ArticleCellular & molecular biology letters2010
The domain structure of Entamoeba α-actinin2.
Article in Cellular & molecular biology letters, 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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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Microbiota-derived indole differentially shapes Entamoeba histolytica physiology and promotes host-compatible colonization.PLoS neglected tropical diseases · 2026Article
- Article
- Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Entamoeba histolytica, a major agent of human amoebiasis, expresses two distinct forms of α-actinin, a ubiquitous actin-binding protein that is present in most eukaryotic organisms. In contrast to all metazoan α-actinins, in both isoforms the intervening rod domain that connects the N-terminal actin-binding domain with the C-terminal EF-hands is much shorter. It is suggested that these α-actinins may be involved in amoeboid motility and phagocytosis, so we cloned and characterised each domain of one of these α-actinins to better understand their functional role. The results clearly showed that the domains have properties very similar to those of conventional α-actinins.
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