메뉴 건너뛰기




Volumn 146, Issue 1, 2004, Pages 53-64

Characterisation and expression of four mRNA sequences encoding glutathione S-transferases pi, mu, omega and sigma classes in the Pacific oyster Crassostrea gigas exposed to hydrocarbons and pesticides

Author keywords

[No Author keywords available]

Indexed keywords

BIVALVE; HYDROCARBON; METABOLISM; PESTICIDE; PHYSIOLOGICAL RESPONSE; POLLUTION EXPOSURE;

EID: 11244303549     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00227-004-1423-6     Document Type: Article
Times cited : (67)

References (60)
  • 2
    • 0032775547 scopus 로고    scopus 로고
    • Purification and characterization of the glutathione-S-transferases from the northern quahog Mercinaria mercinaria
    • Blanchette BN, Singh BR (1999) Purification and characterization of the glutathione-S-transferases from the northern quahog Mercinaria mercinaria. Mar Biotechnol 1:74-80
    • (1999) Mar Biotechnol , vol.1 , pp. 74-80
    • Blanchette, B.N.1    Singh, B.R.2
  • 3
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board PG, Baker RT, Chelvanayagam G, Jermiin LS (1997) Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J 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
  • 5
    • 20244385761 scopus 로고    scopus 로고
    • Molecular identification and expression of Heat Shock Cognate 70 (hsc70) and Heat Shock Protein 70 (hsp70) genes in the Pacific oyster Crassostrea gigas
    • Boutet I, Tanguy A, Rousseau S, Auffret M, Moraga D (2003) Molecular identification and expression of Heat Shock Cognate 70 (hsc70) and Heat Shock Protein 70 (hsp70) genes in the Pacific oyster Crassostrea gigas. Cell Stress Chaperones 8:76-85
    • (2003) Cell Stress Chaperones , vol.8 , pp. 76-85
    • Boutet, I.1    Tanguy, A.2    Rousseau, S.3    Auffret, M.4    Moraga, D.5
  • 6
    • 1642359206 scopus 로고    scopus 로고
    • Response of the Pacific oyster Crassostrea gigas to hydrocarbon contamination under experimental conditions
    • Amst
    • Boutet I, Tanguy A, Moraga D (2004) Response of the Pacific oyster Crassostrea gigas to hydrocarbon contamination under experimental conditions. Gene (Amst) 329:147-157
    • (2004) Gene , vol.329 , pp. 147-157
    • Boutet, I.1    Tanguy, A.2    Moraga, D.3
  • 7
    • 0025271344 scopus 로고
    • Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster
    • Caizzi R, Bozzetti MP, Caggese C, Ritossa F (1990) Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster. J Mol Biol 212:17-26
    • (1990) J Mol Biol , vol.212 , pp. 17-26
    • Caizzi, R.1    Bozzetti, M.P.2    Caggese, C.3    Ritossa, F.4
  • 8
    • 0000370303 scopus 로고
    • Identification of a common nucleotide sequence in the 3′-untranslated region of mRNA molecules specifying inflammatory mediators
    • Caput D, Beutler B, Hartog K, Thayer R, Brown-Shimer S, Cerami A (1986) Identification of a common nucleotide sequence in the 3′-untranslated region of mRNA molecules specifying inflammatory mediators. Proc Natl Acad Sci USA 83:1670-1674
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1670-1674
    • Caput, D.1    Beutler, B.2    Hartog, K.3    Thayer, R.4    Brown-Shimer, S.5    Cerami, A.6
  • 9
    • 0036743326 scopus 로고    scopus 로고
    • Relationships between tissue concentrations of chlorinated hydrocarbons (polychlorinated biphenyls and chlorinated pesticides) and antioxidative responses of marine mussels, Perna viridis
    • Cheung CC, Zheng GJ, Lam PK, Richardson BJ (2002) Relationships between tissue concentrations of chlorinated hydrocarbons (polychlorinated biphenyls and chlorinated pesticides) and antioxidative responses of marine mussels, Perna viridis. Mar Pollut Bull 45:181-191
    • (2002) Mar Pollut Bull , vol.45 , pp. 181-191
    • Cheung, C.C.1    Zheng, G.J.2    Lam, P.K.3    Richardson, B.J.4
  • 10
    • 0000228203 scopus 로고
    • 1979 National Biomedical Research Foundation, Silver Springs, N.D., USA
    • Dayhoff MO (1979) Atlas of protein sequence and structure, vol 5, suppl 3. 1979 National Biomedical Research Foundation, Silver Springs, N.D., USA
    • (1979) Atlas of Protein Sequence and Structure , vol.5 , Issue.3 SUPPL.
