메뉴 건너뛰기




Volumn 56, Issue 1, 2000, Pages 26-36

Mu-Class GSTs are responsible for aflatoxin B1-8,9-epoxide-conjugating activity in the nonhuman primate Macaca fascicularis liver

Author keywords

Aflatoxin; Biotransformation; cDNA; Glutathione S transferase; Liver; mu class; Nonhuman primate

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; AFLATOXIN; AFLATOXIN B1; AFLATOXIN B1 8,9 EPOXIDE; DNA; GLUTATHIONE DERIVATIVE; GLUTATHIONE TRANSFERASE; ISOENZYME; LIVER ENZYME; RECOMBINANT ENZYME; RNA DIRECTED DNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 0033935601     PISSN: 10966080     EISSN: None     Source Type: Journal    
DOI: 10.1093/toxsci/56.1.26     Document Type: Article
Times cited : (23)

References (52)
  • 2
    • 0030967073 scopus 로고    scopus 로고
    • Glutathione transferases catalyze the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes
    • Baez, S., Segura-Aguilar, J., Widersten, M., Johansson, A. S., and Mannervik, B. (1997). Glutathione transferases catalyze the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes. Biochem. J. 324, 25-28.
    • (1997) Biochem. J. , vol.324 , pp. 25-28
    • Baez, S.1    Segura-Aguilar, J.2    Widersten, M.3    Johansson, A.S.4    Mannervik, B.5
  • 3
    • 0029085232 scopus 로고
    • Amino acid differences at positions 10, 11, and 104 explain the profound catalytic differences between two murine pi-class glutathione S-transferases
    • Bammler, T. K., Driessen, H., Finnstrom, N., and Wolf, C. R. (1995). Amino acid differences at positions 10, 11, and 104 explain the profound catalytic differences between two murine pi-class glutathione S-transferases. Biochemistry 34, 9000-9008.
    • (1995) Biochemistry , vol.34 , pp. 9000-9008
    • Bammler, T.K.1    Driessen, H.2    Finnstrom, N.3    Wolf, C.R.4
  • 4
    • 0029565787 scopus 로고
    • The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site
    • Bjornestedt, R., Tardioli, S., and Mannervik, B. (1995). The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site. J. Biol. Chem. 270, 29705-29709.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29705-29709
    • Bjornestedt, R.1    Tardioli, S.2    Mannervik, B.3
  • 5
    • 0021772873 scopus 로고
    • Investigation of the kinetic and stereochemical recognition of arene and azaarene oxides by isozymes A2 and C2 of glutathione S-transferase
    • Boehlert, C. C., and Armstrong, R. N. (1984). Investigation of the kinetic and stereochemical recognition of arene and azaarene oxides by isozymes A2 and C2 of glutathione S-transferase. Biochem. Biophys. Res. Commun. 121, 980-986.
    • (1984) Biochem. Biophys. Res. Commun. , vol.121 , pp. 980-986
    • Boehlert, C.C.1    Armstrong, R.N.2
  • 6
    • 0029883290 scopus 로고    scopus 로고
    • Oltipraz-mediated changes in aflatoxin B1 biotransformation in rat liver: Implications for human chemointervention
    • Buetler, T. M., Bammler, T. K., Hayes, J. D., and Eaton, D. L. (1996). Oltipraz-mediated changes in aflatoxin B1 biotransformation in rat liver: implications for human chemointervention. Cancer Res. 56, 2306-2313.
    • (1996) Cancer Res. , vol.56 , pp. 2306-2313
    • Buetler, T.M.1    Bammler, T.K.2    Hayes, J.D.3    Eaton, D.L.4
  • 7
    • 0026546972 scopus 로고
    • Complementary DNA cloning, messenger RNA expression, and induction of alpha-class glutathione S-transferases in mouse tissues
    • Buetler, T. M., and Eaton, D. L. (1992). Complementary DNA cloning, messenger RNA expression, and induction of alpha-class glutathione S-transferases in mouse tissues. Cancer Res. 52, 314-318.
