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Volumn 31, Issue 4, 1999, Pages 273-300

Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress

Author keywords

glutamylcysteine synthetase; Antioxidant responsive element; Cancer chemoprevention; Glutathione peroxidase; Glutathione S conjugate efflux pump; Glutathione S transferase; Glutathione synthetase; Multidrug resistance associated protein

Indexed keywords

FREE RADICAL; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE SYNTHASE; LEUCINE ZIPPER PROTEIN; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR;

EID: 0032874845     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715769900300851     Document Type: Conference Paper
Times cited : (1317)

References (177)
  • 2
    • 85053972204 scopus 로고    scopus 로고
    • Role of free radicals in alcohol-induced tissue injury
    • (Eds. S.I. Baskin and H. Salem), Taylor and Francis, Washington and London
    • C. Colton and S. Zakhari (1997) Role of free radicals in alcohol-induced tissue injury. In Oxidants, Antioxidants and Free Radicals (Eds. S.I. Baskin and H. Salem), Taylor and Francis, Washington and London, pp. 259-271.
    • (1997) Oxidants, Antioxidants and Free Radicals , pp. 259-271
    • Colton, C.1    Zakhari, S.2
  • 3
    • 85053982890 scopus 로고    scopus 로고
    • The analysis of free radicals, their reaction products, and antioxidants
    • (Eds. S.I. Baskin and H. Salem), Taylor and Francis, Washington and London
    • I.N. Acworth, D.R. McCabe and T.J. Maher (1997) The analysis of free radicals, their reaction products, and antioxidants. In Oxidants, Antioxidants and Free Radicals (Eds. S.I. Baskin and H. Salem), Taylor and Francis, Washington and London, pp. 23-77.
    • (1997) Oxidants, Antioxidants and Free Radicals , pp. 23-77
    • Acworth, I.N.1    McCabe, D.R.2    Maher, T.J.3
  • 4
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • A. Meister (1988) Glutathione metabolism and its selective modification. The Journal of Biological Chemistry, 263, 17205-17208.
    • (1988) The Journal of Biological Chemistry , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 5
    • 0016635533 scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by nonallosteric feedback inhibition by glutathione
    • P.G. Richman and A. Meister (1975) Regulation of γ-glutamylcysteine synthetase by nonallosteric feedback inhibition by glutathione. The Journal of Biological Chemistry, 250, 1422-1426.
    • (1975) The Journal of Biological Chemistry , vol.250 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 6
    • 0025091990 scopus 로고
    • Amino acid sequence of rat kidney γ-glutamylcysteine synthetase
    • N. Yan and A. Meister (1990) Amino acid sequence of rat kidney γ-glutamylcysteine synthetase. The Journal of Biological Chemistry, 265, 1588-1593.
    • (1990) The Journal of Biological Chemistry , vol.265 , pp. 1588-1593
    • Yan, N.1    Meister, A.2
  • 7
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase
    • C-S. Huang, L.-S. Chang, M.E. Anderson and A. Meister (1993) Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase. The Journal of Biological Chemistry, 268, 19675-19680.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 19675-19680
    • Huang, C.-S.1    Chang, L.-S.2    Anderson, M.E.3    Meister, A.4
  • 8
    • 0027227925 scopus 로고
    • Amino acid sequence and function of the light subunit of rat kidney γ-glutamylcysteine synthetase
    • C.-S. Huang, M.E. Anderson and A. Meister (1993) Amino acid sequence and function of the light subunit of rat kidney γ-glutamylcysteine synthetase. The Journal of Biological Chemistry, 268, 20578-20583.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 20578-20583
    • Huang, C.-S.1    Anderson, M.E.2    Meister, A.3
  • 9
    • 0028959153 scopus 로고
    • Cloning and sequencing of the cDNA for the light subunit of human liver γ-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues
    • J.J. Gipp, H.H. Bailey and R.T. Mulcahy (1995) Cloning and sequencing of the cDNA for the light subunit of human liver γ-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues. Biochemical and Biophysical Research Communications, 206, 584-589
    • (1995) Biochemical and Biophysical Research Communications , vol.206 , pp. 584-589
    • Gipp, J.J.1    Bailey, H.H.2    Mulcahy, R.T.3
  • 10
    • 0033082845 scopus 로고    scopus 로고
    • Over-expression of the regulatory subunit of γ-glutamylcysteine synthetase in HeLa cells increases γ-glutamylcysteine synthetase activity and confers drug-resistance
    • S.R. Tipnis, D.G. Blake, A.G. Shepherd and L.I. McLellan (1999) Over-expression of the regulatory subunit of γ-glutamylcysteine synthetase in HeLa cells increases γ-glutamylcysteine synthetase activity and confers drug-resistance. Biochemical Journal, 337, 559-566.