    • Dayhoff, M.O.1
  • 11
    • 0036684496 scopus 로고    scopus 로고
    • Mu-class glutathione transferase from Xenopus laevis: Molecular cloning, expression and site-directed mutagenesis
    • De Luca A, Favaloro B, Angelucci S, Sacchetta P, Di Ilio C (2002) Mu-class glutathione transferase from Xenopus laevis: molecular cloning, expression and site-directed mutagenesis. Biochem J 365:685-691
    • (2002) Biochem J , vol.365 , pp. 685-691
    • De Luca, A.1    Favaloro, B.2    Angelucci, S.3    Sacchetta, P.4    Di Ilio, C.5
  • 12
    • 0035793617 scopus 로고    scopus 로고
    • The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator
    • Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P (2001) The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J Biol Chem 276:3319-3323
    • (2001) J Biol Chem , vol.276 , pp. 3319-3323
    • Dulhunty, A.1    Gage, P.2    Curtis, S.3    Chelvanayagam, G.4    Board, P.5
  • 13
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoprotein-mediated multidrug resistance
    • Endicott JA, Ling V (1989) The biochemistry of P-glycoprotein-mediated multidrug resistance. Annu Rev Biochem 58:137-171
    • (1989) Annu Rev Biochem , vol.58 , pp. 137-171
    • Endicott, J.A.1    Ling, V.2
  • 15
    • 0027421484 scopus 로고
    • Separation of multiple forms of glutathione S-transferase from the blue mussel, Mytilus edulis
    • Fitzpatrick PJ, Sheehan D (1993) Separation of multiple forms of glutathione S-transferase from the blue mussel, Mytilus edulis. Xenobiotica 23:851-861
    • (1993) Xenobiotica , vol.23 , pp. 851-861
    • Fitzpatrick, P.J.1    Sheehan, D.2
  • 16
    • 0028854808 scopus 로고
    • Characterization of a glutathione S-transferase and a related glutathione-binding protein from gill of the blue mussel, Mytilus edulis
    • Fitzpatrick PJ, Krag TO, Hojrup P, Sheehan D (1995) Characterization of a glutathione S-transferase and a related glutathione-binding protein from gill of the blue mussel, Mytilus edulis. Biochem J 305:145-150
    • (1995) Biochem J , vol.305 , pp. 145-150
    • Fitzpatrick, P.J.1    Krag, T.O.2    Hojrup, P.3    Sheehan, D.4
  • 17
    • 0028910282 scopus 로고
    • Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase
    • Amst
    • Fucci L, Piscopo A, Aniello F, Branno M, Di Gregorio A, Calogero R, Geraci G (1995) Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase. Gene (Amst) 152:205-208
    • (1995) Gene , vol.152 , pp. 205-208
    • Fucci, L.1    Piscopo, A.2    Aniello, F.3    Branno, M.4    Di Gregorio, A.5    Calogero, R.6    Geraci, G.7
  • 18
    • 0036752751 scopus 로고    scopus 로고
    • Implications from a field study regarding the relationship between polycyclic aromatic hydrocarbons and glutathione S-transferase activity in mussels
    • Gowlan BT, McIntosh AD, Davies IM, Moffat CF, Webster L (2002) Implications from a field study regarding the relationship between polycyclic aromatic hydrocarbons and glutathione S-transferase activity in mussels. Mar Environ Res 54:231-235
    • (2002) Mar Environ Res , vol.54 , pp. 231-235
    • Gowlan, B.T.1    McIntosh, A.D.2    Davies, I.M.3    Moffat, C.F.4    Webster, L.5
  • 19
    • 0037106544 scopus 로고    scopus 로고
    • Cloning and expression of a novel mu class murine glutathione transferase isoenzyme
    • Guo J, Zimniak L, Zimniak P, Orchard JL, Singh SV (2002) Cloning and expression of a novel mu class murine glutathione transferase isoenzyme. Biochem J 366:817-824
    • (2002) Biochem J , vol.366 , pp. 817-824
    • Guo, J.1    Zimniak, L.2    Zimniak, P.3    Orchard, J.L.4    Singh, S.V.5
