ArticleJournal of molecular biology2011
The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Myosin and tropomyosin-troponin complementarily regulate thermal activation of muscles.The Journal of general physiology · 2023Article
- The effect of gender and obesity in modulating cross-bridge function in cardiac muscle fibers.Journal of muscle research and cell motility · 2022Article
- The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals.Membranes · 2022Article
- Structural Effects of Disease-Related Mutations in Actin-Binding Period 3 of Tropomyosin.Molecules (Basel, Switzerland) · 2021Article
- Hypertrophic cardiomyopathy associated E22K mutation in myosin regulatory light chain decreases calcium-activated tension and stiffness and reduces myofilament CaThe FEBS journal · 2021Article
- Mutations Q93H and E97K inInternational journal of molecular sciences · 2021Article
- Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied withBiophysics and physicobiology · 2019Article
- Article
- Allergens and molecular diagnostics of shellfish allergy: Part 22 of the Series Molecular Allergology.Allergo journal international · 2016Review
- Myosin motor isoforms direct specification of actomyosin function by tropomyosins.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Complex tropomyosin and troponin T isoform expression patterns in orbital and global fibers of adult dog and rat extraocular muscles.Journal of muscle research and cell motility · 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
- Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin.Biophysical journal · 2012Article
- Periodicities designed in the tropomyosin sequence and structure define its functions.BioarchitectureReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
To establish α-tropomyosin (Tm)'s structure-function relationships in cooperative regulation of muscle contraction, thin filaments were reconstituted with a variety of Tm mutants (Δ2Tm, Δ3Tm, Δ6Tm, P2sTm, P3sTm, P2P3sTm, P1P5Tm, and wtTm), and force and sliding velocity of the thin filament were studied using an in vitro motility assay. In the case of deletion mutants, Δ indicates which of the quasi-equivalent repeats in Tm was deleted. In the case of period (P) mutants, an Ala cluster was introduced into the indicated period to strengthen the Tm-actin interaction. In P1P5Tm, the N-terminal half of period 5 was substituted with that of period 1 to test the quasi-equivalence of these two Tm periods. The reconstitution included bovine cardiac troponin. Deletion studies revealed that period 3 is important for the positive cooperative effect of Tm on actin filament regulation and that period 2 also contributes to this effect at low ionic strength, but to a lesser degree. Furthermore, Tm with one extra Ala cluster at period 2 (P2s) or period 3 (P3s) did not increase force or velocity, whereas Tm with two extra Ala clusters (P2P3s) increased both force and velocity, demonstrating interaction between these periods. Most mutants did not move in the absence of Ca(2+). Notable exceptions were Δ6Tm and P1P5Tm, which moved near at the full velocity, but with reduced force, which indicate impaired relaxation. These results are consistent with the mechanism that the Tm-actin interaction cooperatively affects actin to result in generation of greater force and velocity.
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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.