메뉴 건너뛰기




Volumn 5-6, Issue , 2005, Pages 383-402

Glutathione Transferases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85069916631     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B0-44-451924-6/00074-0     Document Type: Chapter
Times cited : (66)

References (98)
  • 1
    • 0034486496 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA clone coding for a glutathione S-transferase class delta enzyme from the biting midge Culicoides variipennis sonorensis Wirth and Jones
    • Abdallah M.A., Pollenz R.S., Droog F.N., Nunamaker R.A., Tabachnick W.J., et al. Isolation and characterization of a cDNA clone coding for a glutathione S-transferase class delta enzyme from the biting midge Culicoides variipennis sonorensis Wirth and Jones. Biochem. Genet. 2000, 38:377-390.
    • (2000) Biochem. Genet. , vol.38 , pp. 377-390
    • Abdallah, M.A.1    Pollenz, R.S.2    Droog, F.N.3    Nunamaker, R.A.4    Tabachnick, W.J.5
  • 2
    • 0037423744 scopus 로고    scopus 로고
    • Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products
    • Agianian B., Tucker P.A., Schouten A., Leonard K., Bullard B., et al. Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products. J. Mol. Biol. 2003, 326:151-165.
    • (2003) J. Mol. Biol. , vol.326 , pp. 151-165
    • Agianian, B.1    Tucker, P.A.2    Schouten, A.3    Leonard, K.4    Bullard, B.5
  • 3
    • 0025971827 scopus 로고
    • Glutathione S-transferases: reaction mechanism, structure, and function
    • Armstrong R.N. Glutathione S-transferases: reaction mechanism, structure, and function. Chem. Res. Toxicol. 1991, 4:131-140.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 131-140
    • Armstrong, R.N.1
  • 5
    • 0030760310 scopus 로고    scopus 로고
    • Induction of IgE antibody responses by glutathione S-transferase from the German cockroach (Blattella germanica)
    • Arruda L.K., Vailes L.D., Platts-Mills T.A., Hayden M.L., Chapman M.D. Induction of IgE antibody responses by glutathione S-transferase from the German cockroach (Blattella germanica). J. Biol. Chem. 1997, 272:20907-20912.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20907-20912
    • Arruda, L.K.1    Vailes, L.D.2    Platts-Mills, T.A.3    Hayden, M.L.4    Chapman, M.D.5
  • 7
    • 0026485274 scopus 로고
    • Isolation of a Drosophila gene encoding glutathione S-transferase
    • Beall C., Fyrberg C., Song S., Fyrberg E. Isolation of a Drosophila gene encoding glutathione S-transferase. Biochem. Genet. 1992, 30:515-527.
    • (1992) Biochem. Genet. , vol.30 , pp. 515-527
    • Beall, C.1    Fyrberg, C.2    Song, S.3    Fyrberg, E.4
  • 8
    • 0032437157 scopus 로고    scopus 로고
    • Characterization and chromosome location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase
    • Blackburn A.C., Woollatt E., Sutherland G.R., Board P.G. Characterization and chromosome location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase. Cytogenet. Cell Genet. 1998, 83:109-114.
    • (1998) Cytogenet. Cell Genet. , vol.83 , pp. 109-114
    • Blackburn, A.C.1    Woollatt, E.2    Sutherland, G.R.3    Board, P.G.4
  • 9
    • 0028211428 scopus 로고
    • Purification, molecular cloning and heterologous expression of a glutathione S-transferase from the Australian sheep blowfly (Lucilia cuprina)
    • Board P., Russell R.J., Marano R.J., Oakeshott J.G. Purification, molecular cloning and heterologous expression of a glutathione S-transferase from the Australian sheep blowfly (Lucilia cuprina). Biochem. J. 1994, 299:425-430.
    • (1994) Biochem. J. , vol.299 , pp. 425-430
    • Board, P.1    Russell, R.J.2    Marano, R.J.3    Oakeshott, J.G.4
  • 10
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board P.G., Baker R.T., Chelvanayagam G., Jermiin L.S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 1997, 328:929-935.
    • (1997) Biochem. J. , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 11
    • 0034637481 scopus 로고    scopus 로고
    • Identification, characterization, and crystal structure of the Omega class glutathione transferases
    • Board P.G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L.S., et al. Identification, characterization, and crystal structure of the Omega class glutathione transferases. J. Biol. Chem. 2000, 275:24798-24806.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24798-24806
    • Board, P.G.1    Coggan, M.2    Chelvanayagam, G.3    Easteal, S.4    Jermiin, L.S.5
  • 12
    • 0000259325 scopus 로고
    • An enzyme from rat liver catalyzing conjugation with glutathione
    • Booth J., Boyland E., Sims P. An enzyme from rat liver catalyzing conjugation with glutathione. Biochem. J. 1961, 79:516-524.
