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Mechanisms through which Glutathione S-Transferase-Mediated Resistance to Alkylating Molecules Can be Augmented

  • William E. Fahl
  • , Andrew M. Gulick
  • , Manoharan T. Herbert
  • , Wyeth W. Wasserman
  • , Jean C. Gallo
  • , Melinda L. Brady
  • University of Wisconsin-Madison

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

For the past two decades it has been known that several of the glutathione S-transferase (GST) isozymes are efficient at catalyzing the conjugation of electrophilic carcinogen and drug metabolites to the cellular nucleophile, glutathione. 1 - 2 Underlying these biochemical observations has been the assumption that conjugation of electrophiles to glutathione, with the concomitant decrease in alkylation of alternate sites in the cell, is an important event in protecting a cell and maintaining the integrity of its genome. 3 - 4.

Original languageEnglish
Title of host publicationStructure and Function of Glutathione S-Transferases
PublisherCRC Press
Pages237-247
Number of pages11
ISBN (Electronic)9781040900758
ISBN (Print)9781003760146
DOIs
StatePublished - Jan 1 2026

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