ArticleProceedings of the National Academy of Sciences of the United States of America2025
The highly conserved C-terminal end segment of troponin T binds tropomyosin and actin to function in modulating contractile kinetics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. 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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4 authors.
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Abstract
The troponin (Tn) complex plays a central role in regulating striated muscle contraction and relaxation. Troponin T (TnT) and troponin I (TnI) are two of the three subunits of Tn, which have evolved from a TnI-like ancestor gene. Proteolytic removal of the evolutionarily added N-terminal variable region of cardiac TnT, as occurs in acute ventricular contractility-afterload mismatch, brings back a TnI-like molecular conformation and function to reduce ventricular systolic velocity, elongates ejection time, and sustains stroke volume. Investigating the underlying mechanism found in addition to the two previously known tropomyosin (Tm)-binding sites another Tm-binding site in the highly conserved C-terminal end segment of TnT, which is also an F-actin binding site. Its functionality is retained in the form of free peptide with an effect on cardiac muscle contractile kinetics. Hypertrophic cardiomyopathy mutations in this segment significantly decrease Tm-binding affinity. The finding of a third Tm-binding site and localizing the actin-binding site of TnT revise our understanding of the dynamic interactions between Tn and actin thin filament with physiological and pathophysiological implications.
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