    • (1961) Biochem. J. , vol.79 , pp. 516-524
    • Booth, J.1    Boyland, E.2    Sims, P.3
  • 13
    • 0028181442 scopus 로고
    • The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin (C14S) and glutathione
    • Bushweller J.H., Billeter M., Holmgren A., Wuthrich K. The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin (C14S) and glutathione. J. Mol. Biol. 1994, 235:1585-1597.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wuthrich, K.4
  • 14
    • 0030662474 scopus 로고    scopus 로고
    • Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly Lucilia cuprina
    • Caccuri A.M., Antonini G., Nicotra M., Battistoni A., Bello M.L., et al. Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly Lucilia cuprina. J. Biol. Chem. 1997, 272:29681-29686.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29681-29686
    • Caccuri, A.M.1    Antonini, G.2    Nicotra, M.3    Battistoni, A.4    Bello, M.L.5
  • 15
    • 0000104664 scopus 로고    scopus 로고
    • Fly fishing for GSTs: a unified nomenclature for mammalian and insect glutathione transferases
    • Chelvanayagam G., Parker M.W., Board P.G. Fly fishing for GSTs: a unified nomenclature for mammalian and insect glutathione transferases. Chem. Bio. Interact. 2001, 133:256-260.
    • (2001) Chem. Bio. Interact. , vol.133 , pp. 256-260
    • Chelvanayagam, G.1    Parker, M.W.2    Board, P.G.3
  • 16
    • 0002746624 scopus 로고
    • Glutathione transferase isozymes of diamondback moth larvae and their role in the degradation of some organophosphorous insecticides
    • Chiang F., Sun C. Glutathione transferase isozymes of diamondback moth larvae and their role in the degradation of some organophosphorous insecticides. Pest. Biochem. Physiol. 1993, 45:7-14.
    • (1993) Pest. Biochem. Physiol. , vol.45 , pp. 7-14
    • Chiang, F.1    Sun, C.2
  • 17
    • 0006551096 scopus 로고
    • Studies on glutathione S-transferase in Helicoverpa (= Heliothis) zea
    • Chien C., Dauterman W.C. Studies on glutathione S-transferase in Helicoverpa (= Heliothis) zea. Insect Biochem. 1991, 21:857-864.
    • (1991) Insect Biochem. , vol.21 , pp. 857-864
    • Chien, C.1    Dauterman, W.C.2
  • 18
    • 0029181832 scopus 로고
    • Separation of multiple forms of acidic glutathione S-transferase isozymes in a susceptible and a resistant strain of housefly, Musca domestica (L.)
    • Chien C., Motoyama N., Dauterman W.C. Separation of multiple forms of acidic glutathione S-transferase isozymes in a susceptible and a resistant strain of housefly, Musca domestica (L.). Arch. Insect Biochem. Physiol. 1995, 28:397-406.
    • (1995) Arch. Insect Biochem. Physiol. , vol.28 , pp. 397-406
    • Chien, C.1    Motoyama, N.2    Dauterman, W.C.3
  • 19
    • 0024488993 scopus 로고
    • The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms
    • Clark A.G. The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms. Comp. Biochem. Physiol. B 1989, 92:419-446.
    • (1989) Comp. Biochem. Physiol. B , vol.92 , pp. 419-446
    • Clark, A.G.1
  • 20
    • 0000903828 scopus 로고
    • The characterization by affinity chromatography of a glutathione S-transferase from different strains of housefly
    • Clark A.G., Dauterman W.C. The characterization by affinity chromatography of a glutathione S-transferase from different strains of housefly. Pestic. Biochem. Physiol. 1982, 17:307-314.
    • (1982) Pestic. Biochem. Physiol. , vol.17 , pp. 307-314
    • Clark, A.G.1    Dauterman, W.C.2
  • 21
    • 0003063265 scopus 로고
    • Glutatione S-transferases from the New Zealand grass grub, Costelytra zealandica
    • Clark A.G., Dick G.K., Martindale S.M., Smith J.N. Glutatione S-transferases from the New Zealand grass grub, Costelytra zealandica. Insect Biochem. 1985, 15:35-44.
    • (1985) Insect Biochem. , vol.15 , pp. 35-44
    • Clark, A.G.1    Dick, G.K.2    Martindale, S.M.3    Smith, J.N.4
  • 22
    • 0017579263 scopus 로고
    • The purification by affinity chromatography of a glutathione S-transferase from larvae of Galleria mellonella
    • Clark A.G., Letoa M., Ting W.S. The purification by affinity chromatography of a glutathione S-transferase from larvae of Galleria mellonella. Life Sci. 1977, 20:141-148.
    • (1977) Life Sci. , vol.20 , pp. 141-148
    • Clark, A.G.1    Letoa, M.2    Ting, W.S.3
  • 23
    • 0021738417 scopus 로고
    • Evidence that DDT dehydrochlorinase from the housefly is a glutathione S-transferase
    • Clark A.G., Shamaan N.A. Evidence that DDT dehydrochlorinase from the housefly is a glutathione S-transferase. Pestic. Biochem. Physiol. 1984, 22:249-261.
    • (1984) Pestic. Biochem. Physiol. , vol.22 , pp. 249-261
    • Clark, A.G.1    Shamaan, N.A.2
  • 24
    • 0022599357 scopus 로고
    • Insecticide metabolism by multiple glutathione S-transferases in two strains of the housefly, Musca domestica (L.)
    • Clark A.G., Shamaan N.A., Sinclair M.D., Dauterman W.C. Insecticide metabolism by multiple glutathione S-transferases in two strains of the housefly, Musca domestica (L.). Pestic. Biochem. Physiol. 1986, 25:169-175.
