ArticleThe Biochemical journal2000
A simple method for measuring the relative force exerted by myosin on actin filaments in the in vitro motility assay: evidence that tropomyosin and troponin increase force in single thin filaments.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 76 citations in OpenAlex.
- Molecular Mechanisms of Effects of Lead and Cadmium Co-exposure on Atrial and Ventricular Myocardium: Soluble Salts Versus Nanoparticles.Cardiovascular toxicology · 2026Article
- Improved longevity of actomyosin in vitro motility assays for sustainable lab-on-a-chip applications.Scientific reports · 2024Article
- Dilated cardiomyopathy mutation in beta-cardiac myosin enhances actin activation of the power stroke and phosphate release.PNAS nexus · 2024Article
- Assessing Cardiac Contractility From Single Molecules to Whole Hearts.JACC. Basic to translational science · 2024Review
- The biochemically defined super relaxed state of myosin-A paradox.The Journal of biological chemistry · 2024Article
- Critical Evaluation of Current Hypotheses for the Pathogenesis of Hypertrophic Cardiomyopathy.International journal of molecular sciences · 2022Review
- Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021Review
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
- A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Science advances · 2017Article
- Robust mechanobiological behavior emerges in heterogeneous myosin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- A single-headed fission yeast myosin V transports actin in a tropomyosin-dependent manner.The Journal of cell biology · 2016Article
- Effects of hypertrophic and dilated cardiomyopathy mutations on power output by human β-cardiac myosin.The Journal of experimental biology · 2016Review
- Ensemble force changes that result from human cardiac myosin mutations and a small-molecule effector.Cell reports · 2015Article
- Hypertrophic cardiomyopathy associated Lys104Glu mutation in the myosin regulatory light chain causes diastolic disturbance in mice.Journal of molecular and cellular cardiology · 2014Article
- Hypertrophic and dilated cardiomyopathy: four decades of basic research on muscle lead to potential therapeutic approaches to these devastating genetic diseases.Biophysical journal · 2014Review
- Hypothesis and theory: mechanical instabilities and non-uniformities in hereditary sarcomere myopathies.Frontiers in physiology · 2014Article
- Molecular mechanical differences between isoforms of contractile actin in the presence of isoforms of smooth muscle tropomyosin.PLoS computational biology · 2013Article
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human β-cardiac myosin motor function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the effect of an internal load on the movement of actin filaments over a bed of heavy meromyosin (HMM) in the in vitro motility assay. Immobilized alpha-actinin can bind to actin filaments reversibly and ultimately stop the filaments from moving. Above a critical concentration of alpha-actinin, thin filament velocity rapidly diminished to zero. The fraction of thin motile filaments decreased linearly to zero with increasing alpha-actinin concentration. The concentration of alpha-actinin needed to stop all filaments from moving (0.8 microg/ml with actin) was very consistent both within and between experiments. In the present study we have defined the 'index of retardation' as the concentration of alpha-actinin needed to stop all filament movement, and we propose that this index is a measure of the isometric force exerted by HMM on actin filaments. When we measured the effect of immobilized alpha-actinin on motility in the presence of 10 mM P(i) we found that the index of retardation was 0.62+/-0.07 (n=3) times that in the absence of P(i). This observation is in agreement with the reduction of isometric tension in chemically-skinned muscle due to P(i). In a series of comparative experiments we observed that tropomyosin and troponin increase the index of retardation and that the degree of increase depends upon the tropomyosin isoform studied. The index of retardation of actin is increased 1.8-fold by skeletal-muscle tropomyosin, and 3-fold by both cardiac-muscle and smooth-muscle tropomyosin. In the presence of troponin the index of retardation is 2.9-3.4-fold greater than that of actin with all tropomyosin isoforms.
Indexed as
Identifiers
10970781PMC1221299W1970900771What 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.