    • (1992) Cancer Res. , vol.52 , pp. 314-318
    • Buetler, T.M.1    Eaton, D.L.2
  • 8
    • 0030785082 scopus 로고    scopus 로고
    • Epidemiological characteristics and risk factors of hepatocellular carcinoma
    • Chen, C. J., Yu, M. W., and Liaw, Y. F. (1997). Epidemiological characteristics and risk factors of hepatocellular carcinoma. J. Gastroenterol. Hepatol. 12, S294-308.
    • (1997) J. Gastroenterol. Hepatol. , vol.12
    • Chen, C.J.1    Yu, M.W.2    Liaw, Y.F.3
  • 9
    • 0021103450 scopus 로고
    • Stereoselectivity of isozyme C of glutathione S-transferase toward arene and azaarene oxides
    • Cobb, D., Boehlert, C., Lewis, D., and Armstrong, R. N. (1983). Stereoselectivity of isozyme C of glutathione S-transferase toward arene and azaarene oxides. Biochemistry 22, 805-812.
    • (1983) Biochemistry , vol.22 , pp. 805-812
    • Cobb, D.1    Boehlert, C.2    Lewis, D.3    Armstrong, R.N.4
  • 10
    • 0027182019 scopus 로고
    • Isolation and analysis of the gene and cDNA for a human mu-class glutathione S-transferase. GSTM4
    • Comstock, K. E., Johnson, K. J., Rifenbery, D., and Henner, W. D. (1993). Isolation and analysis of the gene and cDNA for a human mu-class glutathione S-transferase. GSTM4. J. Biol. Chem. 268, 16958-16965.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16958-16965
    • Comstock, K.E.1    Johnson, K.J.2    Rifenbery, D.3    Henner, W.D.4
  • 12
    • 0011447578 scopus 로고
    • Species and diet-related differences in aflatoxin biotransfromation
    • D. Bhatnagar, E. B. Lillehoj, and D. K. Arora, Eds., Marcel Dekker, New York
    • Eaton, D. L., and Ramsdell, H. H. (1992). Species and diet-related differences in aflatoxin biotransfromation. In Handbook of Applied Mycology: Mycotoxins in Ecological Systems, (D. Bhatnagar, E. B. Lillehoj, and D. K. Arora, Eds.), pp. 157-182. Marcel Dekker, New York.
    • (1992) Handbook of Applied Mycology: Mycotoxins in Ecological Systems , pp. 157-182
    • Eaton, D.L.1    Ramsdell, H.H.2
  • 13
    • 0025892519 scopus 로고
    • Glutathione S-transferase-mediated chlorothalonil metabolism in liver and gill subcellular fractions of channel catfish
    • Gallagher, E. P., Kedderis, G. L., and Di Giulio, R. T. (1991). Glutathione S-transferase-mediated chlorothalonil metabolism in liver and gill subcellular fractions of channel catfish. Biochem. Pharmacol. 42, 139-145.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 139-145
    • Gallagher, E.P.1    Kedderis, G.L.2    Di Giulio, R.T.3
  • 14
    • 0030024642 scopus 로고    scopus 로고
    • Channel catfish glutathione S-transferase isoenzyme activity toward (+/-)-anti-benzo[a]pyrene-trans-7,8-dihydrodiol-9,10-epoxide
    • Gallagher, E. P., Stapleton, P. L., Slone, D. H., Schlenk, D., and Eaton, D. L. (1996). Channel catfish glutathione S-transferase isoenzyme activity toward (+/-)-anti-benzo[a]pyrene-trans-7,8-dihydrodiol-9,10-epoxide. Aq. Toxicol. 34, 135-150.
