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Drug Metabolism and Disposition: the Biological Fate of Chemicals|May 1, 1988
Stereoselectivity and regioselectivity of purified human glutathione transferases pi, alpha-epsilon, and mu with alkene and polycyclic arene oxide substratesL A Dostal, C Guthenberg, B Mannervik, et al.
The Biochemical Journal|January 10, 1998
Mutagenesis of residue 157 in the active site of human glyoxalase IM Ridderström, A D Cameron, T A Jones, et al.
The Journal of Biological Chemistry|April 1, 2000
A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1G Stenberg, B Dragani, R Cocco, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1994
Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferasesK Berhane, M Widersten, A Engström, et al.
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