메뉴 건너뛰기




Volumn 43, Issue 2, 2011, Pages 253-265

Insect glutathione transferases

Author keywords

delta class; epsilon class; glutathione transferase (GST); insecticide resistance; nomenclature; Review; structure function; superfamily

Indexed keywords

GLUTATHIONE TRANSFERASE;

EID: 79954605843     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.3109/03602532.2011.552911     Document Type: Review
Times cited : (143)

References (91)
  • 1
    • 0031045777 scopus 로고    scopus 로고
    • Identification of an N-capping box that affects the α6-helix propensity in glutathione S-transferase superfamily proteins: A role for an invariant aspartic residue
    • Aceto, A., Dragani, B., Melino, S., Allocati, N., Masulli, M., Di Ilio, C., et al. (1997). Identifcation of an N-capping box that afects the a6-helix propensity in glutathione S-transferase superfamily proteins: a role for an invariant aspartic residue. Biochem J 322:229-234. (Pubitemid 27095545)
    • (1997) Biochemical Journal , vol.322 , Issue.1 , pp. 229-234
    • Aceto, A.1    Dragani, B.2    Melino, S.3    Allocati, N.4    Masulli, M.5    Di Ilio, C.6    Petruzzelli, R.7
  • 4
    • 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
    • DOI 10.1016/S0022-2836(02)01327-X
    • Agianian, B., Tucker, P. A., Schouten, A., Leonard, K., Bullard, B., Gros, P. (2003). Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products. J Mol Biol 326:151-165. (Pubitemid 36279365)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.1 , pp. 151-165
    • Agianian, B.1    Tucker, P.A.2    Schouten, A.3    Leonard, K.4    Bullard, B.5    Gros, P.6
  • 5
    • 0017187771 scopus 로고
    • Nonoxidative enzymes in the metabolism of insecticides
    • Ahmad, S., Forgash, A. J. (1976). Nonoxidative enzymes in the metabolism of insecticides. Drug Metab Rev 5:141-164.
    • (1976) Drug Metab Rev , vol.5 , pp. 141-164
    • Ahmad, S.1    Forgash, A.J.2
  • 6
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • DOI 10.1021/tx960072x
    • Armstrong, R. N. (1997). Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 10:2-18. (Pubitemid 27044902)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.1 , pp. 2-18
    • Armstrong, R.N.1
  • 7
    • 33845883023 scopus 로고    scopus 로고
    • Paleontological evidence to date the tree of life
    • DOI 10.1093/molbev/msl150
    • Benton, M. J., Donoghue, P. C. (2007). Paleontological evidence to date the tree of life. Mol Biol Evol 24:26-53. (Pubitemid 46026279)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.1 , pp. 26-53
    • Benton, M.J.1    Donoghue, P.C.J.2
  • 8
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board, P., Baker, R. T., Chelvanayagam, G., Jermiin, L. S. (1997). Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J 328:929-935. (Pubitemid 28005795)
    • (1997) Biochemical Journal , vol.328 , Issue.3 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 9
    • 0014624712 scopus 로고
    • Glutathione S-aralkyltransferase
    • Boyland, E., Chasseaud, L. F. (1969). Glutathione S-aralkyltransferase. Biochem J 115:985-991.
    • (1969) Biochem J , vol.115 , pp. 985-991
    • Boyland, E.1    Chasseaud, L.F.2
  • 10
    • 0342840693 scopus 로고
    • An enzyme catalysing the conjugation of epoxides with glutathione
    • Boyland, E., Williams, K. (1965). An enzyme catalysing the conjugation of epoxides with glutathione. Biochem J 94:190-197.
    • (1965) Biochem J , vol.94 , pp. 190-197
    • Boyland, E.1    Williams, K.2
  • 11
    • 0022732736 scopus 로고
    • Insecticide resistance in mosquitoes: A pragmatic review
    • Brown, A. W. A. (1986). Insecticide resistance in mosquitoes: a pragmatic review. J Am Mosq Control Assoc 2:123-140.
    • (1986) J Am Mosq Control Assoc , vol.2 , pp. 123-140
    • Brown, A.W.A.1
  • 13
    • 0000104664 scopus 로고    scopus 로고
    • Fly fishing for GSTs: A unified nomenclature for mammalian and insect glutathione transferases
    • PII S0009279700002167
    • Chelvanayagam, G., Parker, M. W., Board, P. G. (2001). Fly fshing for GSTs: a unifed nomenclature for mammalian and insect glutathione transferases. Chem Biol Interact 133:256-260. (Pubitemid 33591397)
    • (2001) Chemico-Biological Interactions , vol.133 , Issue.1-3 , pp. 256-260
    • Chelvanayagama, G.1    Parker, M.W.2    Board, P.G.3
  • 14
    • 0346432074 scopus 로고    scopus 로고
    • Structure of an insect δ-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae
    • DOI 10.1107/S0907444903018493
    • Chen, L., Hall, P. R., Zhou, X. E., Ranson, H., Hemingway, J., Meehan, E. J. (2003). Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae. Acta Crystallogr D Biol Crystallogr 59:2211-2217. (Pubitemid 38024855)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.12 , pp. 2211-2217
    • Chen, L.1    Hall, P.R.2    Zhou, X.E.3    Ranson, H.4    Hemingway, J.5    Meehan, E.J.6
  • 15
    • 0014078604 scopus 로고
    • Species diferences in the inhibition of glutathione S-aryltransferase by phthaleins and dicarboxylic acids
    • Clark, A. G., Darby, F. J., Smith, J. N. (1967). Species diferences in the inhibition of glutathione S-aryltransferase by phthaleins and dicarboxylic acids. Biochem J 103:49-54.