  • 20
    • 0033582342 scopus 로고    scopus 로고
    • Thiolation of the gamma B-crystallins in intact bovine lens exposed to hydrogen peroxide
    • Hanson SR, Chen AA, Smith JB, Lou MF (1999) Thiolation of the gamma B-crystallins in intact bovine lens exposed to hydrogen peroxide. J Biol Chem 274:4735-4742
    • (1999) J Biol Chem , vol.274 , pp. 4735-4742
    • Hanson, S.R.1    Chen, A.A.2    Smith, J.B.3    Lou, M.F.4
  • 21
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes JD, Pulford DJ (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol 30:445-600
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 22
    • 0035964430 scopus 로고    scopus 로고
    • Effect of isoproturon pretreatment on the biochemical toxicodynamics of anilofos in male rats
    • Hazarika A, Sarkar SN (2001) Effect of isoproturon pretreatment on the biochemical toxicodynamics of anilofos in male rats. Toxicology 165:87-95
    • (2001) Toxicology , vol.165 , pp. 87-95
    • Hazarika, A.1    Sarkar, S.N.2
  • 23
    • 0037436379 scopus 로고    scopus 로고
    • Influence of malathion pretreatment on the toxicity of anilofos in male rats: A biochemical interaction study
    • Hazarika A, Sarkar SN, Hajare S, Kataria M, Malik JK (2003) Influence of malathion pretreatment on the toxicity of anilofos in male rats: a biochemical interaction study. Toxicology 185:1-8
    • (2003) Toxicology , vol.185 , pp. 1-8
    • Hazarika, A.1    Sarkar, S.N.2    Hajare, S.3    Kataria, M.4    Malik, J.K.5
  • 25
    • 0023355552 scopus 로고
    • The purification and characterization of glutathione S-transferase from the hepatopancreas of the blue crab, Callinectes sapidus
    • Keeran WS, Lee RF (1987) The purification and characterization of glutathione S-transferase from the hepatopancreas of the blue crab, Callinectes sapidus. Arch Biochem Biophys 255:233-243
    • (1987) Arch Biochem Biophys , vol.255 , pp. 233-243
    • Keeran, W.S.1    Lee, R.F.2
  • 26
    • 0035013273 scopus 로고    scopus 로고
    • Biochemical response of the mussel Mytilus galloprovincialis from Bizerta (Tunisia) to chemical pollutant exposure
    • Khessiba A, Hoarau P, Gnassia-Barelli M, Aissa P, Romeo M (2001) Biochemical response of the mussel Mytilus galloprovincialis from Bizerta (Tunisia) to chemical pollutant exposure. Arch Environ Contam Toxicol 40:222-229
    • (2001) Arch Environ Contam Toxicol , vol.40 , pp. 222-229
    • Khessiba, A.1    Hoarau, P.2    Gnassia-Barelli, M.3    Aissa, P.4    Romeo, M.5
  • 27
    • 0033582482 scopus 로고    scopus 로고
    • The cloning and characterization of a new stress response protein. A mammalian member of a family of theta class glutathione S-transferase-like proteins
    • Kodym R, Calkins P, Story M (1999) The cloning and characterization of a new stress response protein. A mammalian member of a family of theta class glutathione S-transferase-like proteins. J Biol Chem 274:5131-5137
    • (1999) J Biol Chem , vol.274 , pp. 5131-5137
    • Kodym, R.1    Calkins, P.2    Story, M.3
  • 28
    • 0028294049 scopus 로고
    • MEGA: Molecular evolutionary genetics analysis software for microcomputers
    • Kumar S, Tamura K, Nei M (1994) MEGA: molecular evolutionary genetics analysis software for microcomputers. Comput Appl Biosci 10:189-191
    • (1994) Comput Appl Biosci , vol.10 , pp. 189-191
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 30
    • 0023517606 scopus 로고
    • Identification of multiple glutathione S-transferases from Daphnia magna