    • (1996) Aq. Toxicol. , vol.34 , pp. 135-150
    • Gallagher, E.P.1    Stapleton, P.L.2    Slone, D.H.3    Schlenk, D.4    Eaton, D.L.5
  • 15
    • 0000650543 scopus 로고
    • Molecular dosimetry methods for assessing human aflatoxin exposure
    • D. L. Eaton and J. D. Groopman, Eds., Academic Press, New York
    • Groopman, J. D. (1994). Molecular dosimetry methods for assessing human aflatoxin exposure. In Toxicology of Aflatoxins: Human Health, Veterinary and Agricultural Significance, (D. L. Eaton and J. D. Groopman, Eds.), pp. 259-280, Academic Press, New York.
    • (1994) Toxicology of Aflatoxins: Human Health, Veterinary and Agricultural Significance , pp. 259-280
    • Groopman, J.D.1
  • 16
    • 0024240828 scopus 로고
    • Aflatoxin exposure in human populations: Measurements and relationship to cancer
    • Groopman, J. D., Cain, L. G., and Kensler, T. W. (1988). Aflatoxin exposure in human populations: measurements and relationship to cancer. CRC Crit. Rev. Toxicol. 19, 113-145.
    • (1988) CRC Crit. Rev. Toxicol. , vol.19 , pp. 113-145
    • Groopman, J.D.1    Cain, L.G.2    Kensler, T.W.3
  • 18
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione S-transferases
    • Habig, W. H., and Jakoby, W. B. (1981). Assays for differentiation of glutathione S-transferases. Methods Enzymol. 77, 398-405.
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 19
    • 0026050193 scopus 로고
    • Ethoxyquin-induced resistance to aflatoxin B1 in the rat is associated with the expression of a novel alpha-class glutathione S-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin B1-8,9-epoxide
    • Hayes, J. D., Judah, D. J., McLellan, L. I., Kerr, L. A., Peacock, S. D., and Neal, G. E. (1991). Ethoxyquin-induced resistance to aflatoxin B1 in the rat is associated with the expression of a novel alpha-class glutathione S-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin B1-8,9-epoxide. Biochem. J. 279, 385-398.
    • (1991) Biochem. J. , vol.279 , pp. 385-398
    • Hayes, J.D.1    Judah, D.J.2    McLellan, L.I.3    Kerr, L.A.4    Peacock, S.D.5    Neal, G.E.6
  • 20
    • 0026639135 scopus 로고
    • Molecular cloning and heterologous expression of a cDNA encoding a mouse glutathione S-transferase Yc subunit possessing high catalytic activity for aflatoxin B1-8,9-epoxide
    • Hayes, J. D., Judah, D. J., Neal, G. E., and Nguyen, T. (1992). Molecular cloning and heterologous expression of a cDNA encoding a mouse glutathione S-transferase Yc subunit possessing high catalytic activity for aflatoxin B1-8,9-epoxide. Biochem. J. 285, 173-180.
