ArticleJournal of photochemistry and photobiology. B, Biology2010
The effects of formins on the conformation of subdomain 1 in actin filaments.
Article in Journal of photochemistry and photobiology. B, Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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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3 citing papers in PubMed.
- Polyphenols at the Helm: Excited State Photophysics and Mechanistic Insights Into Protein-Aggregation Inhibition Through Ultrafast Studies.Chemistry, an Asian journal · 2026Article
- Importance of a Lys113-Glu195 intermonomer ionic bond in F-actin stabilization and regulation by yeast formins Bni1p and Bnr1p.The Journal of biological chemistry · 2013Article
- Myosin and tropomyosin stabilize the conformation of formin-nucleated actin filaments.The Journal of biological chemistry · 2012Article
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4 authors.
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Abstract
In this study we investigated the effects of formins on the conformation of actin filaments by using the method of fluorescence quenching. Actin was labelled with IAEDANS at Cys(374) and the quencher was acrylamide. The results showed that formin binding induced structural changes in the subdomain 1 of actin protomers which were reflected by greater quenching constants (K(SV)). Simultaneously the fraction of the fluorophore population accessible for the quencher (alpha) decreased. These observations suggest that the conformational distribution characteristic for the actin protomers became broader after the binding of formins, for which the structural framework was provided by a more flexible protein matrix in the microenvironment of the label. The effects of formins depended on the formin:actin molar ratio, and also on the ionic strength of the medium. These observations are in agreement with previous results and underline the importance of the intramolecular conformational changes induced by formins in the structure of actin filaments.
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