An evolutionary approach to the design of glutathione-linked enzymes.

[1]  N. Vermeulen.  Glutathione S-transferases : structure, function and clinical implications , 2014 .

[2]  B. Mannervik.  The isoenzymes of glutathione transferase. , 2006, Advances in enzymology and related areas of molecular biology.

[3]  R. Lerner,et al.  Making chemistry selectable by linking it to infectivity. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[4]  L. Hansson,et al.  Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions. , 1997, Biochemistry.

[5]  T A Jones,et al.  Crystal structure of human glyoxalase I—evidence for gene duplication and 3D domain swapping , 1997, The EMBO journal.

[6]  W. Stemmer,et al.  Molecular evolution of an arsenate detoxification pathway by DNA shuffling , 1997, Nature Biotechnology.

[7]  B. Mannervik,et al.  The primary structure of monomeric yeast glyoxalase I indicates a gene duplication resulting in two similar segments homologous with the subunit of dimeric human glyoxalase I. , 1996, The Biochemical journal.

[8]  B. Mannervik,et al.  The High Activity of Rat Glutathione Transferase 8−8 with Alkene Substrates Is Dependent on a Glycine Residue in the Active Site (*) , 1995, The Journal of Biological Chemistry.

[9]  R. Lerner,et al.  From molecular diversity to catalysis: lessons from the immune system. , 1995, Science.

[10]  B. Mannervik,et al.  Glutathione transferases with novel active sites isolated by phage display from a library of random mutants. , 1995, Journal of molecular biology.

[11]  W. Stemmer.  DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[12]  B. Mannervik,et al.  Contribution of amino acid residue 208 in the hydrophobic binding site to the catalytic mechanism of human glutathione transferase A1-1. , 1994, Biochemistry.

[13]  M. Parker,et al.  Structure and function of glutathione S-transferases. , 1994, Biochimica et biophysica acta.

[14]  R. Huber,et al.  X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. , 1994, European journal of biochemistry.

[15]  G J Kleywegt,et al.  Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. , 1993, Journal of molecular biology.

[16]  B. Mannervik,et al.  Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties. , 1992, The Biochemical journal.

[17]  P G Schultz,et al.  At the crossroads of chemistry and immunology: catalytic antibodies. , 1991, Science.

[18]  H. Ammon,et al.  Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase: evidence for enzymic stabilization of sigma-complex intermediates in nucleophilic aromatic substitution reactions. , 1989, Biochemistry.

[19]  P. Karplus,et al.  Refined structure of glutathione reductase at 1.54 A resolution. , 1987, Journal of molecular biology.

[20]  B. Mannervik,et al.  Glutathione transferases--structure and catalytic activity. , 1988, CRC critical reviews in biochemistry.