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Hayes, J.D. and Pulford, D.J. (1995) The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Critical Reviews in Biochemistry and Molecular Biology, 30, 445-600. doi:10.3109/10409239509083491

has been cited by the following article:

• TITLE: The molecular mechanism for DDT detoxification in Anopheles gambiae: A molecular docking study

  AUTHORS: William N. Setzer

  KEYWORDS: Malaria; DDT; Anopheles Gambiae; Glutathione S-transferase; Docking

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.2 No.2, June 2, 2011

  ABSTRACT: The epsilon class glutathione-S-transferase of Anopheles gambiae, agGSTe2, is capable of metabolizing DDT. A molecular docking analysis of DDT with agGSTe2 support an E2 elimination mechanism wherein the glutathione sulfur serves as the base to convert DDT to DDE.