    • (1986) Pestic. Biochem. Physiol. , vol.25 , pp. 169-175
    • Clark, A.G.1    Shamaan, N.A.2    Sinclair, M.D.3    Dauterman, W.C.4
  • 25
    • 0031881901 scopus 로고    scopus 로고
    • Interaction of troponin-H and glutathione S-transferase-2 in the indirect flight muscles of Drosophila melanogaster
    • Clayton J.D., Cripps R.M., Sparrow J.C., Bullard B. Interaction of troponin-H and glutathione S-transferase-2 in the indirect flight muscles of Drosophila melanogaster. J. Muscle Res. Cell Motil. 1998, 19:117-127.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 117-127
    • Clayton, J.D.1    Cripps, R.M.2    Sparrow, J.C.3    Bullard, B.4
  • 27
    • 9144243812 scopus 로고    scopus 로고
    • The Anopheles gambiae glutathione transferase family: annotation, phylogeny and gene expression profiles
    • Ding Y., Ortelli F., Rossiter L., Hemingway J., Ranson H. The Anopheles gambiae glutathione transferase family: annotation, phylogeny and gene expression profiles. BMC Genom. 2003, 13:35.
    • (2003) BMC Genom. , vol.13 , pp. 35
    • Ding, Y.1    Ortelli, F.2    Rossiter, L.3    Hemingway, J.4    Ranson, H.5
  • 28
    • 0033180450 scopus 로고    scopus 로고
    • Dimerisation of maize glutathione transferases in recombinant bacteria
    • Dixon D.P., Cole D.J., Edwards R. Dimerisation of maize glutathione transferases in recombinant bacteria. Plant Mol. Biol. 1999, 40:997-1008.
    • (1999) Plant Mol. Biol. , vol.40 , pp. 997-1008
    • Dixon, D.P.1    Cole, D.J.2    Edwards, R.3
  • 29
    • 0029328493 scopus 로고
    • The separation and identification of glutathione S-transferase subunits from Orthosia gothica
    • Egaas E., Sandvik M., Svendsen N.O., Skaare J.U. The separation and identification of glutathione S-transferase subunits from Orthosia gothica. Insect Biochem. Mol. Biol. 1995, 25:783-788.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 783-788
    • Egaas, E.1    Sandvik, M.2    Svendsen, N.O.3    Skaare, J.U.4
  • 30
    • 0033198377 scopus 로고    scopus 로고
    • Glutathione S-transferase from the spruce budworm, Choristoneura fumiferana: identification, characterization, localization, cDNA cloning, and expression
    • Feng Q.L., Davey K.G., Pang A.S., Primavera M., Ladd T.R., et al. Glutathione S-transferase from the spruce budworm, Choristoneura fumiferana: identification, characterization, localization, cDNA cloning, and expression. Insect Biochem. Mol. Biol. 1999, 29:779-793.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 779-793
    • Feng, Q.L.1    Davey, K.G.2    Pang, A.S.3    Primavera, M.4    Ladd, T.R.5
  • 31
    • 0001939880 scopus 로고    scopus 로고
    • The molecular basis of adaptation in Drosophila
    • Plenum, New York, M.K. Hecht (Ed.)
    • Fogleman J.C., Danielson P.B., Macintyre R.J. The molecular basis of adaptation in Drosophila. Evolutionary Biology 1998, 15. Plenum, New York. M.K. Hecht (Ed.).
    • (1998) Evolutionary Biology , pp. 15
    • Fogleman, J.C.1    Danielson, P.B.2    Macintyre, R.J.3
  • 32
    • 0026575011 scopus 로고
    • Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides
    • Fournier D., Bride J.M., Poirie M., Berge J.B., Plapp F.W. Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides. J. Biol. Chem. 1992, 267:1840-1845.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1840-1845
    • Fournier, D.1    Bride, J.M.2    Poirie, M.3    Berge, J.B.4    Plapp, F.W.5
  • 33
    • 0029257154 scopus 로고
    • Glutathione S-transferases in housefly (Musca domestica): location of GST-1 and GST-2 families
    • Franciosa H., Berge J.B. Glutathione S-transferases in housefly (Musca domestica): location of GST-1 and GST-2 families. Insect Biochem. Mol. Biol. 1995, 25:311-317.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 311-317
    • Franciosa, H.1    Berge, J.B.2
  • 34
    • 44949283543 scopus 로고
    • Glutathione S-transferase isozymes in Aedes aegypti: purification, characterization, and isozyme-specific regulation
    • Grant D.F., Dietze E.C., Hammock B.D. Glutathione S-transferase isozymes in Aedes aegypti: purification, characterization, and isozyme-specific regulation. Insect Biochem. 1991, 21:421-433.
    • (1991) Insect Biochem. , vol.21 , pp. 421-433
    • Grant, D.F.1    Dietze, E.C.2    Hammock, B.D.3
  • 35
    • 0026784377 scopus 로고
    • Genetic and molecular evidence for a trans-acting regulatory locus controlling glutathione S-transferase-2 expression in Aedes aegypti
    • Grant D.F., Hammock B.D. Genetic and molecular evidence for a trans-acting regulatory locus controlling glutathione S-transferase-2 expression in Aedes aegypti. Mol. Gen. Genet. 1992, 234:169-176.
    • (1992) Mol. Gen. Genet. , vol.234 , pp. 169-176
    • Grant, D.F.1    Hammock, B.D.2
  • 36
    • 0016275313 scopus 로고
    • The glutathione S-transferases: the first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., Jakoby W.B. The glutathione S-transferases: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974, 249:7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 37
    • 0032874845 scopus 로고    scopus 로고
    • Glutatione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • Hayes J.D., McLellan L.I. Glutatione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic. Res. 1999, 4:273-300.
