ArticleParasitology research2008
Identification and characterization of a mitochondrial iron-superoxide dismutase of Cryptosporidium parvum.
Article in Parasitology research, 2008. 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, 11 citations in OpenAlex.
- Determination of Serum Oxidative Stress, Antioxidant Capacity and Protein Profiles in Dogs Naturally Infected with Ehrlichia canis.Acta parasitologica · 2021Article
- Oxidative stress control by apicomplexan parasites.BioMed research international · 2015Review
- Functional expression and characterization of an iron-containing superoxide dismutase of Acanthamoeba castellanii.Parasitology research · 2012Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptosporidium parvum is an intracellular protozoan parasite that causes cryptosporidiosis in mammals. In this study, we identified a gene encoding mitochondrial iron-superoxide dismutase of C. parvum (Cp-mtSOD) and characterized biochemical properties of the recombinant protein. Multiple sequence alignment of the deduced amino acid sequence of Cp-mtSOD with those of previously reported iron-containing SODs (Fe-SODs) from other protozoan parasites showed that Cp-mtSOD shares common metal-binding residues and motifs that were conserved in Fe-SODs. However, the N-terminal 26-amino acid residues of Cp-mtSOD did not show sequence identities to any other Fe-SOD sequences. Further analysis of the N-terminal presequence of Cp-mtSOD suggested that it shares common physiochemical characteristics found in mitochondria targeting sequences and predicted localization of Cp-mtSOD in the mitochondria. The recombinant Cp-mtSOD showed typical biochemical properties with other characterized Fe-SODs, including molecular structure, broad pH optimum, and sensitivity to hydrogen peroxide.
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Registered trials
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