    • (1967) Biochem J , vol.103 , pp. 49-54
    • Clark, A.G.1    Darby, F.J.2    Smith, J.N.3
  • 16
    • 0000903828 scopus 로고
    • The characterization by afnity chromatography of glutathione S-transferases from diferent strains of house fy
    • Clark, A. G., Dauterman, W. C. (1982). The characterization by afnity chromatography of glutathione S-transferases from diferent strains of house fy. Pestic Biochem Physiol 17:307-314.
    • (1982) Pestic Biochem Physiol , vol.17 , pp. 307-314
    • Clark, A.G.1    Dauterman, W.C.2
  • 17
    • 0003063265 scopus 로고
    • Glutathione S-transferases from the New Zealand grass grub, Costelytra zealandica. Teir isolation and characterization and the efect on their activity of endogenous factors
    • Clark, A. G., Dick, G. L., Martindale, S. M., Smith, J. N. (1985). Glutathione S-transferases from the New Zealand grass grub, Costelytra zealandica. Teir isolation and characterization and the efect on their activity of endogenous factors. Insect Biochem 15:35-44.
    • (1985) Insect Biochem , vol.15 , pp. 35-44
    • Clark, A.G.1    Dick, G.L.2    Martindale, S.M.3    Smith, J.N.4
  • 18
    • 0021738417 scopus 로고
    • Evidence that DDT-dehydrochlorinase from the house fly is a glutathione S-transferase
    • DOI 10.1016/0048-3575(84)90018-X
    • Clark, A. G., Shamaan, N. A. (1984). Evidence that DDT-dehydrochlorinase from the house fy is a glutathione S-transferase. Pestic Biochem Physiol 22:249-261. (Pubitemid 15220071)
    • (1984) Pesticide Biochemistry and Physiology , vol.22 , Issue.3 , pp. 249-261
    • Clark, A.G.1    Shamaan, N.A.2
  • 19
    • 0021132402 scopus 로고
    • Characterization of multiple glutathione transferases from the house fly, Musca domestica (L)
    • Clark, A. G., Shamaan, N. A., Dauterman, W. C., Hayaoka, T. (1984). Characterization of multiple glutathione transferases from the house fy, Musca domestica (L). Pestic Biochem Physiol 22:51-59. (Pubitemid 14027078)
    • (1984) Pesticide Biochemistry and Physiology , vol.22 , Issue.1 , pp. 51-59
    • Clark, A.G.1    Shamaan, N.A.2    Dauterman, C.3    Hayaoka, T.4
  • 20
    • 0022599357 scopus 로고
    • Insecticide metabolism by multiple glutathione S-transferases in two strains of the house fly, Musca domestica (L)
    • Clark, A. G., Shamaan, N. A., Sinclair, M. D., Dauterman, W. C. (1986). Insecticide metabolism by multiple glutathione S-transferases in two strains of the house fy, Musca domestica (L). Pestic Biochem Physiol 25:169-175. (Pubitemid 16131542)
    • (1986) Pesticide Biochemistry and Physiology , vol.25 , Issue.2 , pp. 169-175
    • Clark, A.G.1    Shamaan, N.A.2    Sinclair, M.D.3    Dauterman, W.C.4
  • 21
    • 0015860902 scopus 로고
    • Cross-specifcity in some vertebrate and insect glutathione transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitro-benzene and S-crotonyl-N-acetylcysteamine as substrates
    • Clark, A. G., Smith, J. N., and Speir, T. W. (1973). Cross-specifcity in some vertebrate and insect glutathione transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitro-benzene and S-crotonyl-N-acetylcysteamine as substrates. Biochem J 135:385-392.
    • (1973) Biochem J , vol.135 , pp. 385-392
    • Clark, A.G.1    Smith, J.N.2    Speir, T.W.3
  • 23
    • 9144243812 scopus 로고    scopus 로고
    • The Anopheles gambiae glutathione transferase supergene family: Annotation, phylogeny, and expression profles
    • Ding, Y., Ortelli, F., Rossiter, L. C., Hemingway, J., Ranson, H. (2003). The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny, and expression profles. BMC Genomics 4:35-50.
    • (2003) BMC Genomics , vol.4 , pp. 35-50
    • Ding, Y.1    Ortelli, F.2    Rossiter, L.C.3    Hemingway, J.4    Ranson, H.5
  • 24
    • 0030824202 scopus 로고    scopus 로고
    • The conserved N-capping box in the hydrophobic core of glutathione S- transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability
    • DOI 10.1074/jbc.272.41.25518
    • Dragani, B., Stenberg, G., Melino, S., Petruzzelli, R., Mannervik, B., Aceto, A. (1997). The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identifcation of a buried and conserved hydrogen bond important for protein stability. J Biol Chem 272:25518-25523. (Pubitemid 27438859)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25518-25523
    • Dragani, B.1    Stenberg, G.2    Melino, S.3    Petruzzelli, R.4    Mannervik, B.5    Aceto, A.6
  • 25
    • 0029008992 scopus 로고
    • Native dimer stabilizes the subunit tertiary structure of porcine class pi glutathione S-transferase
    • Erhardt, J., Dirr, H. (1995). Native dimer stabilizes the subunit tertiary structure of porcine class pi glutathione S-transferase. Eur J Biochem 230:614-620.
