ArticleBiophysical journal2012
Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 117 citations in OpenAlex.
- Cross-bridge model for predicting muscle short-range stiffness during movement.PLoS computational biology · 2026Article
- Isometric slow- and fast-contracting skeletal muscle fibres have more similar cellular and molecular properties at 37°C than at 25°C in older adults.The Journal of physiology · 2026Article
- Mechanoadaptation via Myosin Cytoplasmic Redistribution Protects Circulating Tumor Cells From Shear-induced Death During Hematogenous Dissemination.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Cross-bridge model-based quantification of muscle metabolite alterations leading to fatigue during all-out knee extension exercise.Frontiers in physiology · 2026Article
- A human skeletal muscle cross-bridge model to characterize the role of metabolite accumulation in muscle fatigue.Experimental physiology · 2025Article
- Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamic clamping induces rotation-to-beating transition of pinned filaments in gliding assays.Journal of the Royal Society, Interface · 2025Article
- Cellular and molecular contractile function in aged human skeletal muscle is altered by phosphate and acidosis and partially reversed with an ATP analog.American journal of physiology. Cell physiology · 2025Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk Using QCM-D.Cellular and molecular bioengineering · 2025Article
- Measuring emergent mechanical changes in cytoskeletal ensemblesFrontiers in cell and developmental biology · 2025Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk using QCM-D.bioRxiv : the preprint server for biology · 2024Article
- In defense of Huxley.Biophysical journal · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Homologous mutations in human β, embryonic, and perinatal muscle myosins have divergent effects on molecular power generation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Wave-like oscillations of clamped microtubules driven by collective dynein transport.Biophysical journal · 2024Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Virus-free transfection, transient expression, and purification of human cardiac myosin in mammalian muscle cells for biochemical and biophysical assays.Scientific reports · 2023Article
- Insights into Muscle Contraction Derived from the Effects of Small-Molecular Actomyosin-Modulating Compounds.International journal of molecular sciences · 2022Article
- Myosin II Adjusts Motility Properties and Regulates Force Production Based on Motor Environment.Cellular and molecular bioengineering · 2022Article
- Iron Supplementation Improves Skeletal Muscle Contractile Properties in Mice with CKD.Kidney360 · 2022Article
5 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
3 authors at 3 institutions in 1 country.
Funding
Abstract
In contracting muscle, individual myosin molecules function as part of a large ensemble, hydrolyzing ATP to power the relative sliding of actin filaments. The technological advances that have enabled direct observation and manipulation of single molecules, including recent experiments that have explored myosin's force-dependent properties, provide detailed insight into the kinetics of myosin's mechanochemical interaction with actin. However, it has been difficult to reconcile these single-molecule observations with the behavior of myosin in an ensemble. Here, using a combination of simulations and theory, we show that the kinetic mechanism derived from single-molecule experiments describes ensemble behavior; but the connection between single molecule and ensemble is complex. In particular, even in the absence of external force, internal forces generated between myosin molecules in a large ensemble accelerate ADP release and increase how far actin moves during a single myosin attachment. These myosin-induced changes in strong binding lifetime and attachment distance cause measurable properties, such as actin speed in the motility assay, to vary depending on the number of myosin molecules interacting with an actin filament. This ensemble-size effect challenges the simple detachment limited model of motility, because even when motility speed is limited by ADP release, increasing attachment rate can increase motility speed.
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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.