    • (1999) Free Radic. Res. , vol.4 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 38
    • 0003110983 scopus 로고
    • Role of glutathione transferase in drug resistance
    • Academic Press, London, H. Sies, B. Ketterer (Eds.)
    • Hayes J.D., Wolf C.R. Role of glutathione transferase in drug resistance. Glutathione Conjugation 1988, 315. Academic Press, London. H. Sies, B. Ketterer (Eds.).
    • (1988) Glutathione Conjugation , pp. 315
    • Hayes, J.D.1    Wolf, C.R.2
  • 39
    • 0026059473 scopus 로고
    • A possible novel link between organophosphorous and DDT insecticide resistance genes in Anopheles: supporting evidence from fenitrothion metabolism studies
    • Hemingway J., Miyamoto J., Herath P.R.J. A possible novel link between organophosphorous and DDT insecticide resistance genes in Anopheles: supporting evidence from fenitrothion metabolism studies. Pest. Biochem. Physiol. 1991, 39:49-56.
    • (1991) Pest. Biochem. Physiol. , vol.39 , pp. 49-56
    • Hemingway, J.1    Miyamoto, J.2    Herath, P.R.J.3
  • 40
    • 0034112744 scopus 로고    scopus 로고
    • Insecticide resistance in insect vectors of human disease
    • Hemingway J., Ranson H. Insecticide resistance in insect vectors of human disease. Annu. Rev. Entomol. 2000, 45:371-391.
    • (2000) Annu. Rev. Entomol. , vol.45 , pp. 371-391
    • Hemingway, J.1    Ranson, H.2
  • 41
  • 42
    • 0032168783 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella
    • Huang H.S., Hu N.T., Yao Y.E., Wu C.Y., Chiang S.W., et al. Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella. Insect Biochem. Mol. Biol. 1998, 28:651-658.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 651-658
    • Huang, H.S.1    Hu, N.T.2    Yao, Y.E.3    Wu, C.Y.4    Chiang, S.W.5
  • 43
    • 0033594963 scopus 로고    scopus 로고
    • Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target
    • Jakobsson P.J., Thoren S., Morgenstern R., Samuelsson B. Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc. Natl Acad. Sci. 1999, 96:7220-7225.
    • (1999) Proc. Natl Acad. Sci. , vol.96 , pp. 7220-7225
    • Jakobsson, P.J.1    Thoren, S.2    Morgenstern, R.3    Samuelsson, B.4
  • 44
    • 0029064985 scopus 로고
    • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods
    • Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J., et al. 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 1995, 34:5317-5328.
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.1    von Rosenvinge, E.C.2    Johnson, W.W.3    Tomarev, S.I.4    Piatigorsky, J.5
  • 45
    • 0035954627 scopus 로고    scopus 로고
    • Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene
    • Jirajaroenrat K., Pongjaroenkit S., Krittanai C., Prapanthadara L., Ketterman A.J. Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene. Insect Biochem. Mol. Biol. 2001, 31:867-875.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 867-875
    • Jirajaroenrat, K.1    Pongjaroenkit, S.2    Krittanai, C.3    Prapanthadara, L.4    Ketterman, A.J.5
  • 46
    • 0035185961 scopus 로고    scopus 로고
    • Single amino acid changes outside the active site significantly affect activity of glutathione S-transferases
    • Ketterman A.J., Prommeenate P., Boonchauy C., Chanama U., Leetachewa S., et al. Single amino acid changes outside the active site significantly affect activity of glutathione S-transferases. Insect Biochem. Mol. Biol. 2001, 31:65-74.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 65-74
    • Ketterman, A.J.1    Prommeenate, P.2    Boonchauy, C.3    Chanama, U.4    Leetachewa, S.5
  • 47
    • 0029168198 scopus 로고
    • Multiple mechanisms for enhancement of glutathione S-transferase activities in Spodoptera frugiperda (Lepidoptera: Noctuidae)
    • Kirby M.L., Ottea J.A. Multiple mechanisms for enhancement of glutathione S-transferase activities in Spodoptera frugiperda (Lepidoptera: Noctuidae). Insect Biochem. Mol. Biol. 1995, 25:347-353.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 347-353
    • Kirby, M.L.1    Ottea, J.A.2
  • 49
    • 0033805156 scopus 로고    scopus 로고
    • Mammalian class theta GST and differential susceptibility to carcinogens: a review
    • Landi S. Mammalian class theta GST and differential susceptibility to carcinogens: a review. Mutat. Res. 2000, 463:247-283.
    • (2000) Mutat. Res. , vol.463 , pp. 247-283
    • Landi, S.1
  • 50
    • 0033080845 scopus 로고    scopus 로고
    • Is the insect glutathione S-transferase I gene family intronless?
    • Lougarre A., Bride J.M., Fournier D. Is the insect glutathione S-transferase I gene family intronless?. Insect Mol. Biol. 1999, 8:141-143.
    • (1999) Insect Mol. Biol. , vol.8 , pp. 141-143
    • Lougarre, A.1    Bride, J.M.2    Fournier, D.3
  • 52
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • Mannervik B., Danielson U.H. Glutathione transferases-structure and catalytic activity. CRC Crit. Rev. Biochem. 1988, 23:283-337.
