Glutathione transferases: a structural perspective

References

• Adler, V., Yin, Z., Fuchs, S. Y., Benezra, M., Rosario, L., Tew, K. D., et al. (1999). Regulation of JNK signaling by GSTp. EMBO J 18:1321–1334.
   PubMed Web of Science ®Google Scholar
• Ago, H., Kanaoka, Y., Irikura, D., Lam, B. K., Shimamura, T., Austen, K. F., et al. (2007). Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448:609–612.
   PubMed Web of Science ®Google Scholar
• Allocati, N., Casalone, E., Masulli, M., Polekhina, G., Rossjohn, J., Parker, M. W., et al. (2000). Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases. Biochem J 351(Pt 2):341–346.
   PubMed Web of Science ®Google Scholar
• Allocati, N., Federici, L., Masulli, M., Di Ilio, C. (2009). Glutathione transferases in bacteria. FEBS J 276:58–75.
   PubMed Web of Science ®Google Scholar
• Atkinson, H. J., Babbitt, P. C. (2009). Glutathione transferases are structural and functional outliers in the thioredoxin fold. Biochemistry 48:11108–11116.
   PubMed Web of Science ®Google Scholar
• Balogh, L. M., Le Trong, I., Kripps, K. A., Shireman, L. M., Stenkamp, R. E., Zhang, W., et al. (2010). Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal. Biochemistry 49:1541–1548.
   PubMed Web of Science ®Google Scholar
• Board, P. G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L. S., Schulte, G. K., et al. (2000). Identification, characterization and crystal structure of the omega class glutathione transferases. J Biol Chem 275:24798–24806.
   PubMed Web of Science ®Google Scholar
• Board, P. G., Taylor, M. C., Coggan, M., Parker, M. W., Lantum, H. B., Anders, M. W. (2003). Clarification of the role of key active site residues of glutathionetransferase zeta/maleylacetoacetate isomerase by a new spectrophotometric technique. Biochem J 374:731–737.
   PubMed Web of Science ®Google Scholar
• Boehlert, C. C., Armstrong, R. N. (1984). Investigation of the kinetic and stereochemical recognition of arene and azaarene oxides by isozymes A2 and C2 of glutathione S-transferase. Biochem Biophys Res Commun 121:980–986.
   PubMed Web of Science ®Google Scholar
• Bousset, L., Belrhali, H., Janin, J., Melki, R., Morera, S. (2001). Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9:39–46.
   PubMed Web of Science ®Google Scholar
• Bruns, C. M., Hubatsch, I., Ridderstrom, M., Mannervik, B., Tainer, J. A. (1999). Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J Mol Biol 288:427–439.
   PubMed Web of Science ®Google Scholar
• Cameron, A. D., Sinning, I., L’Hermite, G., Olin, B., Board, P. G., Mannervik, B., et al. (1995). Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure 3:717–727.
   PubMed Web of Science ®Google Scholar
• Cromer, B. A., Gorman, M. A., Hansen, G., Adams, J. J., Coggan, M., Littler, D. R., et al. (2007). Structure of the Janus protein human CLIC2. J Mol Biol 374:719–731.
   PubMed Web of Science ®Google Scholar
• Ferguson, A. D., McKeever, B. M., Xu, S., Wisniewski, D., Miller, D. K., Yamin, T. T., et al. (2007). Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science 317:510–512.
   PubMed Web of Science ®Google Scholar
• Fritz-Wolf, K., Becker, A., Rahlfs, S., Harwaldt, P., Schirmer, R. H., Kabsch, W., et al. (2003). X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum. Proc Natl Acad Sci U S A 100:13821–13826.
   PubMed Web of Science ®Google Scholar
• Gu, Y., Guo, J., Pal, A., Pan, S. S., Zimniak, P., Singh, S. V., et al. (2004). Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity. Biochemistry 43:15673–15679.
   PubMed Web of Science ®Google Scholar
• Gu, Y., Singh, S. V., Ji, X. (2000). Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide. Biochemistry 39:12552–12557.