    • (1992) Biochem. J. , vol.285 , pp. 173-180
    • Hayes, J.D.1    Judah, D.J.2    Neal, G.E.3    Nguyen, T.4
  • 21
    • 0028131485 scopus 로고
    • Cloning of cDNAs from fetal rat liver encoding glutathione S-transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1
    • Hayes, J. D., Nguyen, T., Judah, D. J., Petersson, D. G., and Neal, G. E. (1994). Cloning of cDNAs from fetal rat liver encoding glutathione S-transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1. J. Biol. Chem. 269, 20707-20717.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20707-20717
    • Hayes, J.D.1    Nguyen, T.2    Judah, D.J.3    Petersson, D.G.4    Neal, G.E.5
  • 22
    • 0031238820 scopus 로고    scopus 로고
    • Mechanism of differential catalytic efficiency of two polymorphic forms of human glutathione S-transferase P1-1 in the glutathione conjugation of carcinogenic diol epoxide of chrysene
    • Hu, X., Ji, X., Srivastava, S. K., Xia, H., Awasthi, S., Nanduri, B., Awasthi, Y. C., Zimniak, P., and Singh, S. V. (1997a). Mechanism of differential catalytic efficiency of two polymorphic forms of human glutathione S-transferase P1-1 in the glutathione conjugation of carcinogenic diol epoxide of chrysene. Arch. Biochem. Biophys. 345, 32-38.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 32-38
    • Hu, X.1    Ji, X.2    Srivastava, S.K.3    Xia, H.4    Awasthi, S.5    Nanduri, B.6    Awasthi, Y.C.7    Zimniak, P.8    Singh, S.V.9
  • 23
    • 0031577161 scopus 로고    scopus 로고
    • Active-site architecture of polymorphic forms of human glutathione S-transferase P1-1 accounts for their enantioselectivity and disparate activity in the glutathione conjugation of 7-beta,8-alpha-dihydroxy-9-alpha,10-alpha-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene
    • Hu, X., O'Donnell, R., Srivastava, S. K., Xia, H., Zimniak, P., Nanduri, B., Bleicher, R. J., Awasthi, S., Awasthi, Y. C., Ji, X., and Singh, S. V. (1997b). Active-site architecture of polymorphic forms of human glutathione S-transferase P1-1 accounts for their enantioselectivity and disparate activity in the glutathione conjugation of 7-beta,8-alpha-dihydroxy-9-alpha,10-alpha-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene. Biochem. Biophys. Res. Commun. 235, 424-428.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 424-428
    • Hu, X.1    O'Donnell, R.2    Srivastava, S.K.3    Xia, H.4    Zimniak, P.5    Nanduri, B.6    Bleicher, R.J.7    Awasthi, S.8    Awasthi, Y.C.9    Ji, X.10    Singh, S.V.11
  • 24
    • 0031716994 scopus 로고    scopus 로고
    • Specificities of human glutathione S-transferase isozymes toward anti-diol epoxides of methylchrysenes
    • Hu, X., Pal, A., Krzeminski, J., Amin, S., Awasthi, Y. C., Zimniak, P., and Singh, S. V. (1998). Specificities of human glutathione S-transferase isozymes toward anti-diol epoxides of methylchrysenes. Carcinogenesis 19, 1685-1689.
    • (1998) Carcinogenesis , vol.19 , pp. 1685-1689
    • Hu, X.1    Pal, A.2    Krzeminski, J.3    Amin, S.4    Awasthi, Y.C.5    Zimniak, P.6    Singh, S.V.7
  • 25
    • 0031577576 scopus 로고    scopus 로고
    • Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons
    • Hu, X., Xia, H., Srivastava, S. K., Herzog, C., Awasthi, Y. C., Ji, X., Zimniak, P., and Singh, S. V. (1997c). Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons. Biochem. Biophys. Res. Commun. 238, 397-402.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 397-402
    • Hu, X.1    Xia, H.2    Srivastava, S.K.3    Herzog, C.4    Awasthi, Y.C.5    Ji, X.6    Zimniak, P.7    Singh, S.V.8
  • 26
    • 0027485154 scopus 로고
    • Human mu-class glutathione S-transferases present in liver, skeletal muscle, and testicular tissue
    • Hussey, A. J., and Hayes, J. D. (1993). Human mu-class glutathione S-transferases present in liver, skeletal muscle, and testicular tissue. Biochim. Biophys. Acta 1203, 131-141.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 131-141
    • Hussey, A.J.1    Hayes, J.D.2
  • 28
    • 0030610234 scopus 로고    scopus 로고
    • Reaction of aflatoxin B1 exo-8,9-epoxide with DNA: Kinetic analysis of covalent binding and DNA-induced hydrolysis
    • Johnson, W. W., and Guengerich, F. P. (1997). Reaction of aflatoxin B1 exo-8,9-epoxide with DNA: kinetic analysis of covalent binding and DNA-induced hydrolysis. Proc. Natl. Acad Sci. U.S.A. 94, 6121-6125.