    • (1995) Eur J Biochem , vol.230 , pp. 614-620
    • Erhardt, J.1    Dirr, H.2
  • 26
    • 0026575011 scopus 로고
    • Insect glutathione S-transferases. Biochemical characteristics of the major forms from housefies susceptible and resistant to insecticides
    • Fournier, D., Bride, J.-M., Poirié, M., Bergé, J.-B., Plapp, F. W. (1992). Insect glutathione S-transferases. Biochemical characteristics of the major forms from housefies susceptible and resistant to insecticides. J Biol Chem 267:1840-1845.
    • (1992) J Biol Chem , vol.267 , pp. 1840-1845
    • Fournier, D.1    Bride, J.-M.2    Poirié, M.3    Bergé, J.-B.4    Plapp, F.W.5
  • 27
    • 0014790785 scopus 로고
    • The separation of multiple forms of housefy 1,1,1-trichloro-2,2-bis-(p- chlorophenyl)ethane (DDT) dehydrochlorinase from glutathione S-aryltransferase by electrofocusing and electrophoresis
    • Goodchild, B., Smith, J. N. (1970). The separation of multiple forms of housefy 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) dehydrochlorinase from glutathione S-aryltransferase by electrofocusing and electrophoresis. Biochem J 117:1005-1009.
    • (1970) Biochem J , vol.117 , pp. 1005-1009
    • Goodchild, B.1    Smith, J.N.2
  • 29
    • 0034112744 scopus 로고    scopus 로고
    • Insecticide resistance in insect vectors of human disease
    • DOI 10.1146/annurev.ento.45.1.371
    • Hemingway, J., Ranson, H. (2000). Insecticide resistance in insect vectors of human disease. Annu Rev Entomol 45:371-391. (Pubitemid 30187866)
    • (2000) Annual Review of Entomology , vol.45 , pp. 371-391
    • Hemingway, J.1    Ranson, H.2
  • 30
    • 2242443511 scopus 로고    scopus 로고
    • Molecular recognition at the dimer interface of a class Mu glutathione transferase: Role of a hydrophobic interaction motif in dimer stability and protein function
    • DOI 10.1021/bi020548d
    • Hornby, J. A. T., Codreanu, S. G., Armstrong, R. N., Dirr, H. W. (2002). Molecular recognition at the dimer interface of a class mu glutathione transferase: role of a hydrophobic interaction motif in dimer stability and protein function. Biochemistry 41:14238-14247. (Pubitemid 35403343)
    • (2002) Biochemistry , vol.41 , Issue.48 , pp. 14238-14247
    • Hornby, J.A.T.1    Codreanu, S.G.2    Armstrong, R.N.3    Dirr, H.W.4
  • 31
    • 0034633885 scopus 로고    scopus 로고
    • Equilibrium folding of dimeric class m glutathione transferases involves a stable monomeric intermediate
    • Hornby, J. A. T., Luo, J.-K., Stevens, J. M., Wallace, L. A., Kaplan, W., Armstrong, R. N., et al. (2000). Equilibrium folding of dimeric class m glutathione transferases involves a stable monomeric intermediate. Biochemistry 39:12336-12344.
    • (2000) Biochemistry , vol.39 , pp. 12336-12344
    • Hornby, J.A.T.1    Luo, J.-K.2    Stevens, J.M.3    Wallace, L.A.4    Kaplan, W.5    Armstrong, R.N.6
  • 32
    • 0026460365 scopus 로고
    • The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-Å resolution
    • Ji, X., Zhang, P., Armstrong, R. N., Gilliland, G. L. (1992). The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-Å resolution. Biochemistry 31:10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 33
    • 0035954627 scopus 로고    scopus 로고
    • Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene
    • DOI 10.1016/S0965-1748(01)00032-7, PII S0965174801000327
    • Jirajaroenrat, K., Pongjaroenkit, S., Krittanai, C., Prapanthadara, L., Ketterman, A. J. (2001). Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene. Insect Biochem Molec Biol 31:867-875. (Pubitemid 32666594)
    • (2001) Insect Biochemistry and Molecular Biology , vol.31 , Issue.9 , pp. 867-875
    • Jirajaroenrat, K.1    Pongjaroenkit, S.2    Krittanai, C.3    Prapanthadara, L.-A.4    Ketterman, A.J.5
  • 34
    • 33748755738 scopus 로고    scopus 로고
    • Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the Omega class glutathione S-transferases
    • DOI 10.1042/BJ20060424
    • Kim, J., Suh, H., Kim, S., Kim, K., Ahn, C., Yim, J. (2006). Identification and characteristics of the structural gene for the Drosophila eye color mutant sepia, encoding PDA synthase, a member of the omega class glutathione S-transferases. Biochem J 398:451-460. (Pubitemid 44453389)
    • (2006) Biochemical Journal , vol.398 , Issue.3 , pp. 451-460
    • Kim, J.1    Suh, H.2    Kim, S.3    Kim, K.4    Ahn, C.5    Yim, J.6
  • 37
    • 50149107613 scopus 로고    scopus 로고
    • Expression of glutathione S-transferase (GST) genes in the marine copepod Tigriopus japonicus exposed to trace metals
    • Lee, K. W., Raisuddin, S., Rhee, J. S., Hwang, D. S., Yu, I. T., Lee, Y. M., et al. (2008). Expression of glutathione S-transferase (GST) genes in the marine copepod Tigriopus japonicus exposed to trace metals. Aquat Toxicol 89:158-166.