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 53
    • 0026033569 scopus 로고
    • Theta, a new class of glutathione transferases purified from rat and man
    • Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., et al. Theta, a new class of glutathione transferases purified from rat and man. Biochem. J. 1991, 274:409-414.
    • (1991) Biochem. J. , vol.274 , pp. 409-414
    • Meyer, D.J.1    Coles, B.2    Pemble, S.E.3    Gilmore, K.S.4    Fraser, G.M.5
  • 54
    • 0028871969 scopus 로고
    • Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase
    • Meyer D.J., Thomas M. Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase. Biochem. J. 1995, 311:739-742.
    • (1995) Biochem. J. , vol.311 , pp. 739-742
    • Meyer, D.J.1    Thomas, M.2
  • 55
    • 0034778978 scopus 로고    scopus 로고
    • The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B
    • Oakley A.J., Harnnoi T., Udomsinprasert R., Jirajaroenrat K., Ketterman A.J., et al. The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Protein Sci. 2001, 10:2176-2185.
    • (2001) Protein Sci. , vol.10 , pp. 2176-2185
    • Oakley, A.J.1    Harnnoi, T.2    Udomsinprasert, R.3    Jirajaroenrat, K.4    Ketterman, A.J.5
  • 56
    • 0018771271 scopus 로고
    • Glutathione S-transferases and hydrolytic activity in a tetrachlorovinphos-resistant strain of housefly and their influence on resistance Pestic
    • Oppenoorth F.J., Van der Pas L.J.T., Houx N.W.H. Glutathione S-transferases and hydrolytic activity in a tetrachlorovinphos-resistant strain of housefly and their influence on resistance Pestic. Biochem. Physiol. 1979, 11:176-188.
    • (1979) Biochem. Physiol. , vol.11 , pp. 176-188
    • Oppenoorth, F.J.1    Van der Pas, L.J.T.2    Houx, N.W.H.3
  • 57
    • 0042568971 scopus 로고    scopus 로고
    • Heterologous expression of four glutathione transferase genes genetically linked to a major insecticide resistance locus, from the malaria vector
    • Ortelli F., Rossiter L.C., Vontas J., Ranson H., Hemingway J. Heterologous expression of four glutathione transferase genes genetically linked to a major insecticide resistance locus, from the malaria vector. Anopheles gambiae Biochem. J. 2003, 373:957-963.
    • (2003) Anopheles gambiae Biochem. J. , vol.373 , pp. 957-963
    • Ortelli, F.1    Rossiter, L.C.2    Vontas, J.3    Ranson, H.4    Hemingway, J.5
  • 58
    • 0021151759 scopus 로고
    • Glutathione S-transferases in the house fly: biochemical and genetic changes associated with induction and insecticide resistance
    • Ottea J.A., Plapp F.W. Glutathione S-transferases in the house fly: biochemical and genetic changes associated with induction and insecticide resistance. Pest. Biochem. Physiol. 1984, 22:203-208.
    • (1984) Pest. Biochem. Physiol. , vol.22 , pp. 203-208
    • Ottea, J.A.1    Plapp, F.W.2
  • 59
    • 0026470986 scopus 로고
    • An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences
    • Pemble S.E., Taylor J.B. An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences. Biochem. J. 1992, 287:957-963.
    • (1992) Biochem. J. , vol.287 , pp. 957-963
    • Pemble, S.E.1    Taylor, J.B.2
  • 60
    • 0021203940 scopus 로고
    • The genetic basis of insecticide resistance in the housefly: evidence that a single locus plays a major role in metabolic resistance to insecticides
    • Plapp F.W. The genetic basis of insecticide resistance in the housefly: evidence that a single locus plays a major role in metabolic resistance to insecticides. Pest. Biochem. Physiol. 1984, 22:194-201.
    • (1984) Pest. Biochem. Physiol. , vol.22 , pp. 194-201
    • Plapp, F.W.1
  • 61
    • 0001621038 scopus 로고
    • Partial purification and characterization of glutathione S-transferases involved in DDT resistance from the mosquito Anopheles gambiae
    • Prapanthadara L., Hemingway J., Ketterman A.J. Partial purification and characterization of glutathione S-transferases involved in DDT resistance from the mosquito Anopheles gambiae. Pest. Biochem. Physiol. 1993, 47:119-133.
    • (1993) Pest. Biochem. Physiol. , vol.47 , pp. 119-133
    • Prapanthadara, L.1    Hemingway, J.2    Ketterman, A.J.3
  • 62
    • 84974056012 scopus 로고
    • DDT-resistance in Anopheles gambiae (Diptera: culicidae) from Zanzibar, Tanzania, based on increased DDT-deyhdrochlorinase activity of glutathione S-transferases
    • Prapanthadara L., Hemingway J., Ketterman A.J. DDT-resistance in Anopheles gambiae (Diptera: culicidae) from Zanzibar, Tanzania, based on increased DDT-deyhdrochlorinase activity of glutathione S-transferases. Bull. Ent. Res. 1995, 85:267-274.
    • (1995) Bull. Ent. Res. , vol.85 , pp. 267-274
    • Prapanthadara, L.1    Hemingway, J.2    Ketterman, A.J.3
  • 63
    • 0037020193 scopus 로고    scopus 로고
    • Evolution of supergene families associated with insecticide resistance
    • Ranson H., Claudianos C., Ortelli F., Abgrall C., Hemingway J., et al. Evolution of supergene families associated with insecticide resistance. Science 2002, 298:179-181.