   PubMed Web of Science ®Google Scholar
• Gu, Y., Xiao, B., Wargo, H. L., Bucher, M. H., Singh, S. V., Ji, X. (2003). Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide. Biochemistry 42:917–921.
   PubMed Web of Science ®Google Scholar
• Habig, W. H., Pabst, M. J., Fleischner, G., Gatmaitan, Z., Arias, I. M., Jakoby, W. B. (1974). The identity of glutathione S-transferase B with ligandin, a major binding protein of liver. Proc Natl Acad Sci U S A 71:3879–3882.
   PubMed Web of Science ®Google Scholar
• Hansen, A. M., Gu, Y., Li, M., Andrykovitch, M., Waugh, D. S., Jin, D. J., et al. (2005). Structural basis for the function of stringent starvation protein a as a transcription factor. J Biol Chem 280:17380–17391.
   PubMed Web of Science ®Google Scholar
• Harrop, S. J., DeMaere, M. Z., Fairlie, W. D., Reztsova, T., Valenzuela, S. M., Mazzanti, M., et al. (2001). Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. J Biol Chem 276:44993–45000.
   PubMed Web of Science ®Google Scholar
• Hayes, J. D., Flanagan, J. U., Jowsey, I. R. (2005). Glutathione transferases. Annu Rev Pharmacol Toxicol 45:51–88.
   PubMed Web of Science ®Google Scholar
• Hohwy, M., Spadola, L., Lundquist, B., Hawtin, P., Dahmen, J., Groth-Clausen, I., et al. (2008). Novel prostaglandin D synthase inhibitors generated by fragment-based drug design. J Med Chem 51:2178–2186.
   PubMed Web of Science ®Google Scholar
• Holm, P. J., Bhakat, P., Jegerschold, C., Gyobu, N., Mitsuoka, K., Fujiyoshi, Y., et al. (2006). Structural basis for detoxification and oxidative stress protection in membranes. J Mol Biol 360:934–945.
   PubMed Web of Science ®Google Scholar
• Inoue, T., Irikura, D., Okazaki, N., Kinugasa, S., Matsumura, H., Uodome, N., et al. (2003). Mechanism of metal activation of human hematopoietic prostaglandin D synthase. Nat Struct Biol 10:291–296.
   PubMedGoogle Scholar
• Jakobsson, P. J., Morgenstern, R., Mancini, J., Ford-Hutchinson, A., Persson, B. (1999a). Common structural features of MAPEG—a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Prot Sci 8:689–692.
   PubMed Web of Science ®Google Scholar
• Jakobsson, P. J., Thoren, S., Morgenstern, R., Samuelsson, B. (1999b). Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci U S A 96:7220–7225.
   PubMed Web of Science ®Google Scholar
• Jeppesen, M. G., Ortiz, P., Shepard, W., Kinzy, T. G., Nyborg, J., Andersen, G. R. (2003). The crystal structure of the glutathione S-transferase-like domain of elongation factor 1B gamma from Saccharomyces cerevisiae. J Biol Chem 278:47190–47198.
   PubMed Web of Science ®Google Scholar
• Ji, X., Armstrong, R. N., Gilliland, G. L. (1993). Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry 32:12949–12954.
   PubMed Web of Science ®Google Scholar
• Ji, X., Blaszczyk, J., Xiao, B., O’Donnell, R., Hu, X., Herzog, C., et al. (1999). Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry 38:10231–10238.
   PubMed Web of Science ®Google Scholar
• Ji, X., Johnson, W. W., Sesay, M. A., Dickert, L., Prasad, S. M., Ammon, H. L., et al. (1994). Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry 33:1043–1052.
   PubMed Web of Science ®Google Scholar
• Ji, X., Tordova, M., O’Donnell, R., Parsons, J. F., Hayden, J. B., Gilliland, G. L., et al. (1997). Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry 36:9690–9702.