    • (1999) Biochemical Journal , vol.337 , pp. 559-566
    • Tipnis, S.R.1    Blake, D.G.2    Shepherd, A.G.3    McLellan, L.I.4
  • 11
    • 0030670301 scopus 로고    scopus 로고
    • Regulation of human γ-glutamylcysteine synthetase: Co-ordinate induction of the catalytic and regulatory subunits in HepG2 cells
    • D.C Galloway, D.G. Blake, A.G. Shepherd and L.I. McLellan (1997) Regulation of human γ-glutamylcysteine synthetase: co-ordinate induction of the catalytic and regulatory subunits in HepG2 cells. Biochemical Journal, 328, 99-104.
    • (1997) Biochemical Journal , vol.328 , pp. 99-104
    • Galloway, D.C.1    Blake, D.G.2    Shepherd, A.G.3    McLellan, L.I.4
  • 12
    • 0030956247 scopus 로고    scopus 로고
    • Constitutive and β-naphthoflavone-induced expression of the human γ-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/TRE sequence
    • R.T. Mulcahy, M.A. Wartman, H.H. Bailey and J.J. Gipp (1997) Constitutive and β-naphthoflavone-induced expression of the human γ-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/TRE sequence. The Journal of Biological Chemistry, 272, 7445-7454.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 7445-7454
    • Mulcahy, R.T.1    Wartman, M.A.2    Bailey, H.H.3    Gipp, J.J.4
  • 13
    • 0031172884 scopus 로고    scopus 로고
    • Increased transcription of the regulatory subunit of γ-glutamylcysteine synthetase in rat lung epithelial L2 cells exposed to oxidative stress or glutathione depletion
    • L. Tian, M.M. Shi and H.J. Forman (1997) Increased transcription of the regulatory subunit of γ-glutamylcysteine synthetase in rat lung epithelial L2 cells exposed to oxidative stress or glutathione depletion. Archives of Biochemistry and Biophysics, 342, 126-133.
    • (1997) Archives of Biochemistry and Biophysics , vol.342 , pp. 126-133
    • Tian, L.1    Shi, M.M.2    Forman, H.J.3
  • 14
    • 0030973242 scopus 로고    scopus 로고
    • Alteration of transcriptional and post-transcriptional expression of gamma-glutamylcysteine synthetase by diethylmaleate
    • K.R. Sekhar, M. Long, J. Long, Z.-Q. Xu, M.L. Summar and M.L. Freeman (1997) Alteration of transcriptional and post-transcriptional expression of gamma-glutamylcysteine synthetase by diethylmaleate. Radiation Research, 147, 592-597.
    • (1997) Radiation Research , vol.147 , pp. 592-597
    • Sekhar, K.R.1    Long, M.2    Long, J.3    Xu, Z.-Q.4    Summar, M.L.5    Freeman, M.L.6
  • 15
    • 2642671110 scopus 로고    scopus 로고
    • An electrophile responsive element (EpRE) regulates β-naphthoflavone induction of the human γ-glutamylcysteine synthetase regulatory subunit gene
    • H.R. Moinova and R.T. Mulcahy (1998) An electrophile responsive element (EpRE) regulates β-naphthoflavone induction of the human γ-glutamylcysteine synthetase regulatory subunit gene. The Journal of Biological Chemistry, 273, 14683-14689.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 14683-14689
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 16
    • 0032535320 scopus 로고    scopus 로고
    • Inducible expression of the γ-glutamylcysteine synthetase light subunit by t-butylhydroquinone in HepG2 cells is not dependent on an antioxidant-responsive element
    • D.C. Galloway and L.I. McLellan (1998) Inducible expression of the γ-glutamylcysteine synthetase light subunit by t-butylhydroquinone in HepG2 cells is not dependent on an antioxidant-responsive element. Biochemical Journal, 336, 535-539.
    • (1998) Biochemical Journal , vol.336 , pp. 535-539
    • Galloway, D.C.1    McLellan, L.I.2
  • 18
    • 17144465167 scopus 로고    scopus 로고
    • ATP-dependent transport of glutathione S-conjugates by the multidrug resistance protein MRP1 and its apical isoform MRP2
    • D. Keppler, I. Leier, G. Jedlitschky and J. König (1998) ATP-dependent transport of glutathione S-conjugates by the multidrug resistance protein MRP1 and its apical isoform MRP2. Chemico-Biological Interactions, 111-112, 153-161.
    • (1998) Chemico-Biological Interactions , vol.111-112 , pp. 153-161
    • Keppler, D.1    Leier, I.2    Jedlitschky, G.3    König, J.4
  • 19
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • G.C. Mills (1957) Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. The Journal of Biological Chemistry, 229, 189-197.
    • (1957) The Journal of Biological Chemistry , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 20
  • 23
    • 0031656463 scopus 로고    scopus 로고
    • Glutathione peroxidase protects mice from viral-induced myocarditis
    • M.A. Beck, R.S. Esworthy, Y.-S. Ho and F.-F. Chu (1998) Glutathione peroxidase protects mice from viral-induced myocarditis. The FASEB Journal, 12, 1143-1149.
    • (1998) The FASEB Journal , vol.12 , pp. 1143-1149
    • Beck, M.A.1    Esworthy, R.S.2    Ho, Y.-S.3    Chu, F.-F.4
  • 24
    • 0030883586 scopus 로고    scopus 로고
    • Hyperoxia, unlike phorbol ester, induces glutathione peroxidase through a protein kinase C-independent mechanism
    • L. Jornot and A.F. Junod (1997) Hyperoxia, unlike phorbol ester, induces glutathione peroxidase through a protein kinase C-independent mechanism. Biochemical Journal, 326, 117-123.