    • LeBlanc GA, Cochrane BJ (1987) Identification of multiple glutathione S-transferases from Daphnia magna. Comp Biochem Physiol B 88:39-45
    • (1987) Comp Biochem Physiol B , vol.88 , pp. 39-45
    • LeBlanc, G.A.1    Cochrane, B.J.2
  • 31
    • 0022555842 scopus 로고
    • Complex transcriptional units: Diversity in gene expression by alternative RNA processing
    • Leff SE, Rosenfeld MG, Evans RM (1986) Complex transcriptional units: diversity in gene expression by alternative RNA processing. Annu Rev Biochem 55:1091-1117
    • (1986) Annu Rev Biochem , vol.55 , pp. 1091-1117
    • Leff, S.E.1    Rosenfeld, M.G.2    Evans, R.M.3
  • 32
    • 0037866875 scopus 로고    scopus 로고
    • Induction of glutathione S-transferase in primary cultured digestive gland acini from the mollusc bivalve Pecten maximus (L.): Application of a new cellular model in biomonitoring studies
    • Le Pennec G, Le Pennec M (2003) Induction of glutathione S-transferase in primary cultured digestive gland acini from the mollusc bivalve Pecten maximus (L.): application of a new cellular model in biomonitoring studies. Aquat Toxicol 64:131-142
    • (2003) Aquat Toxicol , vol.64 , pp. 131-142
    • Le Pennec, G.1    Le Pennec, M.2
  • 33
    • 0037047747 scopus 로고    scopus 로고
    • Identification of six mRNA sequences of genes related to multixenobiotic resistance (MXR) and biotransformation in Mytilus edulis
    • Lüdeking A, Köhler A (2002) Identification of six mRNA sequences of genes related to multixenobiotic resistance (MXR) and biotransformation in Mytilus edulis. Mar Ecol Prog Ser 238:115-124
    • (2002) Mar Ecol Prog Ser , vol.238 , pp. 115-124
    • Lüdeking, A.1    Köhler, A.2
  • 34
    • 0033751961 scopus 로고    scopus 로고
    • Multidrug resistance in the embryos and larvae of the mussel Mytilus edulis
    • McFadzen I, Eufemia N, Heath C, Epel D, Moore M, Lowe D (2000) Multidrug resistance in the embryos and larvae of the mussel Mytilus edulis. Mar Environ Res 50:319-323
    • (2000) Mar Environ Res , vol.50 , pp. 319-323
    • McFadzen, I.1    Eufemia, N.2    Heath, C.3    Epel, D.4    Moore, M.5    Lowe, D.6
  • 35
    • 0034003759 scopus 로고    scopus 로고
    • Genetic indicators of herbicide stress in the Pacific oysters (Crassostrea gigas) under experimental conditions
    • Moraga D, Tanguy A (2000) Genetic indicators of herbicide stress in the Pacific oysters (Crassostrea gigas) under experimental conditions. Environ Toxicol Chem 19:712-718
    • (2000) Environ Toxicol Chem , vol.19 , pp. 712-718
    • Moraga, D.1    Tanguy, A.2
  • 36
    • 0023984847 scopus 로고
    • Optimal alignments in linear space
    • Myers EW, Miller W (1988) Optimal alignments in linear space. Comput Appl Biosci 4:11-17
    • (1988) Comput Appl Biosci , vol.4 , pp. 11-17
    • Myers, E.W.1    Miller, W.2
  • 37
    • 0035400069 scopus 로고    scopus 로고
    • Seasonal variation of antioxydant and biotransformation enzymes in barnacle, Balanus balanoides, and their relation with polyaromatic hydrocarbons
    • Niyogi S, Biswas S, Sarker S, Datta AG (2001) Seasonal variation of antioxydant and biotransformation enzymes in barnacle, Balanus balanoides, and their relation with polyaromatic hydrocarbons. Mar Environ Res 52:13-26
    • (2001) Mar Environ Res , vol.52 , pp. 13-26
    • Niyogi, S.1    Biswas, S.2    Sarker, S.3    Datta, A.G.4
  • 38
    • 0024297331 scopus 로고
    • Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase
    • Pavé-Preux M, Ferry N, Bouguet J, Hanoune J, Barouki R (1988) Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase. J Biol Chem 263:17459-17466
