ArticleBiophysical journal1993
Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament.
Article in Biophysical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 467 papers, 1 of them a synthesis that pooled it.
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Who cites it
467 citing papers in PubMed, 1 synthesis or guideline pooled it, 835 citations in OpenAlex.
- Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation.Frontiers in physiology · 2022Pooled it
- Form and function of actin impacts actin health and aging.iScience · 2026Article
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- Subsarcomeric regulation of thin and thick filaments in skeletal muscle myofibrils.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Fine-tuning striated muscle performance: conserved sarcomere-level mechanisms across insect and vertebrate systems.Frontiers in physiology · 2026Review
- The Structural Role of Tropomyosin in Regulating Thin Filament Activation of Actin-Myosin Interaction.Sub-cellular biochemistry · 2026Review
- Direct measurement of mavacamten and deoxyATP perturbation of the SRX/DRX ratio in porcine cardiac myofibrils using a simple, accessible and multiplexed approach.Journal of muscle research and cell motility · 2025Article
- Form and function of actin impacts actin health and aging.bioRxiv : the preprint server for biology · 2025Article
- Functional redundancy and formin-isoform independent localization of tropomyosin paralogs in Saccharomyces cerevisiae.PLoS genetics · 2025Article
- Danicamtiv reduces myosin's working stroke but activates the thin filament by accelerating actomyosin attachment.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Resolving the structure and dynamics of the disordered C terminus of human cardiac troponin T and effects of cardiomyopathic mutations.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Comparative mechanistic analysis of danicamtiv and omecamtiv mecarbil's in vivo cardiac effects.The Journal of general physiology · 2025Article
- The role of the troponin T interactions with actin in regulation of cardiac thin filament revealed by the troponin T pathogenic variant Ile79Asn.Journal of molecular and cellular cardiology · 2025Article
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Myosin binding protein-C modulates loaded sarcomere shortening in rodent permeabilized cardiac myocytes.The Journal of general physiology · 2025Article
- Myosin-actin crossbridge independent sarcomere length induced CaJournal of molecular and cellular cardiology · 2025Article
- Velcro-binding by cardiac troponin-I traps tropomyosin on actin in a low-energy relaxed state.Biochemical and biophysical research communications · 2025Article
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Modeling cardiac contractile cooperativity across species.The Journal of general physiology · 2025Article
407 more citing papers are in PubMed but not listed here.
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Funding
Abstract
Equilibrium titrations and kinetic experiments were used to define the cooperative binding of myosin subfragment 1 (S1) to actin-troponin-tropomyosin. Both types of experiment require an equilibrium between two states of the thin filament in which one state (the off state) binds S1 less readily than the other. Equilibrium titrations are compatible with > 95% of the actin7.Tn.Tm units being in the off state in the absence of calcium and 80% in the off state in the presence of calcium. Kinetic binding data suggest that the presence of calcium switches the thin filament from 70% in the off state to < 5%. The two experiments, therefore, define quite different populations of the off states. We propose a three-state model of the thin filament. A "blocked state" which is unable to bind S1, a "closed state" which can only bind S1 relatively weakly and an "open state" in which the S1 can both bind and undergo an isomerization to a more strongly bound rigor-like conformation. The equilibrium between the three states is calcium-dependent; KB = [closed]/[blocked] = 0.3 and > or = 16 and KT = [open]/[closed] = 0.09 and 0.25 in the absence and presence of calcium, respectively. This model can account for both types of experimental data.
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