    • (1997) Biochemical Journal , vol.326 , pp. 117-123
    • Jornot, L.1    Junod, A.F.2
  • 27
  • 29
    • 0027536023 scopus 로고
    • Expression, characterisation, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • F.-F. Chu, J.H. Doroshow and R.S. Esworthy (1993) Expression, characterisation, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. The Journal of Biological Chemistry, 268, 2571-2576.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 2571-2576
    • Chu, F.-F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 30
    • 0031879339 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine
    • R.S. Esworthy, K.M. Swiderek, Y.-S. Ho and F.-F. Chu (1998) Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine. Biochimica et Biophysica Acta, 1381, 213-226.
    • (1998) Biochimica et Biophysica Acta , vol.1381 , pp. 213-226
    • Esworthy, R.S.1    Swiderek, K.M.2    Ho, Y.-S.3    Chu, F.-F.4
  • 32
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • M. Björnstedt, J. Xue, W. Huang, B. Åkesson and A. Holmgren (1994) The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. The Journal of Biological Chemistry, 269, 29382-29384.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 29382-29384
    • Björnstedt, M.1    Xue, J.2    Huang, W.3    Åkesson, B.4    Holmgren, A.5
  • 35
    • 0032127126 scopus 로고    scopus 로고
    • The majority of human glutathione peroxidase type 5 (GPXS) transcripts are incorrectly spliced: Implications for the role of GPX5 in the male reproductive tract
    • L. Hall, K. Williams, A.C.F. Perry, J. Frayne and J.A. Jury (1998) The majority of human glutathione peroxidase type 5 (GPXS) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract. Biochemical Journal, 333, 5-9.
    • (1998) Biochemical Journal , vol.333 , pp. 5-9
    • Hall, L.1    Williams, K.2    Perry, A.C.F.3    Frayne, J.4    Jury, J.A.5
  • 37
    • 0030803334 scopus 로고    scopus 로고
    • A novel type of glutathione peroxidase: Expression and regulation during wound repair
    • B. Munz, S. Frank, G. Hübner, E. Olsen and S. Werner (1997) A novel type of glutathione peroxidase: expression and regulation during wound repair. Biochemical Journal, 326, 579-585.
    • (1997) Biochemical Journal , vol.326 , pp. 579-585
    • Munz, B.1    Frank, S.2    Hübner, G.3    Olsen, E.4    Werner, S.5
  • 38
    • 0025301491 scopus 로고
    • Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body
    • H. Shichi and J.C. Demar (1990) Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body. Experimental Eye Research, 50, 513-520.
    • (1990) Experimental Eye Research , vol.50 , pp. 513-520
    • Shichi, H.1    Demar, J.C.2
  • 39
  • 40
    • 0032513056 scopus 로고    scopus 로고
    • Characterisation of a mammalian peroxiredoxin that contains one conserved cysteine
    • S.W. Kang, I.C. Baines and S.G. Rhee (1998) Characterisation of a mammalian peroxiredoxin that contains one conserved cysteine. The Journal of Biological Chemistry, 273, 6303-6311.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 41
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • J.D. Hayes and D.J. Pulford (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Critical Reviews in Biochemistry and Molecular Biology, 30, 445-600.
    • (1995) Critical Reviews in Biochemistry and Molecular Biology , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 42
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • R.N. Armstrong (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases. Chemical Research Toxicology, 10, 2-18.
    • (1997) Chemical Research Toxicology , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 43
    • 0026093495 scopus 로고
    • An overview of the relationship between oxidative stress and chemical carcinogenesis
    • M.A. Trush and T.W. Kensler (1991) An overview of the relationship between oxidative stress and chemical carcinogenesis. Free Radical Biology and Medicine, 10, 201-209.
    • (1991) Free Radical Biology and Medicine , vol.10 , pp. 201-209
    • Trush, M.A.1    Kensler, T.W.2
  • 44
    • 0024548960 scopus 로고
    • Amino acid substitutions in the human glutathione S-transferases confer different specificities in the prostaglandin endoperoxide conversion pathway
    • J.R. Burgess, N.-W.I. Chow, C.C. Reddy and C.-P.D. Tu (1989) Amino acid substitutions in the human glutathione S-transferases confer different specificities in the prostaglandin endoperoxide conversion pathway. Biochemical and Biophysical Research Communications, 158, 497-502.
