ArticleBiophysical journal2006
Force generation in single conventional actomyosin complexes under high dynamic load.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
What it found
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Who cites it
104 citing papers in PubMed, 170 citations in OpenAlex.
- Force-Induced Ankle Opening Reveals Mechanical Stabilization of the Ankle of Human β-Cardiac Myosin.ACS nano · 2026Article
- Mechanotransduction through T cell receptors: consensus, controversies and future outlooks.Experimental & molecular medicine · 2026Review
- A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachment.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Ndc80 complex, a conserved coupler for kinetochore-microtubule motility, is a sliding molecular clutch.Science advances · 2025Article
- Considering the effect of Pi rebinding on myosin dynamics based on the distinct functions of cardiac and skeletal myosin.Frontiers in physiology · 2025Article
- A novel kinetic model to demonstrate the independent effects of ATP and ADP/Pi concentrations on sarcomere function.PLoS computational biology · 2024Article
- Design Principles and Benefits of Spatially Explicit Models of Myofilament Function.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Endocytic myosin-1 is a force-insensitive, power-generating motor.The Journal of cell biology · 2023Article
- Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023Article
- Single-molecule mechanics and kinetics of cardiac myosin interacting with regulated thin filaments.Biophysical journal · 2023Article
- Direct Measurement of Kinetic Force Generated by Mycoplasma.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Article
- Molecular mechanisms of cardiac actomyosin transforming from rigor state to post-rigor state.The Journal of chemical physics · 2022Article
- Microtubule Dumbbells to Assess the Effect of Force Geometry on Single Kinesin Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Application of optical tweezers in cardiovascular research: More than just a measuring tool.Frontiers in bioengineering and biotechnology · 2022Review
- High-Speed Optical Traps Address Dynamics of Processive and Non-Processive Molecular Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Cardiac myosin contraction and mechanotransduction in health and disease.The Journal of biological chemistry · 2021Review
- Imaging methods in mechanosensing: a historical perspective and visions for the future.Molecular biology of the cell · 2021Review
- Complexity in genetic cardiomyopathies and new approaches for mechanism-based precision medicine.The Journal of general physiology · 2021Article
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanical load borne by a molecular motor affects its force, sliding distance, and its rate of energy transduction. The control of ATPase activity by the mechanical load on a muscle tunes its efficiency to the immediate task, increasing ATP hydrolysis as the power output increases at forces less than isometric (the Fenn effect) and suppressing ATP hydrolysis when the force is greater than isometric. In this work, we used a novel 'isometric' optical clamp to study the mechanics of myosin II molecules to detect the reaction steps that depend on the dynamic properties of the load. An actin filament suspended between two beads and held in separate optical traps is brought close to a surface that is sparsely coated with motor proteins on pedestals of silica beads. A feedback system increases the effective stiffness of the actin by clamping the force on one of the beads and moving the other bead electrooptically. Forces measured during actomyosin interactions are increased at higher effective stiffness. The results indicate that single myosin molecules transduce energy nearly as efficiently as whole muscle and that the mechanical control of the ATP hydrolysis rate is in part exerted by reversal of the force-generating actomyosin transition under high load without net utilization of ATP.
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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.