ArticleJournal of insect science (Online)2019
Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera: Delphacidae).
Article in Journal of insect science (Online), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 55 citations in OpenAlex.
- Role of Insect and Mammal Glutathione Transferases in Chemoperception.Biomolecules · 2023Review
- Article
- Genomic features of the polyphagous cotton leafworm Spodoptera littoralis.BMC genomics · 2022Article
- Sequence identification and expression profile of seven Dermacentor marginatus glutathione S-transferase genes.Experimental & applied acarology · 2020Article
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3 authors at 1 institution in 1 country.
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Abstract
Glutathione conjugation is a crucial step in xenobiotic detoxification. In the current study, we have functionally characterized an epsilon-class glutathione S-transferase (GST) from a brown planthopper Nilaparvata lugens (nlGSTE). The amino acid sequence of nlGSTE revealed approximately 36-44% identity with epsilon-class GSTs of other species. The recombinant nlGSTE was prepared in soluble form by bacterial expression and was purified to homogeneity. Mutation experiments revealed that the putative substrate-binding sites, including Phe107, Arg112, Phe118, and Phe119, were important for glutathione transferase activity. Furthermore, inhibition study displayed that nlGSTE activity was affected by insecticides, proposing that, in brown planthopper, nlGSTE could recognize insecticides as substrates.
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