    • (2008) Aquat Toxicol , vol.89 , pp. 158-166
    • Lee, K.W.1    Raisuddin, S.2    Rhee, J.S.3    Hwang, D.S.4    Yu, I.T.5    Lee, Y.M.6
  • 38
    • 33846401539 scopus 로고    scopus 로고
    • Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics
    • DOI 10.1146/annurev.ento.51.110104.151104
    • Li, X., Schuler, M. A., Berenbaum, M. R. (2007). Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics. Annu Rev Entomol 52:231-253. (Pubitemid 46133570)
    • (2007) Annual Review of Entomology , vol.52 , pp. 231-253
    • Li, X.1    Schuler, M.A.2    Berenbaum, M.R.3
  • 39
    • 0001242332 scopus 로고
    • DDT dehydrochlorinase. I. Isolation, chemical properties, and spectrophotometric assay
    • Lipke, H., Kearns, C. W. (1959a). DDT dehydrochlorinase. I. Isolation, chemical properties, and spectrophotometric assay. J Biol Chem 234:2123-2128.
    • (1959) J Biol Chem , vol.234 , pp. 2123-2128
    • Lipke, H.1    Kearns, C.W.2
  • 40
    • 9244235850 scopus 로고
    • DDT dehydrochlorinase. II. Substrate and cofactor specifcity
    • Lipke, H., Kearns, C. W. (1959b). DDT dehydrochlorinase. II. Substrate and cofactor specifcity. J Biol Chem 234:2129-2132.
    • (1959) J Biol Chem , vol.234 , pp. 2129-2132
    • Lipke, H.1    Kearns, C.W.2
  • 41
    • 0024265036 scopus 로고
    • Intracellular binding and transport of hormones and xenobiotics by glutathione-S-transferases
    • Listowsky, I., Abramovitz, M., Homma, H., Niitsu, Y. (1988). Intracellular binding and transport of hormones and xenobiotics by glutathione-S-transferases. Drug Metab Rev 19:305-318. (Pubitemid 19043739)
    • (1988) Drug Metabolism Reviews , vol.19 , Issue.3-4 , pp. 305-318
    • Listowsky, I.1    Abramovitz, M.2    Homma, H.3    Niitsu, Y.4
  • 42
    • 0028842236 scopus 로고
    • Site-directed mutatgenesis of human glutathione transferase P1-1. Spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants
    • Lo Bello, M., Battistoni, A., Mazzetti, A. P., Board, P. G., Muramatsu, M., Federici, G., et al. (1995). Site-directed mutatgenesis of human glutathione transferase P1-1. Spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants. J Biol Chem 270:1249-1253.
    • (1995) J Biol Chem , vol.270 , pp. 1249-1253
    • Lo Bello, M.1    Battistoni, A.2    Mazzetti, A.P.3    Board, P.G.4    Muramatsu, M.5    Federici, G.6
  • 44
    • 77954760855 scopus 로고    scopus 로고
    • Recognition and Detoxifcation of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1
    • Low, W. Y., Feil, S. C., Ng, H. L., Gorman, M. A., Morton, C. J., Pyke, J., et al. (2010). Recognition and Detoxifcation of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1. J Mol Biol 399:358-366.
    • (2010) J Mol Biol , vol.399 , pp. 358-366
    • Low, W.Y.1    Feil, S.C.2    Ng, H.L.3    Gorman, M.A.4    Morton, C.J.5    Pyke, J.6
  • 45
    • 0003139854 scopus 로고    scopus 로고
    • Equilibrium unfolding and enzyme kinetics of chimeric mu class glutathione transferases
    • Luo, J.-K., Hornby, J. A. T., Armstrong, R. N., Dirr, H. W. (2001). Equilibrium unfolding and enzyme kinetics of chimeric mu class glutathione transferases. Chem Biol Interact 133:58-59.
