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The oriental fruit fly, Bactrocera dorsalis (Hendel), a widespread agricultural pest, has evolved resistance to many insecticides including organophosphorus compounds. Glutathione S-transferases (GSTs) are involved in xenobiotic detoxification and insecticide resistance in many insects. However, the role of delta class GSTs in detoxifying malathion in B. dorsalis is unknown. Here, we evaluated the roles of two delta class GSTs in malathion detoxification in this species.
This article was published in the following journal.
Name: Pest management science
Glutathione S-transferases (GSTs) are important detoxification enzymes involved in the metabolic resistance development of Plutella xylostella. Uncovering the interactions between representative PxGST...
Heavy metal and metalloid contaminations are among the most concerning types of pollutant in the environment. Consequently, it is important to investigate the molecular mechanisms of cellular response...
In this study, the entire glutathione S-transferases (GSTs), the major phase II detoxification enzyme, were identified in two marine copepod species Tigriopus japonicus and Paracyclopina nana. The gen...
The cattle tick Rhipicephalus microplus is one of the most important ectoparasites with great sanitary and economic impact for cattle rearing worldwide. Ivermectin is commonly used to control tick pop...
Glutathione S-transferases (GSTs) are a superfamily of multifunctional dimeric proteins existing in both prokaryotic and eukaryotic organisms. They are involved in detoxification of both endogenous an...
In this study, 24 adult patients with head lice will be treated with a topical malathion head lice treatment; 12 patients will be treated with a novel product, Malathion Gel, 0.5%, and oth...
In this study, Malathion Gel 0.5% will be compared to Nix (permethrin 1%) as a treatment for head lice in patients 2 years of age and older. Malathion Gel 0.5% is a new formulation of an e...
Current treatments for head lice include over-the-counter products such as permethrin and prescription products such as OVIDE (malathion 0.5%) lotion. In a previous phase II study, a nove...
This is a double-blind, placebo-controlled crossover study to evaluate the safety and efficacy of glutathione alone or glutathione, vitamin C and NAC treatment in children with autism who ...
Availability of sulfur amino acids (SAA) is critical for glutathione/glutathione disulfide (GSH/GSSG) and cysteine/cystine (CYS/CYSS) redox in vivo and for many other physiologic functions...
A subclass of transferases that transfer chemical groups containing a single carbon. These include the METHYLTRANSFERASES, the HYDROXYMETHYL AND FORMYL TRANSFERASES, the CARBOXYL AND CARBAMOYL TRANSFERASES, and the AMIDINOTRANSFERASES. EC 2.1.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 126.96.36.199.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 188.8.131.52.
A glutathione transferase that catalyzes the conjugation of electrophilic substrates to GLUTATHIONE. This enzyme has been shown to provide cellular protection against redox-mediated damage by FREE RADICALS.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.