    • (1989) Biochemical and Biophysical Research Communications , vol.158 , pp. 497-502
    • Burgess, J.R.1    Chow, N.-W.I.2    Reddy, C.C.3    Tu, C.-P.D.4
  • 46
    • 0030923439 scopus 로고    scopus 로고
    • Identification and characterization of a novel microsomal enzyme with glutathione-dependent rransferase and peroxidase activities
    • P.-J. Jakobsson, J.A. Mancini D. Riendeau and A.W. Ford-Hutchinson (1997) Identification and characterization of a novel microsomal enzyme with glutathione-dependent rransferase and peroxidase activities. The Journal of Biological Chemistry, 272, 22934-22939.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 22934-22939
    • Jakobsson, P.-J.1    Mancini, J.A.2    Riendeau, D.3    Ford-Hutchinson, A.W.4
  • 47
    • 0024265036 scopus 로고
    • Intracellular binding and transport of hormones and xenobiotics by glutathione S-transferases
    • I. Listowsky, M. Abramovitz, H. Homma and Y. Niitsu (1988) Intracellular binding and transport of hormones and xenobiotics by glutathione S-transferases. Drug Metabolism Reviews, 19, 305-318.
    • (1988) Drug Metabolism Reviews , vol.19 , pp. 305-318
    • Listowsky, I.1    Abramovitz, M.2    Homma, H.3    Niitsu, Y.4
  • 51
    • 0023445343 scopus 로고
    • Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases
    • U.H. Danielson, H. Esterbauer and B. Mannervik (1987) Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases. Biochemical Journal, 247, 707-713.
    • (1987) Biochemical Journal , vol.247 , pp. 707-713
    • Danielson, U.H.1    Esterbauer, H.2    Mannervik, B.3
  • 52
    • 0032519517 scopus 로고    scopus 로고
    • Human glutathione transferase A4-4: An alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation
    • I. Hubatsch, M. Ridderström and B. Mannervik (1998) Human glutathione transferase A4-4: an Alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochemical Journal, 330, 175-179.
    • (1998) Biochemical Journal , vol.330 , pp. 175-179
    • Hubatsch, I.1    Ridderström, M.2    Mannervik, B.3
  • 53
    • 0002626623 scopus 로고
    • Biological activities of 4-hydroxyalkenals
    • (Ed. H. Sies), Academic Press, London and New York
    • H. Zollner, R.J. Schaur and H. Esterbauer (1991) Biological activities of 4-hydroxyalkenals. In Oxidative Stress: Oxidants and Antioxidants (Ed. H. Sies), Academic Press, London and New York, pp. 337-369.
    • (1991) Oxidative Stress: Oxidants and Antioxidants , pp. 337-369
    • Zollner, H.1    Schaur, R.J.2    Esterbauer, H.3
  • 54
    • 0028797410 scopus 로고
    • Mercapturic acid conjugates as urinary end metabolites of the lipid-peroxidation product 4-hydroxy-2-nonenal in the rat
    • J. Alary, F. Bravais J.-P. Cravedi, L. Debrauwer, D. Rao and G. Bories (1995) Mercapturic acid conjugates as urinary end metabolites of the lipid-peroxidation product 4-hydroxy-2-nonenal in the rat. Chemical Research in Toxicology, 8, 34-39.
    • (1995) Chemical Research in Toxicology , vol.8 , pp. 34-39
    • Alary, J.1    Bravais, F.2    Cravedi, J.-P.3    Debrauwer, L.4    Rao, D.5    Bories, G.6
  • 55
    • 0020466982 scopus 로고
    • 5α,6α-Epoxy-cholestan-3β-ol (cholesterol α-oxide): A specific substrate for rat liver glutathione transferase B
    • D.J. Meyer and B. Ketterer (1982) 5α,6α-Epoxy-cholestan-3β-ol (cholesterol α-oxide): a specific substrate for rat liver glutathione transferase B. FEBS Letters, 150, 499-502.
    • (1982) FEBS Letters , vol.150 , pp. 499-502
    • Meyer, D.J.1    Ketterer, B.2
  • 56
    • 0025044866 scopus 로고
    • Cholesterol epoxides: Formation and measurement
    • G.A.S. Ansari and L.L. Smith (1990) Cholesterol epoxides: formation and measurement. Methods in Enzymology, 186, 438-443.
    • (1990) Methods in Enzymology , vol.186 , pp. 438-443
    • Ansari, G.A.S.1    Smith, L.L.2
  • 57
    • 0028036292 scopus 로고
    • Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
    • K. Berhane, M. Widersten, Å. Engström, J.W. Kozarich and B. Mannervik (1994) Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proceedings of the National Academy of Sciences USA, 91, 1480-1484.
    • (1994) Proceedings of the National Academy of Sciences USA , vol.91 , pp. 1480-1484
    • Berhane, K.1    Widersten, M.2    Engström, Å.3    Kozarich, J.W.4    Mannervik, B.5
  • 60
    • 0031053981 scopus 로고    scopus 로고
    • Subunit Ya-specific glutathione peroxidase activity towards cholesterol 7-hydroperoxides of glutathione S-transferases in cytosols from rat liver and skin
    • A. Hiratsuka, H. Yamane, S. Yamazaki, N. Ozawa and T. Watabe (1997) Subunit Ya-specific glutathione peroxidase activity towards cholesterol 7-hydroperoxides of glutathione S-transferases in cytosols from rat liver and skin. The Journal of Biological Chemistry, 272, 4763-4769.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 4763-4769
    • Hiratsuka, A.1    Yamane, H.2    Yamazaki, S.3    Ozawa, N.4    Watabe, T.5
  • 64
    • 0032524233 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferases
    • R. Hurst, Y. Bao, P. Jemth, B. Mannervik and G. Williamson (1998) Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferases. Biochemical Journal, 332, 97-100.
