ArticleData in brief2019
Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin.
Article in Data in brief, 2019. 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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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- High-Speed Optical Traps Address Dynamics of Processive and Non-Processive Molecular Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Out-of-Equilibrium Biophysical Chemistry: The Case for Multidimensional, Integrated Single-Molecule Approaches.The journal of physical chemistry. B · 2021Article
- Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin.Data in brief · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ultrafast force-clamp spectroscopy is a single molecule technique based on laser tweezers with sub-millisecond and sub-nanometer resolution. The technique has been successfully applied to investigate the rapid conformational changes that occur when a myosin II motor from skeletal muscle interacts with an actin filament. Here, we share data on the kinetics of such interaction and experimental records collected under different forces [1]. The data can be valuable for researchers interested in the mechanosensitive properties of myosin II, both from an experimental and modeling point of view. The data is related to the research article "ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke" [2].
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Registered trials
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