    • (2002) Science , vol.298 , pp. 179-181
    • Ranson, H.1    Claudianos, C.2    Ortelli, F.3    Abgrall, C.4    Hemingway, J.5
  • 64
    • 0032564479 scopus 로고    scopus 로고
    • The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family
    • Ranson H., Collins F., Hemingway J. The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family. Proc. Natl Acad. Sci. USA 1998, 95:14284-14289.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14284-14289
    • Ranson, H.1    Collins, F.2    Hemingway, J.3
  • 65
    • 0033760462 scopus 로고    scopus 로고
    • Genetic mapping of two loci affecting DDT resistance in the malaria vector Anopheles gambiae
    • Ranson H., Jensen B., Wang X., Prapanthadara L., Hemingway J., et al. Genetic mapping of two loci affecting DDT resistance in the malaria vector Anopheles gambiae. Insect Mol. Biol. 2000, 9:499-507.
    • (2000) Insect Mol. Biol. , vol.9 , pp. 499-507
    • Ranson, H.1    Jensen, B.2    Wang, X.3    Prapanthadara, L.4    Hemingway, J.5
  • 66
    • 0030917474 scopus 로고    scopus 로고
    • Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae
    • Ranson H., Prapanthadara L., Hemingway J. Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae. Biochem. J. 1997, 324:97-102.
    • (1997) Biochem. J. , vol.324 , pp. 97-102
    • Ranson, H.1    Prapanthadara, L.2    Hemingway, J.3
  • 67
    • 0035887445 scopus 로고    scopus 로고
    • Identification of a novel class of insect glutathione S-transferases involved in resistance to DDT in the malaria vector Anopheles gambiae
    • Ranson H., Rossiter L., Ortelli F., Jensen B., Wang X., et al. Identification of a novel class of insect glutathione S-transferases involved in resistance to DDT in the malaria vector Anopheles gambiae. Biochem. J. 2001, 359:295-304.
    • (2001) Biochem. J. , vol.359 , pp. 295-304
    • Ranson, H.1    Rossiter, L.2    Ortelli, F.3    Jensen, B.4    Wang, X.5
  • 68
    • 0027898499 scopus 로고
    • A glutathione S-transferase gene of the vector mosquito, Anopheles gambiae
    • Reiss R.A., James A.A. A glutathione S-transferase gene of the vector mosquito, Anopheles gambiae. Insect Mol. Biol. 1993, 2:25-32.
    • (1993) Insect Mol. Biol. , vol.2 , pp. 25-32
    • Reiss, R.A.1    James, A.A.2
  • 69
    • 0033153407 scopus 로고    scopus 로고
    • An olfactory-specific glutathione-S-transferase in the sphinx moth Manduca sexta
    • Rogers M.E., Jani M.K., Vogt R.G. An olfactory-specific glutathione-S-transferase in the sphinx moth Manduca sexta. J. Exp. Biol. 1999, 202(Pt 12):1625-1637.
    • (1999) J. Exp. Biol. , vol.202 , pp. 1625-1637
    • Rogers, M.E.1    Jani, M.K.2    Vogt, R.G.3
  • 70
    • 0027300033 scopus 로고
    • Glutathione S-transferases, structure, regulation, and therapeutic implications
    • Rushmore T.H., Pickett C.B. Glutathione S-transferases, structure, regulation, and therapeutic implications. J. Biol. Chem. 1993, 268:11475-11478.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11475-11478
    • Rushmore, T.H.1    Pickett, C.B.2
  • 71
    • 0035543643 scopus 로고    scopus 로고
    • Overproduction of a P450 that metabolizes diazinon is linked to a loss-of-function in the chromosome 2 ali-esterase (MdalphaE7) gene in resistant house flies
    • Sabourault C., Guzov V.M., Koener J.F., Claudianos C., Plapp F.W., et al. Overproduction of a P450 that metabolizes diazinon is linked to a loss-of-function in the chromosome 2 ali-esterase (MdalphaE7) gene in resistant house flies. Insect Mol. Biol. 2001, 10:609-618.
    • (2001) Insect Mol. Biol. , vol.10 , pp. 609-618
    • Sabourault, C.1    Guzov, V.M.2    Koener, J.F.3    Claudianos, C.4    Plapp, F.W.5
  • 72
    • 0037337927 scopus 로고    scopus 로고
    • 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
    • Sawicki R., Singh S.P., Mondal A.K., Benes H., Zimniak P. 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. 2003, 370:661-669.
    • (2003) Biochem. J. , vol.370 , pp. 661-669
    • Sawicki, R.1    Singh, S.P.2    Mondal, A.K.3    Benes, H.4    Zimniak, P.5
  • 73
    • 0033617247 scopus 로고    scopus 로고
    • The projection structure of the membrane protein microsomal glutathione transferase at 3 A resolution as determined from two-dimensional hexagonal crystals
    • Schmidt-Krey I., Murata K., Hirai T., Mitsuoka K., Cheng Y., et al. The projection structure of the membrane protein microsomal glutathione transferase at 3 A resolution as determined from two-dimensional hexagonal crystals. J. Mol. Biol. 1999, 288:243-253.
    • (1999) J. Mol. Biol. , vol.288 , pp. 243-253
    • Schmidt-Krey, I.1    Murata, K.2    Hirai, T.3    Mitsuoka, K.4    Cheng, Y.5
  • 74
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., Dowd C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 2001, 360:1-16.