    • (1998) Biochemical Journal , vol.332 , pp. 97-100
    • Hurst, R.1    Bao, Y.2    Jemth, P.3    Mannervik, B.4    Williamson, G.5
  • 65
    • 0027051610 scopus 로고
    • Glutathione S-transferases of human lung: Characterization and evaluation of the protective role of the α-class isozymes against lipid peroxidation
    • S.S. Singhal, M. Saxena, H. Ahmad, S. Awasthi, A.K. Haque and Y.C. Awasthi (1992) Glutathione S-transferases of human lung: characterization and evaluation of the protective role of the α-class isozymes against lipid peroxidation. Archives of Biochemistry and Biophysics, 299, 232-241.
    • (1992) Archives of Biochemistry and Biophysics , vol.299 , pp. 232-241
    • Singhal, S.S.1    Saxena, M.2    Ahmad, H.3    Awasthi, S.4    Haque, A.K.5    Awasthi, Y.C.6
  • 66
    • 0027276544 scopus 로고
    • Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation
    • E. Mosialou, G. Ekström, A.E.P. Adang and R. Morgenstern (1993) Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation. Biochemical Pharmacology, 45, 1645-1651.
    • (1993) Biochemical Pharmacology , vol.45 , pp. 1645-1651
    • Mosialou, E.1    Ekström, G.2    Adang, A.E.P.3    Morgenstern, R.4
  • 67
    • 0021879561 scopus 로고
    • Selenium and drug metabolism - III. Relation of glutathione-peroxidase and other hepatic enzyme modulations to dietary supplements
    • R. Reiter and A. Wendel (1985) Selenium and drug metabolism - III. Relation of glutathione-peroxidase and other hepatic enzyme modulations to dietary supplements. Biochemical Pharmacology, 34, 2287-2290.
    • (1985) Biochemical Pharmacology , vol.34 , pp. 2287-2290
    • Reiter, R.1    Wendel, A.2
  • 68
    • 0030767451 scopus 로고    scopus 로고
    • 1 in the rat is associated with the hepatic expression of an aldo-keto reductase and a glutathione S-transferase subunit that metabolise the mycotoxin
    • 1 in the rat is associated with the hepatic expression of an aldo-keto reductase and a glutathione S-transferase subunit that metabolise the mycotoxin. Cancer Research, 57, 4257-4266.
    • (1997) Cancer Research , vol.57 , pp. 4257-4266
    • McLeod, R.1    Ellis, E.M.2    Arthur, J.R.3    Neal, G.E.4    Judah, D.J.5    Manson, M.M.6    Hayes, J.D.7
  • 69
    • 0023574890 scopus 로고
    • Electron transfer from protein to DNA in irradiated chromatin
    • P.M. Cullis, G.D.D. Jones, M.C.R. Symons and J.S. Lea (1987) Electron transfer from protein to DNA in irradiated chromatin. Nature, 330, 773-774.
    • (1987) Nature , vol.330 , pp. 773-774
    • Cullis, P.M.1    Jones, G.D.D.2    Symons, M.C.R.3    Lea, J.S.4
  • 70
    • 0030786577 scopus 로고    scopus 로고
    • Reduction of thymine hydroperoxide by phospholipid hydroperoxide glutathione peroxide and glutathione transferases
    • Y. Bao, P. Jemth, B. Mannervik and G. Williamson (1997) Reduction of thymine hydroperoxide by phospholipid hydroperoxide glutathione peroxide and glutathione transferases. FEBS Letters, 410, 210-212.
    • (1997) FEBS Letters , vol.410 , pp. 210-212
    • Bao, Y.1    Jemth, P.2    Mannervik, B.3    Williamson, G.4
  • 71
    • 0029922601 scopus 로고    scopus 로고
    • Role of HAP1 protein in repair of oxidative DNA damage and regulation of transcription factors
    • G. Barzilay, L.J. Walker, D.G. Rothwell and I.D. Hickson (1996) Role of HAP1 protein in repair of oxidative DNA damage and regulation of transcription factors. British Journal of Cancer, 74 (Suppl. XXVII), S145-S150.
    • (1996) British Journal of Cancer , vol.74 , Issue.SUPPL. XXVII
    • Barzilay, G.1    Walker, L.J.2    Rothwell, D.G.3    Hickson, I.D.4
  • 72
    • 0027506460 scopus 로고
    • Escape from redox regulation enhances the transforming activity of Fos
    • H. Okuno, A. Akahori, H. Sato, S. Xanthoudakis, T. Curran and H. Iba (1993) Escape from redox regulation enhances the transforming activity of Fos. Oncogene, 8, 695-701.
    • (1993) Oncogene , vol.8 , pp. 695-701
    • Okuno, H.1    Akahori, A.2    Sato, H.3    Xanthoudakis, S.4    Curran, T.5    Iba, H.6
  • 74
    • 0030967073 scopus 로고    scopus 로고
    • Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes
    • S. Baez, J. Segura-Aguilar, M. Widersten, A.-S. Johansson and B. Mannervik (1997) Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes. Biochemical Journal, 324, 25-28.