   PubMed Web of Science ®Google Scholar
• Ji, X., von Rosenvinge, E. C., Johnson, W. W., Armstrong, R. N., Gilliland, G. L. (1996). Location of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallography. Proc Natl Acad Sci U S A 93:8208–8213.
   PubMed Web of Science ®Google Scholar
• Ji, X., von Rosenvinge, E. C., Johnson, W. W., Tomarev, S. I., Piatigorsky, J., Armstrong, R. N., et al. (1995). Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry 34:5317–5328.
   PubMed Web of Science ®Google Scholar
• Johansson, A. S., Mannervik, B. (2001). Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J Biol Chem 276:33061–33065.
   PubMed Web of Science ®Google Scholar
• Kanaoka, Y., Ago, H., Inagaki, E., Nanayama, T., Miyano, M., Kikuno, R., et al. (1997). Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell 90:1085–1095.
   PubMed Web of Science ®Google Scholar
• Kong, K. H., Nishida, M., Inoue, H., Takahashi, K. (1992a). Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione-S-transferase—chemical modification and site-directed mutagenesis studies. Biochem Biophys Res Commun 182:1122–1129.
   PubMed Web of Science ®Google Scholar
• Kong, K. H., Takasu, K., Inoue, H., Takahashi, K. (1992b). Tyrosine-7 in human class-pi glutathione-S-transferase is important for lowering the pKa of the thiol-group of glutathione in the enzyme-glutathione complex. Biochem Biophys Res Commun 184:194–197.
   PubMed Web of Science ®Google Scholar
• Laborde, E. (2010). Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death. Cell Death Differ 17:1373–1380.
   PubMed Web of Science ®Google Scholar
• Ladner, J. E., Parsons, J. F., Rife, C. L., Gilliland, G. L., Armstrong, R. N. (2004). Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry 43:352–361.
   PubMed Web of Science ®Google Scholar
• Li, J., Xia, Z., Ding, J. (2005). Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme. Prot Sci 14:2361–2369.
   PubMed Web of Science ®Google Scholar
• Littler, D. R., Brown, L. J., Breit, S. N., Perrakis, A., Curmi, P. M. (2010). Structure of human CLIC3 at 2 Å resolution. Proteins 78:1594–1600.
   PubMed Web of Science ®Google Scholar
• LoBello, M., Oakley, A. J., Battistoni, A., Mazzetti, A. P., Nuccetelli, M., Mazzarese, G., et al. (1997). Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme. Biochemistry 36:6207–6217.
   PubMed Web of Science ®Google Scholar
• Lyttle, M. H., Hocker, M. D., Hui, H. C., Caldwell, C. G., Aaron, D. T., Engqvist-Goldstein, A., et al. (1994). Isozyme-specific glutathione-S-transferase inhibitors: design and synthesis. J Med Chem 37:189–194.
   PubMed Web of Science ®Google Scholar
• Marsh, M., Shoemark, D. K., Jacob, A., Robinson, C., Cahill, B., Zhou, N.-Y., et al. (2008). Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation. J Mol Biol 384:165–177.
   PubMed Web of Science ®Google Scholar
• Martinez Molina, D., Wetterholm, A., Kohl, A., McCarthy, A. A., Niegowski, D., Ohlson, E., et al. (2007). Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase. Nature 448:613–616.
   PubMed Web of Science ®Google Scholar
• McTigue, M. A., Williams, D. R., Tainer, J. A. (1995). Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J Mol Biol 246:21–27.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., Harnnoi, T., Udomsinprasert, R., Jirajaroenrat, K., Ketterman, A. J., Wilce, M. C. J. (2001). The crystal structures of glutathione S-transferases isozymes 1–3 and 1–4 from Anopheles dirus species B. Prot Sci 10:2176–2185.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., Lo Bello, M., Mazzetti, A. P., Federici, G., Parker, M. W. (1997a). The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes. FEBS Lett 419:32–36.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., Lo Bello, M., Nuccetelli, M., Mazzetti, A.P., Parker, M. W. (1999). The ligandin (non-substrate) binding site of human pi class glutathione transferase is located in the electrophile binding site (H-site). J Mol Biol 291:913–926.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., LoBello, M., Battistoni, A., Ricci, G., Rossjohn, J., Villar, H. O., et al. (1997b). The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J Mol Biol 274:84–100.
