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175 related items for PubMed ID: 20097269
1. Residue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1. Shokeer A, Mannervik B. Biochim Biophys Acta; 2010 Apr; 1800(4):466-73. PubMed ID: 20097269 [Abstract] [Full Text] [Related]
2. Residue 234 in glutathione transferase T1-1 plays a pivotal role in the catalytic activity and the selectivity against alternative substrates. Shokeer A, Larsson AK, Mannervik B. Biochem J; 2005 May 15; 388(Pt 1):387-92. PubMed ID: 15683365 [Abstract] [Full Text] [Related]
3. Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1. Widersten M, Björnestedt R, Mannervik B. Biochemistry; 1996 Jun 18; 35(24):7731-42. PubMed ID: 8672473 [Abstract] [Full Text] [Related]
4. Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. Bruns CM, Hubatsch I, Ridderström M, Mannervik B, Tainer JA. J Mol Biol; 1999 May 07; 288(3):427-39. PubMed ID: 10329152 [Abstract] [Full Text] [Related]
5. Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant. Tars K, Larsson AK, Shokeer A, Olin B, Mannervik B, Kleywegt GJ. J Mol Biol; 2006 Jan 06; 355(1):96-105. PubMed ID: 16298388 [Abstract] [Full Text] [Related]
6. Functional studies of single-nucleotide polymorphic variants of human glutathione transferase T1-1 involving residues in the dimer interface. Josephy PD, Pan D, Ianni MD, Mannervik B. Arch Biochem Biophys; 2011 Sep 15; 513(2):87-93. PubMed ID: 21781954 [Abstract] [Full Text] [Related]
7. Effects of directed mutagenesis on conserved arginine residues in a human Class Alpha glutathione transferase. Stenberg G, Board PG, Carlberg I, Mannervik B. Biochem J; 1991 Mar 01; 274 ( Pt 2)(Pt 2):549-55. PubMed ID: 2006917 [Abstract] [Full Text] [Related]
8. An ensemble of theta class glutathione transferases with novel catalytic properties generated by stochastic recombination of fragments of two mammalian enzymes. Broo K, Larsson AK, Jemth P, Mannervik B. J Mol Biol; 2002 Apr 19; 318(1):59-70. PubMed ID: 12054768 [Abstract] [Full Text] [Related]
9. Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation. Nilsson LO, Gustafsson A, Mannervik B. Proc Natl Acad Sci U S A; 2000 Aug 15; 97(17):9408-12. PubMed ID: 10900265 [Abstract] [Full Text] [Related]
10. Shifting substrate specificity of human glutathione transferase (from class Pi to class alpha) by a single point mutation. Nuccetelli M, Mazzetti AP, Rossjohn J, Parker MW, Board P, Caccuri AM, Federici G, Ricci G, Lo Bello M. Biochem Biophys Res Commun; 1998 Nov 09; 252(1):184-9. PubMed ID: 9813167 [Abstract] [Full Text] [Related]
11. Mutational analysis of human glutathione transferase A2-2 identifies structural elements supporting high activity with the prodrug azathioprine. Modén O, Zhang W, Mannervik B. Protein Eng Des Sel; 2012 Apr 09; 25(4):189-97. PubMed ID: 22334756 [Abstract] [Full Text] [Related]
12. Rat glutathione S-transferase M4-4: an isoenzyme with unique structural features including a redox-reactive cysteine-115 residue that forms mixed disulphides with glutathione. Cheng H, Tchaikovskaya T, Tu YS, Chapman J, Qian B, Ching WM, Tien M, Rowe JD, Patskovsky YV, Listowsky I, Tu CP. Biochem J; 2001 Jun 01; 356(Pt 2):403-14. PubMed ID: 11368767 [Abstract] [Full Text] [Related]
13. A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes. Comstock KE, Widersten M, Hao XY, Henner WD, Mannervik B. Arch Biochem Biophys; 1994 Jun 01; 311(2):487-95. PubMed ID: 8203914 [Abstract] [Full Text] [Related]
14. The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site. Björnestedt R, Tardioli S, Mannervik B. J Biol Chem; 1995 Dec 15; 270(50):29705-9. PubMed ID: 8530359 [Abstract] [Full Text] [Related]
15. Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Jemth P, Mannervik B. Arch Biochem Biophys; 1997 Dec 15; 348(2):247-54. PubMed ID: 9434735 [Abstract] [Full Text] [Related]
16. Engineering GST M2-2 for high activity with indene 1,2-oxide and indication of an H-site residue sustaining catalytic promiscuity. Norrgård MA, Mannervik B. J Mol Biol; 2011 Sep 09; 412(1):111-20. PubMed ID: 21821040 [Abstract] [Full Text] [Related]
17. Regio- and enantioselectivities in epoxide conjugations are modulated by residue 210 in Mu class glutathione transferases. Ivarsson Y, Mannervik B. Protein Eng Des Sel; 2005 Dec 09; 18(12):607-16. PubMed ID: 16251220 [Abstract] [Full Text] [Related]
18. Emergence of novel enzyme quasi-species depends on the substrate matrix. Kurtovic S, Shokeer A, Mannervik B. J Mol Biol; 2008 Sep 26; 382(1):136-53. PubMed ID: 18640124 [Abstract] [Full Text] [Related]
19. Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues. Tan KL, Chelvanayagam G, Parker MW, Board PG. Biochem J; 1996 Oct 01; 319 ( Pt 1)(Pt 1):315-21. PubMed ID: 8870684 [Abstract] [Full Text] [Related]
20. An approach to optimizing the active site in a glutathione transferase by evolution in vitro. Hansson LO, Widersten M, Mannervik B. Biochem J; 1999 Nov 15; 344 Pt 1(Pt 1):93-100. PubMed ID: 10548538 [Abstract] [Full Text] [Related] Page: [Next] [New Search]