ArticleThe Journal of physiology2001
Strong binding of myosin increases shortening velocity of rabbit skinned skeletal muscle fibres at low levels of Ca(2+).
Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Negative Charges Introduced Near the IT Helix of Cardiac Troponin T Stabilize the Active State of Actin Filaments.Biochemistry · 2023Article
- cMyBP-C phosphorylation modulates the time-dependent slowing of unloaded shortening in murine skinned myocardium.The Journal of general physiology · 2021Article
- CaAmerican journal of physiology. Cell physiology · 2020Article
- Structural determinants of muscle thin filament cooperativity.Archives of biochemistry and biophysics · 2016Review
- The novel cardiac myosin activator omecamtiv mecarbil increases the calcium sensitivity of force production in isolated cardiomyocytes and skeletal muscle fibres of the rat.British journal of pharmacology · 2015Article
- Sarcomere length-dependent Ca2+ activation in skinned rabbit psoas muscle fibers: coordinated regulation of thin filament cooperative activation and passive force.The journal of physiological sciences : JPS · 2011Article
- Regulatory mechanism of length-dependent activation in skinned porcine ventricular muscle: role of thin filament cooperative activation in the Frank-Starling relation.The Journal of general physiology · 2010Article
- Activation of the calcium-regulated thin filament by myosin strong binding.Biophysical journal · 2003Article
- Regulatory proteins alter nucleotide binding to acto-myosin of sliding filaments in motility assays.Biophysical journal · 2003Article
- Thin filament activation and unloaded shortening velocity of rabbit skinned muscle fibres.The Journal of physiology · 2003Article
- Isotonic force modulates force redevelopment rate of intact frog muscle fibres: evidence for cross-bridge induced thin filament activation.The Journal of physiology · 2002Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
1. At low levels of activation, unloaded shortening of skinned skeletal muscle fibres takes place in two phases: an initial phase of high-velocity shortening followed by a phase of low-velocity shortening. The basis for Ca(2+) dependence of unloaded shortening velocity (V(o)) in the low-velocity phase was investigated by varying the level of thin filament activation with Ca(2+) and N-ethyl-maleimide myosin subfragment-1 (NEM-S1), a non-tension-generating, strong binding derivative of subfragment-1. V(o) was measured with the slack-test method. 2. Treatment of skinned fibres with 5 microM NEM-S1 eliminated the low-velocity phase of shortening but had no effect on the high-velocity phase of shortening during submaximal activation with Ca(2+), or on V(o) during maximal activation with Ca(2+). 3. Extensive washout of NEM-S1 from the treated fibres restored the low-velocity phase of shortening and returned low-velocity V(o) to pre-treatment values. 4. The effect of NEM-S1 to increase low-velocity V(o) can be explained in terms of a model in which strong binding myosin cross-bridges activate the thin filament to a state in which the rate of ADP release from the actin-myosin-ADP complex and the rate of cross-bridge detachment from actin are accelerated during unloaded shortening.
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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.