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 75
    • 0034833919 scopus 로고    scopus 로고
    • Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products
    • Singh S.P., Coronella J.A., Benes H., Cochrane B.J., Zimniak P. Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products. Eur. J. Biochem. 2001, 268:2912-2923.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2912-2923
    • Singh, S.P.1    Coronella, J.A.2    Benes, H.3    Cochrane, B.J.4    Zimniak, P.5
  • 76
    • 0034682035 scopus 로고    scopus 로고
    • Cloning and characterization of a new theta-class glutathione-S-transferase (GST) gene, gst-3, from Drosophila melanogaster
    • Singh M., Silva E., Schulze S., Sinclair D.A., Fitzpatrick K.A., et al. Cloning and characterization of a new theta-class glutathione-S-transferase (GST) gene, gst-3, from Drosophila melanogaster. Gene 2000, 247:167-173.
    • (2000) Gene , vol.247 , pp. 167-173
    • Singh, M.1    Silva, E.2    Schulze, S.3    Sinclair, D.A.4    Fitzpatrick, K.A.5
  • 77
    • 0029278802 scopus 로고
    • Glutathione S-transferases from larval Manduca sexta midgut: sequence of two cDNAs and enzyme induction
    • Snyder M.J., Walding J.K., Feyereisen R. Glutathione S-transferases from larval Manduca sexta midgut: sequence of two cDNAs and enzyme induction. Insect Biochem. Mol. Biol. 1995, 25:455-465.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 455-465
    • Snyder, M.J.1    Walding, J.K.2    Feyereisen, R.3
  • 78
    • 0035189168 scopus 로고    scopus 로고
    • Structural analysis and antibody response to the extracellular glutathione S-transferases from Onchocerca volvulus
    • Sommer A., Nimtz M., Conradt H.S., Brattig N., Boettcher K., et al. Structural analysis and antibody response to the extracellular glutathione S-transferases from Onchocerca volvulus. Infect. Immun. 2001, 69:7718-7728.
    • (2001) Infect. Immun. , vol.69 , pp. 7718-7728
    • Sommer, A.1    Nimtz, M.2    Conradt, H.S.3    Brattig, N.4    Boettcher, K.5
  • 79
    • 0028089884 scopus 로고
    • Glutathione transferase gene family from the housefly Musca domestica
    • Syvanen M., Zhou Z.H., Wang J.Y. Glutathione transferase gene family from the housefly Musca domestica. Mol. Gen. Genet. 1994, 245:25-31.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 25-31
    • Syvanen, M.1    Zhou, Z.H.2    Wang, J.Y.3
  • 80
    • 0028112999 scopus 로고
    • Biochemical characterization of Drosophila glutathione S-transferases D1 and D21
    • Tang A.H., Tu C.P Biochemical characterization of Drosophila glutathione S-transferases D1 and D21. J. Biol. Chem. 1994, 269:27876-27884.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27876-27884
    • Tang, A.H.1    Tu, C.P.2
  • 81
    • 0029054158 scopus 로고
    • Pentobarbital-induced changes in Drosophila glutathione S-transferase D21 mRNA stability
    • Tang A.H., Tu C.P. Pentobarbital-induced changes in Drosophila glutathione S-transferase D21 mRNA stability. J. Biol. Chem. 1995, 270:13819-13825.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13819-13825
    • Tang, A.H.1    Tu, C.P.2
  • 82
    • 0006257343 scopus 로고
    • Purification and characterization of glutathione transferases of Eorenma loftini and Diatraea sacohara (Lepidoptera: Pyralidae)
    • Tiwari N.K., Singhai S.S., Sharma R., Meagher R.L., Awasthi Y.C. Purification and characterization of glutathione transferases of Eorenma loftini and Diatraea sacohara (Lepidoptera: Pyralidae). J. Econ. Entomol. 1991, 84:1424-1432.
    • (1991) J. Econ. Entomol. , vol.84 , pp. 1424-1432
    • Tiwari, N.K.1    Singhai, S.S.2    Sharma, R.3    Meagher, R.L.4    Awasthi, Y.C.5
  • 83
    • 0034622645 scopus 로고    scopus 로고
    • Disruption of the microsomal glutathione S-transferase-like gene reduces life span of Drosophila melanogaster
    • Toba G., Aigaki T. Disruption of the microsomal glutathione S-transferase-like gene reduces life span of Drosophila melanogaster. Gene 2000, 253:179-187.
    • (2000) Gene , vol.253 , pp. 179-187
    • Toba, G.1    Aigaki, T.2
  • 84
    • 0025021987 scopus 로고
    • Drosophila glutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III
    • Toung Y.P., Hsieh T.S., Tu C.P. Drosophila glutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III. Proc. Natl Acad. Sci. USA 1990, 87:31-35.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 31-35
    • Toung, Y.P.1    Hsieh, T.S.2    Tu, C.P.3
  • 85
    • 0027211012 scopus 로고
    • The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster
    • Toung Y.P., Hsieh T.S., Tu C.P. The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster. J. Biol. Chem. 1993, 268:9737-9746.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9737-9746
    • Toung, Y.P.1    Hsieh, T.S.2    Tu, C.P.3
  • 86
    • 0036009123 scopus 로고    scopus 로고
    • Expression and characterization of a novel class of glutathione S-transferase from Anopheles dirus
    • Udomsinprasert R., Ketterman A.J. Expression and characterization of a novel class of glutathione S-transferase from Anopheles dirus. Insect Biochem. Mol. Biol. 2002, 32:425-433.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 425-433
    • Udomsinprasert, R.1    Ketterman, A.J.2
  • 87
    • 0035397391 scopus 로고    scopus 로고
    • Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens
    • Vontas J.G., Small G.J., Hemingway J. Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens. Biochem. J. 2001, 357:65-72.