    • (1997) Proc. Natl. Acad Sci. U.S.A. , vol.94 , pp. 6121-6125
    • Johnson, W.W.1    Guengerich, F.P.2
  • 29
    • 0030894660 scopus 로고    scopus 로고
    • Conjugation of highly reactive aflatoxin B1 exo-8,9-epoxide catalyzed by rat and human glutathione transferases: Estimation of kinetic parameters
    • Johnson, W. W., Ueng, Y. F., Widersten, M., Mannervik, B., Hayes, J. D., Sherratt, P. J., Ketterer, B., and Guengerich, F. P. (1997). Conjugation of highly reactive aflatoxin B1 exo-8,9-epoxide catalyzed by rat and human glutathione transferases: estimation of kinetic parameters. Biochemistry 36, 3056-3060.
    • (1997) Biochemistry , vol.36 , pp. 3056-3060
    • Johnson, W.W.1    Ueng, Y.F.2    Widersten, M.3    Mannervik, B.4    Hayes, J.D.5    Sherratt, P.J.6    Ketterer, B.7    Guengerich, F.P.8
  • 30
    • 0024976419 scopus 로고
    • Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue
    • Lindberg, R. L., and Negishi, M. (1989). Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue. Nature 339, 632-634.
    • (1989) Nature , vol.339 , pp. 632-634
    • Lindberg, R.L.1    Negishi, M.2
  • 33
    • 0029956734 scopus 로고    scopus 로고
    • Binding of the aflatoxin-glutathione conjugate to mouse glutathione S-transferase A3-3 is saturated at only one ligand per dimer
    • McHugh, T. E., Atkins, W. M., Racha, J. K., Kunze, K. L., and Eaton, D. L. (1996). Binding of the aflatoxin-glutathione conjugate to mouse glutathione S-transferase A3-3 is saturated at only one ligand per dimer. J. Biol. Chem. 271, 27470-27474.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27470-27474
    • McHugh, T.E.1    Atkins, W.M.2    Racha, J.K.3    Kunze, K.L.4    Eaton, D.L.5
  • 34
    • 0023252403 scopus 로고
    • Comparative effects of butylated hydroxyanisole on hepatic in vivo DNA binding and in vitro biotransformation of aflatoxin B1 in the rat and mouse
    • Monroe, D. H., and Eaton, D. L. (1987). Comparative effects of butylated hydroxyanisole on hepatic in vivo DNA binding and in vitro biotransformation of aflatoxin B1 in the rat and mouse. Toxicol. Appl. Pharmacol. 90, 401-409.
    • (1987) Toxicol. Appl. Pharmacol. , vol.90 , pp. 401-409
    • Monroe, D.H.1    Eaton, D.L.2
  • 35
    • 0023949442 scopus 로고
    • Effects of modulation of hepatic glutathione on biotransformation and covalent binding of aflatoxin B1 to DNA in the mouse
    • Monroe, D. H., and Eaton, D. L. (1988). Effects of modulation of hepatic glutathione on biotransformation and covalent binding of aflatoxin B1 to DNA in the mouse Toxicol. Appl. Pharmacol. 94, 118-127.