    • (1988) J Biol Chem , vol.263 , pp. 17459-17466
    • Pavé-Preux, M.1    Ferry, N.2    Bouguet, J.3    Hanoune, J.4    Barouki, R.5
  • 39
    • 0029854518 scopus 로고    scopus 로고
    • Glutathione S-transferase class kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue
    • Pemble SE, Wardle AF, Taylor JB (1996) Glutathione S-transferase class kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem J 319:749-754
    • (1996) Biochem J , vol.319 , pp. 749-754
    • Pemble, S.E.1    Wardle, A.F.2    Taylor, J.B.3
  • 40
    • 0037073278 scopus 로고    scopus 로고
    • Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments
    • Petushok N, Gabryelak T, Palecz D, Zavodnik L, Szollosi Varga I, Deér KA (2002) Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments. Aquat Toxicol 61:65-72
    • (2002) Aquat Toxicol , vol.61 , pp. 65-72
    • Petushok, N.1    Gabryelak, T.2    Palecz, D.3    Zavodnik, L.4    Szollosi Varga, I.5    Deér, K.A.6
  • 41
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • Ravichandran V, Seres T, Moriguchi T, Thomas JA, Johnston RB Jr (1994) S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J Biol Chem 269:25010-25015
    • (1994) J Biol Chem , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston Jr., R.B.5
  • 42
    • 0023404462 scopus 로고
    • Posttranscriptional gene regulation and specific binding of the nonhistone protein HMG-I by the 3′ untranslated region of bovine interleukin 2 cDNA
    • Reeves R, Elton TS, Nissen MS, Lehn D, Johnson KR (1987) Posttranscriptional gene regulation and specific binding of the nonhistone protein HMG-I by the 3′ untranslated region of bovine interleukin 2 cDNA. Proc Natl Acad Sci USA 84:6531-6535
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6531-6535
    • Reeves, R.1    Elton, T.S.2    Nissen, M.S.3    Lehn, D.4    Johnson, K.R.5
  • 43
    • 0037674821 scopus 로고    scopus 로고
    • The role of abiotic factors and pesticide levels on enzymatic activity in the freshwater mussel Anodonta cygnea at three different exposure sites
    • Robillard S, Beauchamp G, Laulier M (2003) The role of abiotic factors and pesticide levels on enzymatic activity in the freshwater mussel Anodonta cygnea at three different exposure sites. Comp Biochem Physiol C 135:49-59
    • (2003) Comp Biochem Physiol C , vol.135 , pp. 49-59
    • Robillard, S.1    Beauchamp, G.2    Laulier, M.3
  • 44
    • 0029796105 scopus 로고    scopus 로고
    • Characterization of pig liver glutathione S-transferases using HPLC-electrospray-ionization mass spectrometry
    • Rouimi P, Anglade P, Debrauwer L, Tulliez J (1996) Characterization of pig liver glutathione S-transferases using HPLC-electrospray-ionization mass spectrometry. Biochem J 317:879-884
    • (1996) Biochem J , vol.317 , pp. 879-884
    • Rouimi, P.1    Anglade, P.2    Debrauwer, L.3    Tulliez, J.4
  • 45
    • 0035882080 scopus 로고    scopus 로고
    • Purification and characterization of a glutathione S-transferase omega in pig: Evidence for two distinct organ-specific transcripts
    • Rouimi P, Anglade P, Benzekri A, Costet P, Debrauwer L, Pineau T, Tulliez J (2001) Purification and characterization of a glutathione S-transferase omega in pig: evidence for two distinct organ-specific transcripts. Biochem J 358:257-262
    • (2001) Biochem J , vol.358 , pp. 257-262
    • Rouimi, P.1    Anglade, P.2    Benzekri, A.3    Costet, P.4    Debrauwer, L.5    Pineau, T.6    Tulliez, J.7
  • 46
    • 0032955185 scopus 로고    scopus 로고
    • Glutathione S-transferases - A review
