ArticleBiophysical journal2010
Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.Frontiers in physiology · 2025Article
- Mechanistic insights into effects of the cardiac myosin activator omecamtiv mecarbil from mechanokinetic modelling.Frontiers in physiology · 2025Article
- Insights into Muscle Contraction Derived from the Effects of Small-Molecular Actomyosin-Modulating Compounds.International journal of molecular sciences · 2022Article
- Multistep orthophosphate release tunes actomyosin energy transduction.Nature communications · 2022Article
- Critical Evaluation of Current Hypotheses for the Pathogenesis of Hypertrophic Cardiomyopathy.International journal of molecular sciences · 2022Review
- The Synergic Role of Actomyosin Architecture and Biased Detachment in Muscle Energetics: Insights in Cross Bridge Mechanism Beyond the Lever-Arm Swing.International journal of molecular sciences · 2021Article
- 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
- The effects of inorganic phosphate on muscle force development and energetics: challenges in modelling related to experimental uncertainties.Journal of muscle research and cell motility · 2021Article
- Switch-1 instability at the active site decouples ATP hydrolysis from force generation in myosin II.Cytoskeleton (Hoboken, N.J.) · 2021Article
- Active Force Generation in Cardiac Muscle Cells: Mathematical Modeling and Numerical Simulation of the Actin-Myosin Interaction.Vietnam journal of mathematics · 2021Review
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
- The Location and Rate of the Phosphate Release Step in the Muscle Cross-Bridge Cycle.Biophysical journal · 2020Article
- Cardiac muscle regulatory units are predicted to interact stronger than neighboring cross-bridges.Scientific reports · 2020Article
- Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity.The Journal of general physiology · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- On the Shape of the Force-Velocity Relationship in Skeletal Muscles: The Linear, the Hyperbolic, and the Double-Hyperbolic.Frontiers in physiology · 2019Review
- A new myofilament contraction model with ATP consumption for ventricular cell model.The journal of physiological sciences : JPS · 2018Article
- Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin.Biophysical journal · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
Corrections and comments
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1 author.
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Abstract
Despite intense efforts to elucidate the molecular mechanisms that determine the maximum shortening velocity and the shape of the force-velocity relationship in striated muscle, our understanding of these mechanisms remains incomplete. Here, this issue is addressed by means of a four-state cross-bridge model with significant explanatory power for both shortening and lengthening contractions. Exploration of the parameter space of the model suggests that an actomyosin-ADP state (AM( *)ADP) that is separated from the actual ADP release step by a strain-dependent isomerization is important for determining both the maximum shortening velocity and the shape of the force-velocity relationship. The model requires a velocity-dependent, cross-bridge attachment rate to account for certain experimental findings. Of interest, the velocity dependence for shortening contraction is similar to that for population of the AM( *)ADP state (with a velocity-independent attachment rate). This accords with the idea that attached myosin heads in the AM( *)ADP state position the partner heads for rapid attachment to the next site along actin, corresponding to the apparent increase in attachment rate in the model.
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