    • (2001) Biochem. J. , vol.357 , pp. 65-72
    • Vontas, J.G.1    Small, G.J.2    Hemingway, J.3
  • 88
    • 0036499691 scopus 로고    scopus 로고
    • Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the rice brown planthopper, Nilaparvata lugens
    • Vontas J.G., Small G.J., Nikou D.C., Ranson H., Hemingway J. Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the rice brown planthopper, Nilaparvata lugens. Biochem. J. 2002, 362:329-337.
    • (2002) Biochem. J. , vol.362 , pp. 329-337
    • Vontas, J.G.1    Small, G.J.2    Nikou, D.C.3    Ranson, H.4    Hemingway, J.5
  • 89
    • 0035983888 scopus 로고    scopus 로고
    • Probing the diversity of the Arabidopsis glutathione S-transferase gene family
    • Wagner U., Edwards R., Dixon D.P., Mauch F. Probing the diversity of the Arabidopsis glutathione S-transferase gene family. Plant Mol. Biol. 2002, 49:515-532.
    • (2002) Plant Mol. Biol. , vol.49 , pp. 515-532
    • Wagner, U.1    Edwards, R.2    Dixon, D.P.3    Mauch, F.4
  • 90
    • 0025864722 scopus 로고
    • Molecular cloning of a glutathione S-transferase overproduced in an insecticide-resistant strain of the housefly (Musca domestica)
    • Wang J.Y., McCommas S., Syvanen M. Molecular cloning of a glutathione S-transferase overproduced in an insecticide-resistant strain of the housefly (Musca domestica). Mol. Gen. Genet. 1991, 227:260-266.
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 260-266
    • Wang, J.Y.1    McCommas, S.2    Syvanen, M.3
  • 91
    • 0035499462 scopus 로고    scopus 로고
    • Identification and cloning of a key insecticide-metabolizing glutathione S-transferase (MdGST-6A) from a hyper insecticide-resistant strain of the housefly Musca domestica
    • Wei S.H., Clark A.G., Syvanen M. Identification and cloning of a key insecticide-metabolizing glutathione S-transferase (MdGST-6A) from a hyper insecticide-resistant strain of the housefly Musca domestica. Insect Biochem. Mol. Biol. 2001, 31:1145-1153.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 1145-1153
    • Wei, S.H.1    Clark, A.G.2    Syvanen, M.3
  • 92
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • Wilce M.C., Board P.G., Feil S.C., Parker M.W. Crystal structure of a theta-class glutathione transferase. EMBO J. 1995, 14:2133-2143.
    • (1995) EMBO J. , vol.14 , pp. 2133-2143
    • Wilce, M.C.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 93
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce M.C., Parker M.W. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1994, 1205:1-18.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.1    Parker, M.W.2
  • 94
    • 0022463716 scopus 로고
    • Distribution and properties of glutathione S-transferases from T. infestans
    • Wood E., Casabe N., Melgar F., Zebra E. Distribution and properties of glutathione S-transferases from T. infestans. Comp. Biochem. Physiol. 1986, 84:607-617.
    • (1986) Comp. Biochem. Physiol. , vol.84 , pp. 607-617
    • Wood, E.1    Casabe, N.2    Melgar, F.3    Zebra, E.4
  • 95
    • 0035919812 scopus 로고    scopus 로고
    • Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases
    • Xia B., Vlamis-Gardikas A., Holmgren A., Wright P.E., Dyson H.J. Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases. J. Mol. Biol. 2001, 310:907-918.
    • (2001) J. Mol. Biol. , vol.310 , pp. 907-918
    • Xia, B.1    Vlamis-Gardikas, A.2    Holmgren, A.3    Wright, P.E.4    Dyson, H.J.5
  • 96
    • 0021214199 scopus 로고
    • Interactions of allelochemicals with detoxication enzymes of insecticide-susceptible and resistant fall army-worms
    • Yu S.J. Interactions of allelochemicals with detoxication enzymes of insecticide-susceptible and resistant fall army-worms. Pestic. Biochem. Physiol. 1984, 22:60-68.
    • (1984) Pestic. Biochem. Physiol. , vol.22 , pp. 60-68
    • Yu, S.J.1
  • 97
    • 22944473357 scopus 로고    scopus 로고
    • Insect glutathione S-transferases
    • Yu S.J. Insect glutathione S-transferases. Zool. Stud. 1996, 35:9-19.
    • (1996) Zool. Stud. , vol.35 , pp. 9-19
    • Yu, S.J.1
  • 98
    • 0030695430 scopus 로고    scopus 로고
    • A complex glutathione transferase gene family in the housefly Musca domestica
    • Zhou Z.H., Syvanen M. A complex glutathione transferase gene family in the housefly Musca domestica. Mol. Gen. Genet. 1997, 256:187-194.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 187-194
    • Zhou, Z.H.1    Syvanen, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.