    • Salinas AE, Wong MG (1999) Glutathione S-transferases - a review. Curr Med Chem 6:279-309
    • (1999) Curr Med Chem , vol.6 , pp. 279-309
    • Salinas, A.E.1    Wong, M.G.2
  • 47
    • 0021801236 scopus 로고
    • Induction of rat hepatic drug metabolizing enzymes by substituted urea herbicides
    • Schoket B, Vincze I (1985) Induction of rat hepatic drug metabolizing enzymes by substituted urea herbicides. Acta Pharmacol Toxicol 56:283-288
    • (1985) Acta Pharmacol Toxicol , vol.56 , pp. 283-288
    • Schoket, B.1    Vincze, I.2
  • 48
    • 0023058975 scopus 로고
    • Conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G, Kamen RA (1986) Conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46:659-667
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.A.2
  • 49
    • 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 VM, Dowd CA (2001) Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem J 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
  • 50
  • 52
    • 0034954904 scopus 로고    scopus 로고
    • Induction of marine mollusc stress proteins by chemical or physical stress
    • Snyder MJ, Girvetz E, Mulder EP (2001) Induction of marine mollusc stress proteins by chemical or physical stress. Arch Environ Contam Toxicol 41:22-29
    • (2001) Arch Environ Contam Toxicol , vol.41 , pp. 22-29
    • Snyder, M.J.1    Girvetz, E.2    Mulder, E.P.3
  • 53
    • 0018496721 scopus 로고
    • Glutathione S-transferases in earthworms (Lumbricidae)
    • Stenersen J, Guthenberg C, Mannervik B (1979) Glutathione S-transferases in earthworms (Lumbricidae). Biochem J 181:47-50
    • (1979) Biochem J , vol.181 , pp. 47-50
    • Stenersen, J.1    Guthenberg, C.2    Mannervik, B.3
  • 55
    • 0025048493 scopus 로고
    • An immunohistochemical study of pi class glutathione S-transferase expression in normal human tissue
    • Terrier P, Townsend AJ, Coindre JM, Triche TJ, Cowan KH (1990) An immunohistochemical study of pi class glutathione S-transferase expression in normal human tissue. Am J Pathol 137:845-853
    • (1990) Am J Pathol , vol.137 , pp. 845-853
    • Terrier, P.1    Townsend, A.J.2    Coindre, J.M.3    Triche, T.J.4    Cowan, K.H.5
  • 56
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acid Res 25:4876-4882
    • (1997) Nucleic Acid Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 58
    • 0037290663 scopus 로고    scopus 로고
    • Fish bioaccumulation and biomarkers in environmental risk assessment: A review
    • Van der Oost R, Beyer J, Vermeulen NPE (2003) Fish bioaccumulation and biomarkers in environmental risk assessment: a review. Environ Toxicol Pharmacol 13:57-149
    • (2003) Environ Toxicol Pharmacol , vol.13 , pp. 57-149
    • Van Der Oost, R.1    Beyer, J.2    Vermeulen, N.P.E.3
  • 59
    • 0036234536 scopus 로고    scopus 로고
    • Purification and characterisation of glutathione S-transferases from the freshwater clam Corbicula fluminea (Muller)
    • Vidai ML, Rouimi P, Debrauwer L, Narbonne JF (2002) Purification and characterisation of glutathione S-transferases from the freshwater clam Corbicula fluminea (Muller). Comp Biochem Physiol C 131:477-489
    • (2002) Comp Biochem Physiol C , vol.131 , pp. 477-489
    • Vidai, M.L.1    Rouimi, P.2    Debrauwer, L.3    Narbonne, J.F.4
  • 60
    • 0032437130 scopus 로고    scopus 로고
    • Human glutathione S-transferases
    • Whalen R, Boyer TD (1998) Human glutathione S-transferases. Semin Liver Dis 18:345-358
    • (1998) Semin Liver Dis , vol.18 , pp. 345-358
    • Whalen, R.1    Boyer, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.