   PubMed Web of Science ®Google Scholar
• Oakley, A. J., Rossjohn, J., LoBello, M., Caccuri, A. M., Federici, G., Parker, M. W. (1997c). The three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione. Biochemistry 36:576–585.
   PubMed Web of Science ®Google Scholar
• Parker, L. J., Ciccone, S., Italiano, L. C., Primavera, A., Oakley, A. J., Morton, C. J., et al. (2008). The anti-cancer drug chlorambucil as a substrate for the human polymorphic enzyme glutathione transferase P1-1: kinetic properties and crystallographic characterisation of allelic variants. J Mol Biol 380:131–144.
   PubMed Web of Science ®Google Scholar
• Perito, B., Allocati, N., Casalone, E., Masulli, M., Dragani, B., Polsinelli, M., et al. (1996). Molecular cloning and overexpression of a glutathione transferase gene from Proteus mirabilis. Biochem J 318(Pt 1):157–162.
   PubMed Web of Science ®Google Scholar
• Polekhina, G., Board, P. G., Blackburn, A. C., Parker, M. W. (2001). Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 40:1567–1576.
   PubMed Web of Science ®Google Scholar
• Prade, L., Huber, R., Manoharan, T. H., Fahl, W. E., Reuter, W. (1997). Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue, and inhibitor. Structure 5:1287–1295.
   PubMed Web of Science ®Google Scholar
• Reinemer, P., Dirr, H. W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G., et al. (1992). Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol 227:214–226.
   PubMed Web of Science ®Google Scholar
• Reinemer, P., Dirr, H. W., Ladenstein, R., Schaffer, J., Gallay, O., Huber, R. (1991). The 3-dimensional structure of class-pi glutathione-S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J 10:1997–2005.
   PubMed Web of Science ®Google Scholar
• Reinemer, P., Prade, L., Hof, P., Neuefeind, T., Huber, R., Zettl, R., et al. (1996). Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J Mol Biol 255:289–309.
   PubMed Web of Science ®Google Scholar
• Rossjohn, J., McKinstry, W. J., Oakley, A. J., Verger, D., Flanagan, J., Chelvanayagam, G., et al. (1998a). Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure 6:309–322.
   PubMed Web of Science ®Google Scholar
• Rossjohn, J., Polekhina, G., Feil, S. C., Allocati, N., Masulli, M., De Illio, C., et al. (1998b). A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6:721–734.
   PubMed Web of Science ®Google Scholar
• Sawicki, R., Singh, S. P., Mondal, A. K., Benes, H., Zimniak, P. (2003). Cloning, expression, and biochemical characterization of one epsilon-class (GST-3) and ten delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the epsilon class. Biochem J 370:661–669.
   PubMed Web of Science ®Google Scholar
• Schuller, D. J., Liu, Q., Kriksunov, I. A., Campbell, A. M., Barrett, J., Brophy, P. M., et al. (2005). Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus. Proteins 61:1024–1031.
   PubMed Web of Science ®Google Scholar
• Sinning, I., Kleywegt, G. J., Cowan, S. W., Reinemer, P., Dirr, H. W., Huber, R., et al. (1993). Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes. J Mol Biol 232:192–212.
   PubMed Web of Science ®Google Scholar
• Slaga, T. J., Bracken, W. J., Gleason, G., Levin, W., Yagi, H., Jerina, D. M., et al. (1979). Marked differences in the skin tumor-initiating activities of the optical enantiomers of the diastereomeric benzo(a)pyrene 7,8-diol-9,10-epoxides. Cancer Res 39:67–71.
