotomal muscle at their physiological temperature, 12 degrees C. One goal was to test the validity of our kinetic scheme that accounts for energy release, work production and ATP hydrolysis. Fibres were activated by flash photolysis of the P(3)-1-(2 nitrophenyl) ethyl ester of ATP (NPE-caged ATP), and time-resolved phosphate (P(i)) release was detected with the fluorescent protein MDCC-PBP, N-(2[1-maleimidyl]ethyl)-7-diethylamino-coumarin-3-carboxamide phosphate binding protein. High IS slowed the transition from rest to contraction, but as the fibres approached the isometric force plateau they showed little IS sensitivity. By 0.5 s of contraction, the force and the rate of P(i) release at standard and high IS values were not significantly different. A five-step reaction mechanism was used to account for the observed time courses of force and P(i) release in all conditions explored here. Only the rate constants for reactions of ATP, ADP and P(i) with the contractile proteins varied with IS, thus suggesting that the actin-myosin interactions are largely non-ionic. Our reaction scheme also fits previous results for intact fibres.
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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.