    • (2001) Chem Biol Interact , vol.133 , pp. 58-59
    • Luo, J.-K.1    Hornby, J.A.T.2    Armstrong, R.N.3    Dirr, H.W.4
  • 46
    • 0036708004 scopus 로고    scopus 로고
    • Impact of domain interchange on conformational stability and equilibrium folding of chimeric class μ glutathione transferases
    • DOI 10.1110/ps.0208002
    • Luo, J.-K., Hornby, J. A. T., Wallace, L. A., Chen, J., Armstrong, R. N., Dirr, H. W. (2002). Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases. Prot Sci 11:2208-2217. (Pubitemid 34919624)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2208-2217
    • Luo, J.-K.1    Hornby, J.A.T.2    Wallace, L.A.3    Chen, J.4    Armstrong, R.N.5    Dirr, H.W.6
  • 48
    • 30144439026 scopus 로고    scopus 로고
    • Nomenclature for mammalian soluble glutathione transferases
    • DOI 10.1016/S0076-6879(05)01001-3, PII S0076687905010013, 1, Gluthione Transferases and Gamma-Glutamyl Transpeptidases
    • Mannervik, B., Board, P. G., Hayes, J. D., Listowsky, I., Pearson, W. R. (2005). Nomenclature for mammalian soluble glutathione transferases. Meth Enzymol 401:1-8. (Pubitemid 43052383)
    • (2005) Methods in Enzymology , vol.401 , pp. 1-8
    • Mannervik, B.1    Board, P.G.2    Hayes, J.D.3    Listowsky, I.4    Pearson, W.R.5
  • 49
    • 0024222079 scopus 로고
    • How many species are there on earth?
    • May, R. M. (1988). How many species are there on Earth? Science 241:1441-1449. (Pubitemid 19320384)
    • (1988) Science , vol.241 , Issue.4872 , pp. 1441-1449
    • May, R.M.1
  • 50
    • 0016817561 scopus 로고
    • Interstrain comparison of glutathione-dependent reactions in susceptible and resistant housefies
    • Motoyama, N., Dauterman, W. C. (1975). Interstrain comparison of glutathione-dependent reactions in susceptible and resistant housefies. Pestic Biochem Physiol 5:489-495.
    • (1975) Pestic Biochem Physiol , vol.5 , pp. 489-495
    • Motoyama, N.1    Dauterman, W.C.2
  • 51
    • 0037171817 scopus 로고    scopus 로고
    • Low host specificity of herbivorous insects in a tropical forest
    • DOI 10.1038/416841a
    • Novotny, V., Basset, Y., Miller, S. E., Weiblen, G. D., Bremer, B., Cizek, L., et al. (2002). Low host specifcity of herbivorous insects in a tropical forest. Nature 416:841-844. (Pubitemid 34453738)
    • (2002) Nature , vol.416 , Issue.6883 , pp. 841-844
    • Novotny, V.1    Basset, Y.2    Miller, S.E.3    Weiblen, G.D.4    Bremer, B.5    Cizek, L.6    Drozd, P.7
  • 52
    • 75649096765 scopus 로고    scopus 로고
    • Metabolic enzymes associated with xenobiotic and chemosensory responses in Nasonia vitripennis
    • Oakeshott, J. G., Johnson, R. M., Berenbaum, M. R., Ranson, H., Cristino, A. S., Claudianos, C. (2010). Metabolic enzymes associated with xenobiotic and chemosensory responses in Nasonia vitripennis. Insect Mol Biol 19(Suppl 1):147-163.
    • (2010) Insect Mol Biol , vol.19 , Issue.SUPPL. 1 , pp. 147-163
    • Oakeshott, J.G.1    Johnson, R.M.2    Berenbaum, M.R.3    Ranson, H.4    Cristino, A.S.5    Claudianos, C.6
  • 53
    • 0034778978 scopus 로고    scopus 로고
    • The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B
    • DOI 10.1110/ps.21201
    • 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. (Pubitemid 32988634)
    • (2001) Protein Science , vol.10 , Issue.11 , pp. 2176-2185
    • Oakley, A.J.1    Harnnoi, T.2    Udomsinprasert, R.3    Jirajaroenrat, K.4    Ketterman, A.J.5    Wilce, M.C.J.6
  • 54
    • 0026470986 scopus 로고
    • An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences
    • Pemble, S. E., Taylor, J. B. (1992). An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences. Biochem J 287:957-963.
    • (1992) Biochem J , vol.287 , pp. 957-963
    • Pemble, S.E.1    Taylor, J.B.2
  • 55
    • 21644446896 scopus 로고    scopus 로고
    • Functional analysis and localisation of a delta-class glutathione S-transferase from Sarcoptes scabiei
    • DOI 10.1016/j.ijpara.2004.09.006
    • Pettersson, E. U., Ljunggren, E. L., Morrison, D. A., Mattsson, J. G. (2005). Functional analysis and localisation of a delta-class glutathione S-transferase from Sarcoptes scabiei. Int J Parasitol 35:39-48. (Pubitemid 41556670)
    • (2005) International Journal for Parasitology , vol.35 , Issue.1 , pp. 39-48
    • Pettersson, E.U.1    Ljunggren, E.L.2    Morrison, D.A.3    Mattsson, J.G.4
  • 56
    • 33846862217 scopus 로고    scopus 로고
    • Differences in the subunit interface residues of alternatively spliced glutathione transferases affects catalytic and structural functions
    • DOI 10.1042/BJ20060603
    • Piromjitpong, J., Wongsantichon, J., Ketterman, A. J. (2007). Diferences in the subunit interface residues of alternatively spliced glutathione transferases afects catalytic and structural functions. Biochem J 401:635-644. (Pubitemid 46219257)
    • (2007) Biochemical Journal , vol.401 , Issue.3 , pp. 635-644
    • Piromjitpong, J.1    Wongsantichon, J.2    Ketterman, A.J.3
  • 57
    • 0016895096 scopus 로고
    • Biochemical genetics of insecticide resistance
    • Plapp, F. W. (1976). Biochemical genetics of insecticide resistance. Annu Rev Entomol 21:179-197.
