ArticleBiophysical journal1997
Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
109 citing papers in PubMed, 254 citations in OpenAlex.
- Force-Induced Ankle Opening Reveals Mechanical Stabilization of the Ankle of Human β-Cardiac Myosin.ACS nano · 2026Article
- Far-from-equilibrium thermodynamics of the human uterus: A self-organized dissipative structure.Physiological reports · 2025Article
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- 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
- Tail length and E525K dilated cardiomyopathy mutant alter human β-cardiac myosin super-relaxed state.The Journal of general physiology · 2024Article
- Collective Molecular Machines: Multidimensionality and Reconfigurability.Nano-micro letters · 2024Review
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Tail Length and E525K Dilated Cardiomyopathy Mutant Alter Human β-Cardiac Myosin Super-Relaxed State.bioRxiv : the preprint server for biology · 2023Article
- Thermodynamics and Kinetics of a Binary Mechanical System: Mechanisms of Muscle Contraction.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Molecular-level evidence of force maintenance by smooth muscle myosin during LC20 dephosphorylation.The Journal of general physiology · 2022Article
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- A chemical thermodynamic model of motor enzymes unifies chemical-Fx and powerstroke models.Biophysical journal · 2022Article
- High-Speed Optical Traps Address Dynamics of Processive and Non-Processive Molecular Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Actomyosin Complex.Sub-cellular biochemistry · 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
- Computational Tool for Ensemble Averaging of Single-Molecule Data.Biophysical journal · 2021Article
- Positional Isomers of a Non-Nucleoside Substrate Differentially Affect Myosin Function.Biophysical journal · 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
49 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Purified smooth muscle myosin in the in vitro motility assay propels actin filaments at 1/10 the velocity, yet produces 3-4 times more force than skeletal muscle myosin. At the level of a single myosin molecule, these differences in force and actin filament velocity may be reflected in the size and duration of single motion and force-generating events, or in the kinetics of the cross-bridge cycle. Specifically, an increase in either unitary force or duty cycle may explain the enhanced force-generating capacity of smooth muscle myosin. Similarly, an increase in attached time or decrease in unitary displacement may explain the reduced actin filament velocity of smooth muscle myosin. To discriminate between these possibilities, we used a laser trap to measure unitary forces and displacements from single smooth and skeletal muscle myosin molecules. We analyzed our data using mean-variance analysis, which does not rely on scoring individual events by eye, and emphasizes periods in the data with constant properties. Both myosins demonstrated multiple but similar event populations with discrete peaks at approximately +11 and -11 nm in displacement, and 1.5 and 3.5 pN in force. Mean attached times for smooth muscle myosin were longer than for skeletal-muscle myosin. These results explain much of the difference in actin filament velocity between these myosins, and suggest that an increased duty cycle is responsible for the enhanced force-generating capacity of smooth over skeletal-muscle myosin.
Indexed as
Identifiers
What OpenQuestion holds
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.