ArticleThe protein journal2018
Interaction Between a Gelsolin from Dendrorhynchus zhejiangensis with Three Gelsolin-Like Domains and Actin In Vitro.
Article in The protein journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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5 authors at 1 institution in 1 country.
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Abstract
The gelsolin family proteins are best known for involvement in cytoskeletal rearrangement by controlling actin organization during a variety of cellular processes. Previously, a 1962 bp cDNA encoding a 41.7 kDa protein with three gelsolin-like domains (G domains) from Dendrorhynchus zhejiangensis was identified and named as DzGSN. In this study, the sequence and function of a novel member of the gelsolin family proteins from D. zhejiangensis have been analyzed. Sequence alignment indicates that DzGSN is highly homologous to human gelsolin (35% identity) and human CapG (36% identity). The important functional motifs and critical amino acids were identified. The nucleating- and severing-actin activities of recombinant DzGSN (rDzGSN) were then investigated by using atomic force microscopy in vitro. After incubation with rDzGSN in the presence of Ca
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