    • (1976) Annu Rev Entomol , vol.21 , pp. 179-197
    • Plapp, F.W.1
  • 58
    • 0032077652 scopus 로고    scopus 로고
    • Cloning, expression and characterization of an insect class I glutathione S-transferase from Anopheles dirus species B
    • DOI 10.1016/S0965-1748(98)00006-X, PII S096517489800006X
    • Prapanthadara, L., Ranson, H., Somboon, P., Hemingway, J. (1998). Cloning, expression, and characterization of an insect class I glutathione S-transferase from Anopheles dirus species B. Insect Biochem Molec Biol 28:321-329. (Pubitemid 28328325)
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , Issue.5-6 , pp. 321-329
    • Prapanthadara, L.-A.1    Ranson, H.2    Somboon, P.3    Hemingway, J.4
  • 59
    • 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
    • DOI 10.1042/0264-6021:3590295
    • Ranson, H., Rossiter, L., Ortelli, F., Jensen, B., Wang, X., Roth, C. W., et al. (2001). Identifcation of a novel class of insect glutathione S-transferases involved in resistance to DDT in the malaria vector Anopheles gambiae. Biochem J 359:295-304. (Pubitemid 32999773)
    • (2001) Biochemical Journal , vol.359 , Issue.2 , pp. 295-304
    • Ranson, H.1    Rossiter, L.2    Ortelli, F.3    Jensen, B.4    Wang, X.5    Roth, C.W.6    Collins, F.H.7    Hemingway, J.8
  • 60
    • 0026722795 scopus 로고
    • Three-dimensional structure of class p glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution
    • Reinemer, P., Dirr, H. W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G., et al. (1992). Three-dimensional structure of class p glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J Mol Biol 227:214-226.
    • (1992) J Mol Biol , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    Lo Bello, M.5    Federici, G.6
  • 61
    • 0025816448 scopus 로고
    • The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • Reinemer, P., Dirr, H. W., Ladenstein, R., Schäfer, J., Gallay, O., Huber, R. (1991). The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Åresolution. EMBO J 10:1997-2005. (Pubitemid 21905669)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schaffer, J.4    Gallay, O.5    Huber, R.6
  • 62
    • 0028809193 scopus 로고
    • Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1
    • Ricci, G., Lo Bello, M., Caccuri, A. M., Pastore, A., Nuccetelli, M., Parker, M. W., et al. (1995). Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1. J Biol Chem 270:1243-1248.
    • (1995) J Biol Chem , vol.270 , pp. 1243-1248
    • Ricci, G.1    Lo Bello, M.2    Caccuri, A.M.3    Pastore, A.4    Nuccetelli, M.5    Parker, M.W.6
  • 63
    • 0033985179 scopus 로고    scopus 로고
    • The hydrophobic lock-and-key intersubunit motif of glutathione transferase A1-1: Implications for catalysis, ligandin function and stability
    • DOI 10.1016/S0014-5793(99)01747-0, PII S0014579399017470
    • Sayed, Y., Wallace, L. A., Dirr, H. W. (2000). The hydrophobic lock-and-key intersubunit motif of glutathione transferase A1-1: implications for catalysis, ligandin function, and stability. FEBS Lett 465:169-172. (Pubitemid 30021468)
    • (2000) FEBS Letters , vol.465 , Issue.2-3 , pp. 169-172
    • Sayed, Y.1    Wallace, L.A.2    Dirr, H.W.3
  • 64
    • 0034833919 scopus 로고    scopus 로고
    • Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products
    • DOI 10.1046/j.1432-1327.2001.02179.x
    • Singh, S. P., Coronella, J. A., Bene?, H., Cochrane, B. J., Zimniak, P. (2001). Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products. Eur J Biochem 268:2912-2923. (Pubitemid 32862975)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.10 , pp. 2912-2923
    • Singh, S.P.1    Coronella, J.A.2    Benes, H.3    Cochrane, B.J.4    Zimniak, P.5
  • 66
    • 0034728774 scopus 로고    scopus 로고
    • Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function
    • DOI 10.1006/bbrc.2000.2579
    • Stenberg, G., Abdalla, A.-M., Mannervik, B. (2000). Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function. Biochem Biophys Res Comm 271:59-63. (Pubitemid 30444856)
    • (2000) Biochemical and Biophysical Research Communications , vol.271 , Issue.1 , pp. 59-63
    • Stenberg, G.1    Abdalla, A.-M.2    Mannervik, B.3
  • 67
    • 0026024379 scopus 로고
    • Efects of directed mutagenesis on conserved arginine residues in a human class alpha glutathione transferase
    • Stenberg, G., Board, P. G., Carlberg, I., Mannervik, B. (1991). Efects of directed mutagenesis on conserved arginine residues in a human class alpha glutathione transferase. Biochem J 274:549-555.
    • (1991) Biochem J , vol.274 , pp. 549-555
    • Stenberg, G.1    Board, P.G.2    Carlberg, I.3    Mannervik, B.4
  • 68
    • 0003144091 scopus 로고    scopus 로고
    • A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1
    • Stenberg, G., Dragani, B., Cocco, R., Principe, D. R., Mannervik, B., Aceto, A. (2001). A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1. Chem Biol Interact 133:49-50.
