ArticleThe Journal of veterinary medical science2014
Cloning and characterization of a 2-Cys peroxiredoxin from Babesia gibsoni.
Article in The Journal of veterinary medical science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 9 citations in OpenAlex.
- A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target inFrontiers in veterinary science · 2020Article
- Identification of 2-Cys Peroxiredoxin (BmTPx-2) as Antioxidant Active Molecule fromFrontiers in microbiology · 2017Article
- Identification and functional analysis of a novel mitochondria-localized 2-Cys peroxiredoxin, BbTPx-2, from Babesia bovis.Parasitology research · 2016Article
- Oxidative stress control by apicomplexan parasites.BioMed research international · 2015Review
- New Molecules in Babesia gibsoni and their application for diagnosis, vaccine development, and drug discovery.The Korean journal of parasitology · 2014Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxiredoxins (Prxs) are a family of antioxidant enzymes. Here, we cloned a 2-Cys Prx, BgTPx-1, from the canine Babesia parasite B. gibsoni. Sequence identity between BgTPx-1 and 2-Cys Prx of B. bovis was 81% at the amino acid level. Enzyme activity assay by using recombinant BgTPx-1 (rBgTPx-1) indicated that BgTPx-1 has antioxidant activity. Antiserum from a mouse immunized with rBgTPx-1 reacted with parasite lysates and detect a protein with a monomeric size of 22 kDa and also a 44 kDa protein, which might be an inefficiently reduced dimer. BgTPx-1 was expressed in the cytoplasm of B. gibsoni merozoites. These results suggest that the BgTPx-1 may play a role to control redox balance in the cytoplasm of B. gibsoni.
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Registered trials
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