ReviewJournal of muscle research and cell motility2020
Functional outcomes of structural peculiarities of striated muscle tropomyosin.
Review in Journal of muscle research and cell motility, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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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
3 citing papers in PubMed, 6 citations in OpenAlex.
- Dilated Cardiomyopathy - Exploring the Underlying Causes.Medical research archives · 2024Article
- De Novo Asp219Val Mutation in Cardiac Tropomyosin Associated with Hypertrophic Cardiomyopathy.International journal of molecular sciences · 2022Article
- Impact of A134 and E218 Amino Acid Residues of Tropomyosin on Its Flexibility and Function.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tropomyosin is a dimer coiled-coil actin-binding protein. Adjacent tropomyosin molecules connect each other 'head-to-tail' via an overlap junction and form a continuous strand that winds around an actin filament and controls the actin-myosin interaction. High cooperativity of muscle contraction largely depends on tropomyosin characteristics. Here we summarise experimental evidence that local peculiarities of tropomyosin structure have long-range effects and determine functional properties of the strand, including changes in its bending stiffness and interaction with actin and myosin. Point mutations and posttranslational modifications help to probe the roles of the conserved 'non-canonical' residues, clusters of stabilising and destabilising core residues, and core gap in tropomyosin function. The data suggest that tropomyosin structural lability including a diversity of homo- and heterodimers of different isoforms provide a balance of stiffness, flexibility, and strength of interaction with partner sarcomere proteins necessary for fine-tuning of Ca
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Registered trials
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