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The Journal of Biological Chemistry|July 27, 2001
Human glutathione transferase A1-1 demonstrates both half-of-the-sites and all-of-the-sites reactivityS Lien, A Gustafsson, A K Andersson, et al.
Biochimica Et Biophysica Acta|October 6, 2000
The active-site residue tyr-175 in human glyoxalase II contributes to binding of glutathione derivativesM Ridderström, P Jemth, A D Cameron, et al.
The Biochemical Journal|June 1, 1991
Heterologous expression of the allelic variant mu-class glutathione transferases mu and psiM Widersten, W R Pearson, A Engström, et al.
The Biochemical Journal|August 1, 1983
Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of low-molecular-mass and protein disulphidesB Mannervik, K Axelsson, A C Sundewall, et al.
Biochimica Et Biophysica Acta|August 1, 1980
Induction of glutathione S-transferases A, B and C in rat liver cytosol by trans-stilbene oxideC Guthenberg, R Morgenstern, J W DePierre, et al.
Comparative Biochemistry and Physiology. B, Comparative Biochemistry|January 1, 1985
Immunological comparison of glyoxalase I from yeast and mammals and quantitative determination of the enzyme in human tissues by radioimmunoassayK Larsen, A C Aronsson, E Marmstål, et al.
Journal of Molecular Biology|June 20, 1998
Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105A S Johansson, G Stenberg, M Widersten, et al.
Structure (London, England : 1993)|October 6, 1999
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogueA D Cameron, M Ridderström, B Olin, et al.
The Journal of Biological Chemistry|October 26, 2000
Yeast glyoxalase I is a monomeric enzyme with two active sitesE M Frickel, P Jemth, M Widersten, et al.
The Biochemical Journal|March 1, 1992
Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic propertiesR Björnestedt, M Widersten, P G Board, et al.
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