ArticleBiophysical journal2002
The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 123 citations in OpenAlex.
- The E525K β-Myosin Mutation Causes Hypocontractility in Cardiomyocytes Without Altering Loaded Crossbridge Cycling.bioRxiv : the preprint server for biology · 2026Article
- CaBiomolecules · 2025Review
- Scaling in Biological Systems: A Molecular-Ensemble Duality.bioRxiv : the preprint server for biology · 2025Article
- Considering the effect of Pi rebinding on myosin dynamics based on the distinct functions of cardiac and skeletal myosin.Frontiers in physiology · 2025Article
- Stochastic force generation in an isometric binary mechanical system.The Journal of general physiology · 2024Article
- Four phases of a force transient emerge from a binary mechanical system.Journal of muscle research and cell motility · 2024Article
- In defense of Huxley.Biophysical journal · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Design Principles and Benefits of Spatially Explicit Models of Myofilament Function.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The Problem with Inventing Molecular Mechanisms to Fit Thermodynamic Equations of Muscle.International journal of molecular sciences · 2023Article
- Cells solved the Gibbs paradox by learning to contain entropic forces.Scientific reports · 2023Article
- Article
- Thermodynamics and Kinetics of a Binary Mechanical System: Mechanisms of Muscle Contraction.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- A chemical thermodynamic model of motor enzymes unifies chemical-Fx and powerstroke models.Biophysical journal · 2022Article
- Force-velocity and tension transient measurements from Drosophila jump muscle reveal the necessity of both weakly-bound cross-bridges and series elasticity in models of muscle contraction.Archives of biochemistry and biophysics · 2021Article
- Evidence for S2 flexibility by direct visualization of quantum dot-labeled myosin heads and rods within smooth muscle myosin filaments moving on actin in vitro.The Journal of general physiology · 2021Article
- Complexity in genetic cardiomyopathies and new approaches for mechanism-based precision medicine.The Journal of general physiology · 2021Article
- Enhancing diastolic function by strain-dependent detachment of cardiac myosin crossbridges.The Journal of general physiology · 2020Article
- The load dependence and the force-velocity relation in intact myosin filaments from skeletal and smooth muscles.American journal of physiology. Cell physiology · 2020Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To better understand how skeletal muscle myosin molecules move actin filaments, we determine the motion-generating biochemistry of a single myosin molecule and study how it scales with the motion-generating biochemistry of an ensemble of myosin molecules. First, by measuring the effects of various ligands (ATP, ADP, and P(i)) on event lifetimes, tau(on), in a laser trap, we determine the biochemical kinetics underlying the stepwise movement of an actin filament generated by a single myosin molecule. Next, by measuring the effects of these same ligands on actin velocities, V, in an in vitro motility assay, we determine the biochemistry underlying the continuous movement of an actin filament generated by an ensemble of myosin molecules. The observed effects of P(i) on single molecule mechanochemistry indicate that motion generation by a single myosin molecule is closely associated with actin-induced P(i) dissociation. We obtain additional evidence for this relationship by measuring changes in single molecule mechanochemistry caused by a smooth muscle HMM mutation that results in a reduced P(i)-release rate. In contrast, we observe that motion generation by an ensemble of myosin molecules is limited by ATP-induced actin dissociation (i.e., V varies as 1/tau(on)) at low [ATP], but deviates from this relationship at high [ATP]. The single-molecule data uniquely provide a direct measure of the fundamental mechanochemistry of the actomyosin ATPase reaction under a minimal load and serve as a clear basis for a model of ensemble motility in which actin-attached myosin molecules impose a load.
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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.