    • (2001) Chem Biol Interact , vol.133 , pp. 49-50
    • Stenberg, G.1    Dragani, B.2    Cocco, R.3    Principe, D.R.4    Mannervik, B.5    Aceto, A.6
  • 69
    • 21544481538 scopus 로고
    • Enzymatic dehydrochlorination of DDT by resistant fies
    • Sternburg, J. G., Vinson, E. B., Kearns, C. W. (1953). Enzymatic dehydrochlorination of DDT by resistant fies. J Econ Entomol 46:513-515.
    • (1953) J Econ Entomol , vol.46 , pp. 513-515
    • Sternburg, J.G.1    Vinson, E.B.2    Kearns, C.W.3
  • 70
    • 1242352089 scopus 로고    scopus 로고
    • Temporal Patterns of Fruit Fly (Drosophila) Evolution Revealed by Mutation Clocks
    • DOI 10.1093/molbev/msg236
    • Tamura, K., Subramanian, S., Kumar, S. (2004). Temporal patterns of fruit fy (Drosophila) evolution revealed by mutation clocks. Mol Biol Evol 21:36-44. (Pubitemid 38233516)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.1 , pp. 36-44
    • Tamura, K.1    Subramanian, S.2    Kumar, S.3
  • 71
    • 0021295946 scopus 로고
    • Induction of detoxication enzymes in insects
    • Terriere, L. C. (1984). Induction of detoxication enzymes in insects. Annu Rev Entomol 29:71-88.
    • (1984) Annu Rev Entomol , vol.29 , pp. 71-88
    • Terriere, L.C.1
  • 73
    • 0025941575 scopus 로고
    • The Drosophila glutathione S-transferase 1-1 is encoded by an intronless gene at 87B
    • Toung, Y. P. S., Hsieh, T.-S., Tu, C. P. D. (1991). The Drosophila glutathione S-transferase 1-1 is encoded by an intronless gene at 87B. Biochem Biophys Res Comm 178:1205-1211.
    • (1991) Biochem Biophys Res Comm , vol.178 , pp. 1205-1211
    • Toung, Y.P.S.1    Hsieh, T.-S.2    Tu, C.P.D.3
  • 74
    • 0027211012 scopus 로고
    • The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster
    • Toung, Y. P. S., Hsieh, T.-S., Tu, C. P. D. (1993). The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster. J Biol Chem 268:9737-9746. (Pubitemid 23146035)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.13 , pp. 9737-9746
    • Toung, Y.-P.S.1    Hsieh, T.-S.2    Tu, C.-P.D.3
  • 75
    • 0026501652 scopus 로고
    • Drosophila glutathione S-transferases have sequence homology to the stringent starvation protein of Escherichia coli
    • Toung, Y. P. S., Tu, C. P. D. (1992). Drosophila glutathione S-transferases have sequence homology to the stringent starvation protein of Escherichia coli. Biochem Biophys Res Comm 182:355-360.
    • (1992) Biochem Biophys Res Comm , vol.182 , pp. 355-360
    • Toung, Y.P.S.1    Tu, C.P.D.2
  • 76
    • 30344432127 scopus 로고    scopus 로고
    • Drosophila glutathione S-transferases
    • DOI 10.1016/S0076-6879(05)01013-X, PII S007668790501013X, 13, Gluthione Transferases and Gamma-Glutamyl Transpeptidases
    • Tu, C.-P. D., Akgul, B. (2005). Drosophila glutathione S-transferases. Meth Enzymol 401:204-226. (Pubitemid 43054901)
    • (2005) Methods in Enzymology , vol.401 , pp. 204-226
    • Tu, C.-P.D.1    Akgul, B.2
  • 78
    • 34548169608 scopus 로고    scopus 로고
    • A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis
    • DOI 10.1042/BJ20070422
    • Vararattanavech, A., Ketterman, A. J. (2007). A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis. Biochem J 406:247-256. (Pubitemid 47310955)
    • (2007) Biochemical Journal , vol.406 , Issue.2 , pp. 247-256
    • Vararattanavech, A.1    Ketterman, A.J.2
  • 79
    • 0035397391 scopus 로고    scopus 로고
    • Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens
    • DOI 10.1042/0264-6021:3570065
    • Vontas, J. G., Small, G. J., Hemingway, J. (2001). Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens. Biochem J 357:65-72. (Pubitemid 32642904)
    • (2001) Biochemical Journal , vol.357 , Issue.1 , pp. 65-72
    • Vontas, J.G.1    Small, G.J.2    Hemingway, J.3
  • 80
    • 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
    • DOI 10.1042/0264-6021:3620329
    • Vontas, J. G., Small, G. J., Nikou, D. C., Ranson, H., Hemingway, J. (2002). Purifcation, molecular cloning, and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the rice brown planthopper, Nilaparvata lugens. Biochem J 362:329-337. (Pubitemid 34214475)
    • (2002) Biochemical Journal , vol.362 , Issue.2 , pp. 329-337
    • Vontas, J.G.1    Small, G.J.2    Nikou, D.C.3    Ranson, H.4    Hemingway, J.5
  • 81
    • 71049179825 scopus 로고    scopus 로고
    • Evolution of the GST omega gene family in 12 Drosophila species
    • Walters, K. B., Grant, P., Johnson, D. L. (2009). Evolution of the GST omega gene family in 12 Drosophila species. J Hered 100:742-753.