    • (1997) Biochemical Journal , vol.324 , pp. 25-28
    • Baez, S.1    Segura-Aguilar, J.2    Widersten, M.3    Johansson, A.-S.4    Mannervik, B.5
  • 76
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG - A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • P.-J. Jakobsson, R. Morgenstern, J. Mancini, A. Ford-Hutchinson and B. Persson (1999) Common structural features of MAPEG - a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Science, 8, 1-4.
    • (1999) Protein Science , vol.8 , pp. 1-4
    • Jakobsson, P.-J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 78
    • 0032031503 scopus 로고    scopus 로고
    • Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4
    • P.G. Board (1998) Identification of cDNAs encoding two human Alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. Biochemical Journal, 330, 827-831.
    • (1998) Biochemical Journal , vol.330 , pp. 827-831
    • Board, P.G.1
  • 79
    • 0032374046 scopus 로고    scopus 로고
    • Genomic organization, 5′-flanking region and chromosomal localization of the human glutathione transferase A4 gene
    • F. Desmots, C. Rauch, C. Henry, A. Guillouzo and F. Morel (1998) Genomic organization, 5′-flanking region and chromosomal localization of the human glutathione transferase A4 gene. Biochemical Journal, 336, 437-442.
    • (1998) Biochemical Journal , vol.336 , pp. 437-442
    • Desmots, F.1    Rauch, C.2    Henry, C.3    Guillouzo, A.4    Morel, F.5
  • 80
    • 0032488893 scopus 로고    scopus 로고
    • Characterization of the human class Mu-glutathione-S-transferase gene-cluster and the GSTM1 deletion
    • S.-j. Xu, Y.-p. Wang, B. Roe and W.R. Pearson (1998) Characterization of the human class Mu-glutathione-S-transferase gene-cluster and the GSTM1 deletion. Journal of Biological Chemistry, 273, 3517-3527.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 3517-3527
    • Xu, S.-J.1    Wang, Y.-P.2    Roe, B.3    Pearson, W.R.4
  • 81
    • 0031558812 scopus 로고    scopus 로고
    • Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola-hepatica glutathione S-transferase
    • J. Rossjohn, S.C. Feil, M.C.J. Wilce, J.L. Sexton, T.W. Spithill and M.W. Parker (1997) Crystallization, structural determination and analysis of a novel parasite vaccine candidate: fasciola-hepatica glutathione S-transferase. Journal of Molecular Biology, 273, 857-872.
    • (1997) Journal of Molecular Biology , vol.273 , pp. 857-872
    • Rossjohn, J.1    Feil, S.C.2    Wilce, M.C.J.3    Sexton, J.L.4    Spithill, T.W.5    Parker, M.W.6
  • 82
    • 0032540336 scopus 로고    scopus 로고
    • Rationale for reclassification of a distinctive subdivision of mammalian class Mu glutathione S-transferases that are primarily expressed in testis
    • J.D. Rowe, Y.V. Patskovsky, L.N. Patskovska, E. Novikova and I. Listowsky (1998) Rationale for reclassification of a distinctive subdivision of mammalian class Mu glutathione S-transferases that are primarily expressed in testis. The Journal of Biological Chemistry, 273, 9593-9601.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 9593-9601
    • Rowe, J.D.1    Patskovsky, Y.V.2    Patskovska, L.N.3    Novikova, E.4    Listowsky, I.5
  • 84
    • 0032496408 scopus 로고    scopus 로고
    • Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105
    • A.-S. Johansson, G. Stenberg, M. Widersten and B. Mannervik (1998) Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105. Journal of Molecular Biology, 278, 687-698.
    • (1998) Journal of Molecular Biology , vol.278 , pp. 687-698
    • Johansson, A.-S.1    Stenberg, G.2    Widersten, M.3    Mannervik, B.4
  • 89
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • P.G. Board, R.T. Baker, G. Chelvanayagam and L.S. Jermiin (1997) Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochemical Journal, 328, 929-935.
    • (1997) Biochemical Journal , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 90
    • 0029854518 scopus 로고    scopus 로고
    • Glutathione S-transferase class Kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue
    • S.E. Pemble, A.F. Wardle and J.B. Taylor (1996) Glutathione S-transferase class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochemical Journal, 319, 749-754.
    • (1996) Biochemical Journal , vol.319 , pp. 749-754
    • Pemble, S.E.1    Wardle, A.F.2    Taylor, J.B.3
  • 91
    • 0033582482 scopus 로고    scopus 로고
    • The cloning and characterization of a new stress response protein. A mammalian member of a family of 9 class glutathione S-transferase-like proteins
    • R. Kodym, P. Calkins and M. Story (1999) The cloning and characterization of a new stress response protein. A mammalian member of a family of 9 class glutathione S-transferase-like proteins. The Journal of Biological Chemistry, 274, 5131-5137.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 5131-5137
    • Kodym, R.1    Calkins, P.2    Story, M.3
  • 92
    • 0032921649 scopus 로고    scopus 로고
    • Panning for genes - A visual strategy for identifying novel gene orthologs and paralogs
    • J.D. Retief, K.R. Lynch and W.R. Pearson (1999) Panning for genes - a visual strategy for identifying novel gene orthologs and paralogs. Genome Research, 9, 373-382.
