ArticleBiophysical journal1991
A physical model of ATP-induced actin-myosin movement in vitro.
Article in Biophysical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 83 citations in OpenAlex.
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- Strain in shock-loaded skeletal muscle and the time scale of muscular wobbling mass dynamics.Scientific reports · 2017Article
- Role of Turnover in Active Stress Generation in a Filament Network.Physical review letters · 2016Article
- Muscle as a molecular machine for protecting joints and bones by absorbing mechanical impacts.Medical hypotheses · 2014Article
- Rigidity sensing explained by active matter theory.Biophysical journal · 2011Article
- Analysis of video-based microscopic particle trajectories using Kalman filtering.Biophysical journal · 2010Article
- The molecular basis of frictional loads in the in vitro motility assay with applications to the study of the loaded mechanochemistry of molecular motors.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Interactions between subunits in heterodimeric Ncd molecules.The Journal of biological chemistry · 2009Article
- Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis.Biophysical journal · 2007Article
- Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.Biophysical journal · 2001Article
- Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding.Biophysical journal · 2000Article
- A single-fiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers.Journal of muscle research and cell motility · 1999Article
- Fluctuation in the microtubule sliding movement driven by kinesin in vitro.Biophysical journal · 1996Article
- Weakly-coupled models for motor enzyme function.Journal of muscle research and cell motility · 1995Article
- A single-track fluctuation analysis in the sliding movement by protein motors in vitro.Biophysical journal · 1995Article
- Actin-crosslinking protein regulation of filament movement in motility assays: a theoretical model.Biophysical journal · 1994Article
- Kinetic mechanism of myofibril ATPase.Biophysical journal · 1994Article
- High frequency characteristics of elasticity of skeletal muscle fibres kept in relaxed and rigor state.Journal of muscle research and cell motility · 1994Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nature of the mechanism limiting the velocity of ATP-induced unidirectional movements of actin-myosin filaments in vitro is considered. In the sliding process two types of "cyclic" interactions between myosin heads and actin are involved, i.e., productive and nonproductive. In the productive interaction, myosin heads split ATP and generate a force which produces sliding between actin and myosin. In the nonproductive interaction "cycle," on the other hand, myosin heads rapidly attach to and detach from actin "reversibly," i.e., without splitting ATP or generating an active force. Such a nonproductive interaction "cycle" causes irreversible dissipation of sliding energy into heat, because the myosin cross-bridges during this interaction are passive elastic structures. This consideration has led us to postulate that such cross-bridges, in effect, exert viscous-like frictional drag on moving elements. Energetic considerations suggest that this frictional drag is much greater than the hydrodynamic viscous drag. We present a model in which the sliding velocity is limited by the balance between the force generated by myosin cross-bridges in the productive interaction and the frictional drag exerted by other myosin cross-bridges in the nonproductive interaction. The model is consistent with experimental findings of in vitro sliding, including the dependence of velocity on ATP concentration, as well as the sliding velocity of co-polymers of skeletal muscle myosin and phosphorylated and unphosphorylated smooth muscle myosins.
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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.