ArticleBiophysical journal2000
Influence of ionic strength on the actomyosin reaction steps in contracting skeletal muscle fibers.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 26 citations in OpenAlex.
- The tymbal muscle of cicada has flight muscle-type sarcomeric architecture and protein expression.Zoological letters · 2017Article
- High ionic strength depresses muscle contractility by decreasing both force per cross-bridge and the number of strongly attached cross-bridges.Journal of muscle research and cell motility · 2015Article
- X-ray diffraction pattern from the flight muscle of Toxorhynchites towadensis reveals the specific phylogenic position of mosquito among Diptera.Zoological letters · 2015Article
- X-ray diffraction from flight muscle with a headless myosin mutation: implications for interpreting reflection patterns.Frontiers in physiology · 2014Article
- Peptide mapping of polymorphic myosin heavy chain isoforms in different muscle types of some freshwater teleosts.Fish physiology and biochemistry · 2013Article
- Characterizations of myosin essential light chain's N-terminal truncation mutant Δ43 in transgenic mouse papillary muscles by using tension transients in response to sinusoidal length alterations.Journal of muscle research and cell motility · 2013Article
- Cadherin-based intercellular adhesions organize epithelial cell-matrix traction forces.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- SHP-2 acts via ROCK to regulate the cardiac actin cytoskeleton.Development (Cambridge, England) · 2012Article
- Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction.Biophysical journal · 2009Article
- Flight muscle myofibrillogenesis in the pupal stage of Drosophila as examined by X-ray microdiffraction and conventional diffraction.Proceedings. Biological sciences · 2007Article
- Diversity of structural behavior in vertebrate conventional myosins complexed with actin.Journal of molecular biology · 2007Article
- Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas.Biophysical journal · 2007Article
- Effects of solution tonicity on crossbridge properties and myosin lever arm disposition in intact frog muscle fibres.The Journal of physiology · 2007Article
- Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres.The Journal of physiology · 2005Article
- The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Biophysical journal · 2004Article
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscle contraction occurs as the result of actin-myosin interaction, which is mediated by the intermolecular forces exerted at the actin-myosin interface. To obtain information about the nature of these intermolecular forces, we tested the sensitivity of various contractile parameters of skinned skeletal muscle fibers to ionic strength (IS) at 3-5 degrees C; IS variation is a useful technique for distinguishing between ionic and nonionic (primarily hydrophobic) types of intermolecular forces. The most striking effect of elevated IS was the strong suppression of isometric tension. However, none of the measured parameters suggested a corresponding decrease in the number of force-generating myosin heads on actin. The rate of actin-myosin association seemed to be only modestly IS-sensitive. The following force-generating isomerization was apparently IS-insensitive. The dissociation of the force-generating actomyosin complex was decelerated by elevated IS, contrary to the expectation from the suppressed isometric tension. These results led us to conclude that an IS-sensitive step, responsible for the large suppression of tension, occurs after force-generating isomerization but before dissociation. The present study suggests that the actomyosin interaction is generally nonionic in nature, but there are at least two ionic processes, one at the beginning and the other close to the end of the actomyosin interaction.
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.