    • (2009) J Hered , vol.100 , pp. 742-753
    • Walters, K.B.1    Grant, P.2    Johnson, D.L.3
  • 82
    • 53949123101 scopus 로고    scopus 로고
    • Structure of an insect epsilon class glutathione S-transferase from the malaria vector Anopheles gambiae provides an explanation for the high DDT-detoxifying activity
    • Wang, Y., Qiu, L., Ranson, H., Lumjuan, N., Hemingway, J., Setzer, W. N., et al. (2008). Structure of an insect epsilon class glutathione S-transferase from the malaria vector Anopheles gambiae provides an explanation for the high DDT-detoxifying activity. J Struct Biol 164:228-235.
    • (2008) J Struct Biol , vol.164 , pp. 228-235
    • Wang, Y.1    Qiu, L.2    Ranson, H.3    Lumjuan, N.4    Hemingway, J.5    Setzer, W.N.6
  • 83
    • 0030010768 scopus 로고    scopus 로고
    • Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1
    • DOI 10.1021/bi9601619
    • Widersten, M., Björnestedt, R., Mannervik, B. (1996). Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1. Biochemistry 35:7731-7742. (Pubitemid 26202513)
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7731-7742
    • Widersten, M.1    Bjornestedt, R.2    Mannervik, B.3
  • 84
    • 24744441319 scopus 로고    scopus 로고
    • An electron-sharing network involved in the catalytic mechanism is functionally conserved in different glutathione transferase classes
    • DOI 10.1074/jbc.M502612200
    • Winayanuwattikun, P., Ketterman, A. J. (2005). An electron-sharing network involved in the catalytic mechanism is functionally conserved in diferent glutathione transferase classes. J Biol Chem 280:31776-31782. (Pubitemid 41291927)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31776-31782
    • Winayanuwattikun, P.1    Ketterman, A.J.2
  • 85
    • 33847712107 scopus 로고    scopus 로고
    • Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases
    • DOI 10.1042/BJ20061253
    • Winayanuwattikun, P., Ketterman, A. J. (2007). Glutamate 64, a newly identifed residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases. Biochem J 402:339-348. (Pubitemid 46383431)
    • (2007) Biochemical Journal , vol.402 , Issue.2 , pp. 339-348
    • Winayanuwattikun, P.1    Ketterman, A.J.2
  • 86
    • 0043069892 scopus 로고    scopus 로고
    • A sensitive core region in the structure of glutathione S-transferases
    • DOI 10.1042/BJ20030394
    • Wongsantichon, J., Harnnoi, T., Ketterman, A. J. (2003). A sensitive core region in the structure of glutathione S-transferases. Biochem J 373:759-765. (Pubitemid 36981085)
    • (2003) Biochemical Journal , vol.373 , Issue.3 , pp. 759-765
    • Wongsantichon, J.1    Harnnoi, T.2    Ketterman, A.J.3
  • 87
    • 32944456314 scopus 로고    scopus 로고
    • An intersubunit lock-and-key 'Clasp' motif in the dimer interface of Delta class glutathione transferase
    • DOI 10.1042/BJ20050915
    • Wongsantichon, J., Ketterman, A. J. (2006). An intersubunit lock-and-key 'clasp' motif in the dimer interface of delta class glutathione transferase. Biochem J 394:135-144. (Pubitemid 43259663)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 135-144
    • Wongsantichon, J.1    Ketterman, A.J.2
  • 88
    • 77953416164 scopus 로고    scopus 로고
    • Structural contributions of delta class glutathione transferase active site residues to catalysis
    • Wongsantichon, J., Robinson, R. C., Ketterman, A. J. (2010). Structural contributions of delta class glutathione transferase active site residues to catalysis. Biochem J 428:25-32.
    • (2010) Biochem J , vol.428 , pp. 25-32
    • Wongsantichon, J.1    Robinson, R.C.2    Ketterman, A.J.3
  • 90
    • 63449105163 scopus 로고    scopus 로고
    • Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori
    • Yamamoto, K., Nagaoka, S., Banno, Y., Aso, Y. (2009). Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori. Comp Biochem Physiol C Toxicol Pharmacol 149:461-467.
    • (2009) Comp Biochem Physiol C Toxicol Pharmacol , vol.149 , pp. 461-467
    • Yamamoto, K.1    Nagaoka, S.2    Banno, Y.3    Aso, Y.4
  • 91
    • 77955511816 scopus 로고    scopus 로고
    • A delta-class glutathione transferase from the Chinese mitten crab Eriocheir sinensis: CDNA cloning, characterization, and mRNA expression
    • Zhao, D., Chen, L., Qin, C., Zhang, H., Wu, P., Zhang, F. (2010). A delta-class glutathione transferase from the Chinese mitten crab Eriocheir sinensis: cDNA cloning, characterization, and mRNA expression. Fish Shellfsh Immunol 29:698-703.
    • (2010) Fish Shellfsh Immunol , vol.29 , pp. 698-703
    • Zhao, D.1    Chen, L.2    Qin, C.3    Zhang, H.4    Wu, P.5    Zhang, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.