ReviewJournal of muscle research and cell motility2008
Gestalt-binding of tropomyosin to actin filaments.
Review in Journal of muscle research and cell motility, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
What it found
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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.
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Who cites it
96 citing papers in PubMed.
- Mechanism of actin thin filament pointed-end elongation by leiomodin.Nature communications · 2026Article
- Disease-associated mutations inbioRxiv : the preprint server for biology · 2026Article
- The Structural Role of Tropomyosin in Regulating Thin Filament Activation of Actin-Myosin Interaction.Sub-cellular biochemistry · 2026Review
- Screening single nucleotide changes to tropomyosin to identify novel cardiomyopathy mutants.Journal 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
- Cryo-EM structures of cardiac muscle α-actin mutants M305L and A331P give insights into the structural mechanisms of hypertrophic cardiomyopathy.European journal of cell biology · 2024Article
- Article
- Myosin's powerstroke transitions define atomic scale movement of cardiac thin filament tropomyosin.The Journal of general physiology · 2024Article
- Troponin-I-induced tropomyosin pivoting defines thin-filament function in relaxed and active muscle.The Journal of general physiology · 2023Article
- Molecular Dynamics Assessment of Mechanical Properties of the Thin Filaments in Cardiac Muscle.International journal of molecular sciences · 2023Article
- Myosin loop-4 is critical for optimal tropomyosin repositioning on actin during muscle activation and relaxation.The Journal of general physiology · 2023Article
- mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.Journal of cell science · 2022Article
- Distinct actin-tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes.iScience · 2022Article
- Genotype-Phenotype Associations with Restrictive Cardiomyopathy Induced by Pathogenic Genetic Mutations.Reviews in cardiovascular medicine · 2022Review
- Effect of pressure cooking alone and in combination with other treatments on shrimp allergic protein, tropomyosin.Journal of food science and technology · 2022Article
- Modeling Human Cardiac Thin Filament Structures.Frontiers in physiology · 2022Review
- The Oxidative Balance Orchestrates the Main Keystones of the Functional Activity of Cardiomyocytes.Oxidative medicine and cellular longevity · 2022Review
- Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activity.The Journal of biological chemistry · 2020Article
- Cryo-EM and Molecular Docking Shows Myosin Loop 4 Contacts Actin and Tropomyosin on Thin Filaments.Biophysical journal · 2020Article
- Article
36 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We argue that the overall behavior of tropomyosin on F-actin cannot be easily discerned by examining thin filaments reduced to their smallest interacting units. In isolation, the individual interactions of actin and tropomyosin, by themselves, are too weak to account for the specificity of the system. Instead the association of tropomyosin on actin can only be fully explained after considering the concerted action of the entire acto-tropomyosin system. We propose that the low K ( a ) describing tropomyosin:actin interaction, when taken together with the form-fitting complementarity of tropomyosin strands on F-actin and the tendency for tropomyosin to polymerize end-to-end, make possible unique thin filament functions both locally and at higher levels of filament organization.
Indexed as
Identifiers
19116763What 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.