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Results: 4
THE 3-DIMENSIONAL STRUCTURE OF A CLASS-PI GLUTATHIONE-S-TRANSFERASE COMPLEXED WITH GLUTATHIONE - THE ACTIVE-SITE HYDRATION PROVIDES INSIGHTS INTO THE REACTION-MECHANISM
Authors: PARRAGA A GARCIASAEZ I WALSH SB MANTLE TJ COLL M
Citation: A. Parraga et al., THE 3-DIMENSIONAL STRUCTURE OF A CLASS-PI GLUTATHIONE-S-TRANSFERASE COMPLEXED WITH GLUTATHIONE - THE ACTIVE-SITE HYDRATION PROVIDES INSIGHTS INTO THE REACTION-MECHANISM, Biochemical journal, 333, 1998, pp. 811-816
THE 3-DIMENSIONAL STRUCTURE OF CYS-47-MODIFIED MOUSE-LIVER GLUTATHIONE-S-TRANSFERASE P1-1 - CARBOXYMETHYLATION DRAMATICALLY DECREASES THE AFFINITY FOR GLUTATHIONE AND IS ASSOCIATED WITH A LOSS OF ELECTRON-DENSITY IN THE ALPHA-B-3(10)B REGION
Authors: VEGA MC WALSH SB MANTLE TJ COLL M
Citation: Mc. Vega et al., THE 3-DIMENSIONAL STRUCTURE OF CYS-47-MODIFIED MOUSE-LIVER GLUTATHIONE-S-TRANSFERASE P1-1 - CARBOXYMETHYLATION DRAMATICALLY DECREASES THE AFFINITY FOR GLUTATHIONE AND IS ASSOCIATED WITH A LOSS OF ELECTRON-DENSITY IN THE ALPHA-B-3(10)B REGION, The Journal of biological chemistry, 273(5), 1998, pp. 2844-2850
EVIDENCE FOR MODULATION OF THE INTERACTION BETWEEN CYS-47 AND LYS-54 IN GLUTATHIONE-S-TRANSFERASE-PI BY THE NATURE OF THE RESIDUE AT POSITION-56
Authors: WALSH SB FRANKLIN E MANTLE TJ
Citation: Sb. Walsh et al., EVIDENCE FOR MODULATION OF THE INTERACTION BETWEEN CYS-47 AND LYS-54 IN GLUTATHIONE-S-TRANSFERASE-PI BY THE NATURE OF THE RESIDUE AT POSITION-56, Biochemical Society transactions, 25(4), 1997, pp. 614-614
MODIFICATION OF MOUSE-LIVER GLUTATHIONE-S-TRANSFERASE-PI BY IODOACETIC ACID
Authors: WALSH SB MANTLE TJ
Citation: Sb. Walsh et Tj. Mantle, MODIFICATION OF MOUSE-LIVER GLUTATHIONE-S-TRANSFERASE-PI BY IODOACETIC ACID, Biochemical Society transactions, 23(3), 1995, pp. 485-485
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