   PubMed Web of Science ®Google Scholar
• Stacpoole, P. W., Henderson, G. N., Yan, Z., James, M. O. (1998). Clinical pharmacology and toxicology of dichloroacetate. Environ Health Perspect 106(Suppl 4):989–994.
   PubMed Web of Science ®Google Scholar
• Suzuki, T., Nishio, K., Tanabe, S. (2001). The MRP family and anticancer drug metabolism. Curr Drug Metab 2:367–377.
   PubMed Web of Science ®Google Scholar
• Tan, K. L., Chelvanayagam, G., Parker, M. W., Board, P. G. (1996). Mutagenesis of the active site of the human theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues. Biochem J 319:315–321.
   PubMed Web of Science ®Google Scholar
• Tanikawa, N., Ohmiya, Y., Ohkubo, H., Hashimoto, K., Kangawa, K., Kojima, M., et al. (2002). Identification and characterization of a novel type of membrane-associated prostaglandin E synthase. Biochem Biophys Res Commun 291:884–889.
   PubMed Web of Science ®Google Scholar
• Tew, K. D. (1994). Glutathione-associated enzymes in anticancer drug resistance. Cancer Res 54:4313–4320.
   PubMed Web of Science ®Google Scholar
• Thom, R., Cummins, I., Dixon, D. P., Edwards, R., Cole, D. J., Lapthorn, A. J. (2002). Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification. Biochemistry 41:7008–7020.
   PubMed Web of Science ®Google Scholar
• Thompson, L. C., Ladner, J. E., Codreanu, S. G., Harp, J., Gilliland, G. L., Armstrong, R. N. (2007). 2-hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida. Biochemistry 46:6710–6722.
   PubMed Web of Science ®Google Scholar
• Tocheva, E. I., Fortin, P. D., Eltis, L. D., Murphy, M. E. (2006). Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites. J Biol Chem 281:30933–30940.
   PubMed Web of Science ®Google Scholar
• Vargo, M. A., Colman, R. F. (2001). Affinity labeling of rat glutathione S-transferase isozyme 1-1 by 17beta -iodoacetoxy-estradiol-3-sulfate. J Biol Chem 276:2031–2036.
   PubMed Web of Science ®Google Scholar
• Watanabe, K., Ito, S., Yamamoto, S. (2008). Studies on membrane-associated prostaglandin E synthase-2 with reference to production of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT). Biochem Biophys Res Commun 367:782–786.
   PubMed Web of Science ®Google Scholar
• Weber, J. E., Oakley, A. J., Christ, A. N., Clark, A. G., Hayes, J. D., Hall, R., et al. (2010). Identification and characterisation of new inhibitors for the human hematopoietic prostaglandin D2 synthase. Eur J Med Chem 45:447–454.
   PubMed Web of Science ®Google Scholar
• Wilce, M. C., Board, P. G., Feil, S. C., Parker, M. W. (1995). Crystal structure of a theta-class glutathione transferase. EMBO J 14:2133–2143.
   PubMed Web of Science ®Google Scholar
• Xiao, B., Singh, S. P., Nanduri, B., Awasthi, Y. C., Zimniak, P., Ji, X. (1999). Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface. Biochemistry 38:11887–11894.
   PubMed Web of Science ®Google Scholar
• Yamada, T., Komoto, J., Watanabe, K., Ohmiya, Y., Takusagawa, F. (2005). Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2). J Mol Biol 348:1163–1176.
   PubMed Web of Science ®Google Scholar
• Yamada, T., Takusagawa, F. (2007). PGH2 degradation pathway catalyzed by GSH-heme complex bound microsomal prostaglandin E2 synthase type 2: the first example of a dual-function enzyme. Biochemistry 46:8414–8424.
   PubMed Web of Science ®Google Scholar
• Zhang, Z. R., Bai, M., Wang, X. Y., Zhou, J. M., Perrett, S. (2008). “Restoration” of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2. J Mol Biol 384:641–651.
   PubMed Web of Science ®Google Scholar