Bivalent inhibitors of glutathione S-transferase: the effect of spacer length on isozyme selectivity.

@article{Maeda2006BivalentIO,
  title={Bivalent inhibitors of glutathione S-transferase: the effect of spacer length on isozyme selectivity.},
  author={Dean Y. Maeda and Sumit S. Mahajan and William M Atkins and John A. Zebala},
  journal={Bioorganic & medicinal chemistry letters},
  year={2006},
  volume={16 14},
  pages={3780-3}
}
Glutathione S-transferases (GSTs) are cytosolic enzymes that catalyze the conjugation of glutathione with a variety of exogenous and endogenous electrophiles. High affinity, isozyme-specific inhibitors of GST are required for use as pharmacological tools as well as potential therapeutics. The design of selective inhibitors is hindered due to the broad substrate binding capabilities of the GST enzymes. GSTs are dimeric enzymes, and therefore offer a unique discriminator for achieving inhibitor… CONTINUE READING

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