    • (1999) Genome Research , vol.9 , pp. 373-382
    • Retief, J.D.1    Lynch, K.R.2    Pearson, W.R.3
  • 93
    • 0027330057 scopus 로고
    • MIF proteins are theta-class glutathione S-transferase homologs
    • F.A. Blocki, L.B.M. Ellis and L.P. Wackett (1993) MIF proteins are theta-class glutathione S-transferase homologs. Protein Science, 2, 2095-2102.
    • (1993) Protein Science , vol.2 , pp. 2095-2102
    • Blocki, F.A.1    Ellis, L.B.M.2    Wackett, L.P.3
  • 94
    • 0030732390 scopus 로고    scopus 로고
    • Plant glutathione S-transferases, a tale of Theta and Tau
    • F. Droog (1997) Plant glutathione S-transferases, a tale of Theta and Tau. Journal of Plant Growth Regulation, 16, 95-107.
    • (1997) Journal of Plant Growth Regulation , vol.16 , pp. 95-107
    • Droog, F.1
  • 96
    • 0027211012 scopus 로고
    • The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster
    • Y.-P.S. Toung, T.-s. Hsieh and C.-P.D. Tu (1993) The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster. The Journal of Biological Chemistry, 268, 9737-9746.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 9737-9746
    • Toung, Y.-P.S.1    Hsieh, T.-S.2    Tu, C.-P.D.3
  • 97
    • 0028112999 scopus 로고
    • Biochemical characterization of Drosophila glutathione S-transferases D1 and D21
    • A.M. Tang and C.-P.D. Tu (1994) Biochemical characterization of Drosophila glutathione S-transferases D1 and D21. The Journal of Biological Chemistry, 269, 27876-27884.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 27876-27884
    • Tang, A.M.1    Tu, C.-P.D.2
  • 98
    • 0032526942 scopus 로고    scopus 로고
    • A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
    • J. Rossjohn, G. Polekhina, S.C. Feil, N. Allocati, M. Masulli, C. Di Ilio and M.W. Parker (1998) A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure, 6, 721-734.
    • (1998) Structure , vol.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Allocati, N.4    Masulli, M.5    Di Ilio, C.6    Parker, M.W.7
  • 103
    • 0029886863 scopus 로고    scopus 로고
    • Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35
    • J.F. Penrose, J. Spector, M. Baldasaro, K. Xu, J. Boyce, J.P. Arm, K.F. Austen and B.K. Lam (1996) Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35. The Journal of Biological Chemistry, 271, 11356-11361.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 11356-11361
    • Penrose, J.F.1    Spector, J.2    Baldasaro, M.3    Xu, K.4    Boyce, J.5    Arm, J.P.6    Austen, K.F.7    Lam, B.K.8
  • 106
    • 0028262418 scopus 로고
    • Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
    • G. Ricci, A.M. Caccuri, M. Lo Bello, A. Pastore, F. Piemonte and G. Federici (1994) Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Analytical Biochemistry, 218, 463-465.
    • (1994) Analytical Biochemistry , vol.218 , pp. 463-465
    • Ricci, G.1    Caccuri, A.M.2    Lo Bello, M.3    Pastore, A.4    Piemonte, F.5    Federici, G.6
  • 107
    • 0029956983 scopus 로고    scopus 로고
    • Glutathione S-transferase A1-1 catalyzed conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons with glutathione
    • B. Jernström, M. Funk, H. Frank, B. Mannervik and A. Seidel (1996) Glutathione S-transferase A1-1 catalyzed conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons with glutathione. Carcinogenesis, 17, 1491-1498.
    • (1996) Carcinogenesis , vol.17 , pp. 1491-1498
    • Jernström, B.1    Funk, M.2    Frank, H.3    Mannervik, B.4    Seidel, A.5
  • 109
    • 0030822939 scopus 로고    scopus 로고
    • Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1
    • K. Sundberg, M. Wildersten, A. Seidel, B. Mannervik and B. Jernström (1997) Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1. Chemical Research in Toxicology, 10, 1221-1227.
    • (1997) Chemical Research in Toxicology , vol.10 , pp. 1221-1227
    • Sundberg, K.1    Wildersten, M.2    Seidel, A.3    Mannervik, B.4    Jernström, B.5
  • 110
    • 0030778937 scopus 로고    scopus 로고
    • Evidence that human class Theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GSTT1-1 with that of classes Alpha, Mu and Pi GST in human
    • P.J. Sherratt, D.J. Pulford, D.J. Harrison, T. Green and J.D. Hayes (1997) Evidence that human class Theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GSTT1-1 with that of classes Alpha, Mu and Pi GST in human. Biochemical Journal, 326, 837-846.
