ReviewSub-cellular biochemistry2026
The Structural Role of Tropomyosin in Regulating Thin Filament Activation of Actin-Myosin Interaction.
Review in Sub-cellular biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Thin filament interaction and CaJournal of molecular and cellular cardiology · 2026Article
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1 author.
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Abstract
Myosin motor-heads projecting from muscle thick filaments interact cyclically with actin-based thin filament tracks, thereby driving inter-filament sliding that powers muscle contraction. Here, controlled recruitment of myosin heads from thick filaments leads pre-powerstroke myosin to bind weakly to actin. Myosin then isomerizes into strongly bound post-powerstroke conformations on actin, thus producing crossbridge motion in active muscles. In striated muscles, this process is regulated by a steric mechanism involving coiled-coil tropomyosin controlling access to myosin-binding sites on actin. Biochemical and structural studies suggest the regulatory mechanism involves tropomyosin occupying three average configurations on the actin thin filament, dependent on Ca
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