ArticleMethods in molecular biology (Clifton, N.J.)2024
Motility Assay to Probe the Calcium Sensitivity of Myosin and Regulated Thin Filaments.
Article in Methods in molecular biology (Clifton, N.J.), 2024. 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, 2 citations in OpenAlex.
- Mechanistic insights into effects of the cardiac myosin activator omecamtiv mecarbil from mechanokinetic modelling.Frontiers in physiology · 2025Article
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3 authors at 2 institutions in 1 country.
Funding
Abstract
Calcium-dependent activation of the thin filament mediated by the troponin-tropomyosin complex is key in the regulation of actin-myosin based muscle contraction. Perturbations to this system, either physiological (e.g., phosphorylation of myosin light chains) or pathological (e.g., mutations that cause familial cardiomyopathies), can alter calcium sensitivity and thus have important implications in human health and disease. The in vitro motility assay provides a quantitative and precise method to study the calcium sensitivity of the reconstituted myosin-thin filament motile system. Here we present a simple and robust protocol to perform calcium-dependent motility of β-cardiac myosin and regulated thin filaments. The experiment is done on a multichannel microfluidic slide requiring minimal amounts of proteins. A complete velocity vs. calcium concentration curve is produced from one experiment in under 1 h.
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