    • (1988) Toxicol. Appl. Pharmacol. , vol.94 , pp. 118-127
    • Monroe, D.H.1    Eaton, D.L.2
  • 36
    • 0022270571 scopus 로고
    • The metabolism of aflatoxin B1 by human liver
    • Moss, E. J., and Neal, G. E. (1985). The metabolism of aflatoxin B1 by human liver. Biochem. Pharmacol. 34, 3193-3197.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3193-3197
    • Moss, E.J.1    Neal, G.E.2
  • 37
    • 0030588937 scopus 로고    scopus 로고
    • Amino acid residue 104 in an alpha-class glutathione S-transferase is essential for the high selectivity and specificity of the enzyme for 4-hydroxynonenal
    • Nanduri, B., Hayden, J. B., Awasthi, Y. C., and Zimniak, P. (1996). Amino acid residue 104 in an alpha-class glutathione S-transferase is essential for the high selectivity and specificity of the enzyme for 4-hydroxynonenal. Arch. Biochem. Biophys. 335, 305-310.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 305-310
    • Nanduri, B.1    Hayden, J.B.2    Awasthi, Y.C.3    Zimniak, P.4
  • 39
    • 0023823920 scopus 로고
    • Modification of aflatoxin B1 biotransformation in vitro and DNA binding in vivo by dietary broccoli in rats
    • Ramsdell, H. S., and Eaton, D. L. (1988). Modification of aflatoxin B1 biotransformation in vitro and DNA binding in vivo by dietary broccoli in rats. J. Toxicol. Env. Health 25, 269-284.
    • (1988) J. Toxicol. Env. Health , vol.25 , pp. 269-284
    • Ramsdell, H.S.1    Eaton, D.L.2
  • 40
    • 0025000688 scopus 로고
    • Mouse liver glutathione S-transferase isoenzyme activity toward aflatoxin B1-8,9-epoxide and benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide
    • Ramsdell, H. S., and Eaton, D. L. (1990). Mouse liver glutathione S-transferase isoenzyme activity toward aflatoxin B1-8,9-epoxide and benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide. Toxicol. Appl. Pharmacol. 105, 216-225.
    • (1990) Toxicol. Appl. Pharmacol. , vol.105 , pp. 216-225
    • Ramsdell, H.S.1    Eaton, D.L.2
  • 42
    • 0026730960 scopus 로고
    • Glutathione conjugation of aflatoxin B1 exo- and endo-epoxides by rat and human glutathione S-transferases
    • Raney, K. D., Meyer, D. J., Ketterer, B., Harris, T. M., and Guengerich, F. P. (1992b). Glutathione conjugation of aflatoxin B1 exo- and endo-epoxides by rat and human glutathione S-transferases. Chem. Res. Toxicol. 5, 470-478.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 470-478
    • Raney, K.D.1    Meyer, D.J.2    Ketterer, B.3    Harris, T.M.4    Guengerich, F.P.5
  • 43
    • 0027296348 scopus 로고
    • Molecular cloning and heterologous expression of an alternatively spliced human mu-class glutathione S-transferase transcript
    • Ross, V. L., and Board, P. G. (1993). Molecular cloning and heterologous expression of an alternatively spliced human mu-class glutathione S-transferase transcript. Biochem. J. 294, 373-380.
    • (1993) Biochem. J. , vol.294 , pp. 373-380
    • Ross, V.L.1    Board, P.G.2
  • 44
    • 0030744050 scopus 로고    scopus 로고
    • Subunit diversity and tissue distribution of human glutathione S-transferases: Interpretations based on electrospray ionization-MS and peptide sequence-specific antisera
    • Rowe, J. D., Nieves, E., and Listowsky, I. (1997). Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera. Biochem. J. 325, 481-486.
    • (1997) Biochem. J. , vol.325 , pp. 481-486
    • Rowe, J.D.1    Nieves, E.2    Listowsky, I.3
  • 45
    • 0028605708 scopus 로고
    • Rational reconstruction of the active site of a class-mu glutathione S-transferase
    • Shan, S., and Armstrong, R. N. (1994). Rational reconstruction of the active site of a class-mu glutathione S-transferase. J. Biol. Chem. 269, 32373-32379.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32373-32379
    • Shan, S.1    Armstrong, R.N.2
  • 46
    • 0029037994 scopus 로고
    • Human variability in hepatic glutathione S-transferase-mediated conjugation of aflatoxin B1-epoxide and other substrates
    • Slone, D. H., Gallagher, E. P., Ramsdell, H. S., Rettie, A. E., Stapleton, P. L., Berlad, L. G., and Eaton, D. L. (1995). Human variability in hepatic glutathione S-transferase-mediated conjugation of aflatoxin B1-epoxide and other substrates. Pharmacogenetics 5, 224-233.
    • (1995) Pharmacogenetics , vol.5 , pp. 224-233
    • Slone, D.H.1    Gallagher, E.P.2    Ramsdell, H.S.3    Rettie, A.E.4    Stapleton, P.L.5    Berlad, L.G.6    Eaton, D.L.7
  • 47
    • 0031737378 scopus 로고    scopus 로고
    • Identification of amino acid residues essential for high aflatoxin B1-8,9-epoxide conjugation activity in alpha class glutathione S-transferases through site-directed mutagenesis
    • van Ness, K. P., McHugh, T. E., Bammler, T. K., and Eaton, D. L. (1998). Identification of amino acid residues essential for high aflatoxin B1-8,9-epoxide conjugation activity in alpha class glutathione S-transferases through site-directed mutagenesis. Toxicol. Appl. Pharmacol. 152, 166-174.
    • (1998) Toxicol. Appl. Pharmacol. , vol.152 , pp. 166-174
    • Van Ness, K.P.1    McHugh, T.E.2    Bammler, T.K.3    Eaton, D.L.4
  • 48
    • 0025778535 scopus 로고
    • Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus
    • Vorachek, W. R., Pearson, W. R., and Rule, G. S. (1991). Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc. Natl. Acad. Sci. 88, 4443-4447.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 4443-4447
    • Vorachek, W.R.1    Pearson, W.R.2    Rule, G.S.3
  • 49
    • 0001123818 scopus 로고
    • Factors affecting aspergillus flavus-group infection and aflatoxin contaminatin of crops
    • D. L. Eaton and J. D. Groopman, Eds., Academic Press, New York
    • Wilson, D. M., and Payne, G. A. (1994). Factors affecting aspergillus flavus-group infection and aflatoxin contaminatin of crops. In The Toxicology of Aflatoxins: Human Health, Veterinary, and Agricultural Significance, (D. L. Eaton and J. D. Groopman, Eds.), pp. 309-325. Academic Press, New York.
    • (1994) The Toxicology of Aflatoxins: Human Health, Veterinary, and Agricultural Significance , pp. 309-325
    • Wilson, D.M.1    Payne, G.A.2
  • 50
    • 0001545268 scopus 로고
    • Aflatoxin carcinogenesis
    • H. Busch, Ed., Academic Press, New York
    • Wogan, G. (1973). Aflatoxin carcinogenesis. In Methods of Cancer Research, (H. Busch, Ed.), pp. 309-344, Academic Press, New York.
    • (1973) Methods of Cancer Research , pp. 309-344
    • Wogan, G.1
  • 51
    • 0014169657 scopus 로고
    • Dose-response characteristics of aflatoxin B1 carcinogenesis in the rat
    • Wogan, G. N., and Newberne, P. M. (1967). Dose-response characteristics of aflatoxin B1 carcinogenesis in the rat. Cancer Res. 27, 2370-2376.
    • (1967) Cancer Res. , vol.27 , pp. 2370-2376
    • Wogan, G.N.1    Newberne, P.M.2
  • 52
    • 0028088048 scopus 로고
    • Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties
    • Zimniak, P., Nanduri, B., Pikula, S., Bandorowicz-Pikula, J., Singhal, S. S., Srivastava, S. K., Awasthi, S., and Awasthi, Y. C. (1994). Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties. Eur. J. Biochem. 224, 893-899.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 893-899
    • Zimniak, P.1    Nanduri, B.2    Pikula, S.3    Bandorowicz-Pikula, J.4    Singhal, S.S.5    Srivastava, S.K.6    Awasthi, S.7    Awasthi, Y.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.