    • (1997) Biochemical Journal , vol.326 , pp. 837-846
    • Sherratt, P.J.1    Pulford, D.J.2    Harrison, D.J.3    Green, T.4    Hayes, J.D.5
  • 111
    • 0031574268 scopus 로고    scopus 로고
    • Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme
    • P. Jemth and B. Mannervik (1997) Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Archives of Biochemistry and Biophysics, 348, 247-254.
    • (1997) Archives of Biochemistry and Biophysics , vol.348 , pp. 247-254
    • Jemth, P.1    Mannervik, B.2
  • 112
    • 0029853099 scopus 로고    scopus 로고
    • Mutagenesis of the active-site of the human Theta-class glutathione transferase GSTT2-2 - Catalysis with different substrates involves different residues
    • K.-L. Tan, G. Chelvanayagam, M.W. Parker and P.G. Board (1996) Mutagenesis of the active-site of the human Theta-class glutathione transferase GSTT2-2 - catalysis with different substrates involves different residues. Biochemical Journal, 319, 315-321.
    • (1996) Biochemical Journal , vol.319 , pp. 315-321
    • Tan, K.-L.1    Chelvanayagam, G.2    Parker, M.W.3    Board, P.G.4
  • 113
    • 0029009655 scopus 로고
    • A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2
    • K.A. Marrs, M.R. Alfenito, A.M. Lloyd and V. Walbot (1995) A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2. Nature, 375, 397-400.
    • (1995) Nature , vol.375 , pp. 397-400
    • Marrs, K.A.1    Alfenito, M.R.2    Lloyd, A.M.3    Walbot, V.4
  • 114
    • 0032522741 scopus 로고    scopus 로고
    • Glutathione transferase Zeta catalyzes the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid
    • Z. Tong, P.G. Board and M.W. Anders (1998) Glutathione transferase Zeta catalyzes the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid. Biochemical Journal, 331, 371-374.
    • (1998) Biochemical Journal , vol.331 , pp. 371-374
    • Tong, Z.1    Board, P.G.2    Anders, M.W.3
  • 115
    • 0040942636 scopus 로고    scopus 로고
    • Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue
    • J.M. Fernández-Cañón and M.A. Peñalva (1998) Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue. The Journal of Biological Chemistry, 273, 329-337.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 329-337
    • Fernández-Cañón, J.M.1    Peñalva, M.A.2
  • 116
    • 0031741776 scopus 로고    scopus 로고
    • Glutathione transferase Zeta-catalysed biotransformation of dichloroacetic acid and other α-haloacids
    • Z. Tong, P.G. Board and M.W. Anders (1998) Glutathione transferase Zeta-catalysed biotransformation of dichloroacetic acid and other α-haloacids. Chemical Research in Toxicology, 11, 1332-1338.
    • (1998) Chemical Research in Toxicology , vol.11 , pp. 1332-1338
    • Tong, Z.1    Board, P.G.2    Anders, M.W.3
  • 117
    • 0032437157 scopus 로고    scopus 로고
    • Characterization and chromosomal location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase
    • A.C. Blackburn, E. Woollatt, G.R. Sutherland and P.G. Board (1999) Characterization and chromosomal location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase. Cytogenetics and Cell Genetics, 83, 109-114.
    • (1999) Cytogenetics and Cell Genetics , vol.83 , pp. 109-114
    • Blackburn, A.C.1    Woollatt, E.2    Sutherland, G.R.3    Board, P.G.4
  • 118
    • 0031104709 scopus 로고    scopus 로고
    • Increased resistance to oxidative stress in transfected cultured-cells overexpressing glutathione S-transferase mgsta4-4
    • L. Zimniak, S. Awasthi, S.K. Srivastava and P. Zimniak (1997) Increased resistance to oxidative stress in transfected cultured-cells overexpressing glutathione S-transferase mgsta4-4. Toxicology and Applied Pharmacology, 143, 221-229.
    • (1997) Toxicology and Applied Pharmacology , vol.143 , pp. 221-229
    • Zimniak, L.1    Awasthi, S.2    Srivastava, S.K.3    Zimniak, P.4
  • 119
    • 0014232104 scopus 로고
    • The inhibitory effect of reduced glutathione on the lipid peroxidation of the microsomal fraction and mitochondria
    • B.O. Christophersen (1968) The inhibitory effect of reduced glutathione on the lipid peroxidation of the microsomal fraction and mitochondria. Biochemical Journal, 106, 515-522.
    • (1968) Biochemical Journal , vol.106 , pp. 515-522
    • Christophersen, B.O.1
  • 121
    • 0032617027 scopus 로고    scopus 로고
    • Cellular response to cancer chemopreventive agents: Contribution of the antioxidant responsive element to the adaptive response to oxidative and chemical stress
    • Cellular Responses to Stress (Eds. C.P. Downes, C.R. Wolf and D.P. Lane) Portland Press, London
    • J.D. Hayes, E.M. Ellis, G.E. Neal, D.J. Harrison and M.M. Manson (1999) Cellular response to cancer chemopreventive agents: contribution of the antioxidant responsive element to the adaptive response to oxidative and chemical stress. In Cellular Responses to Stress (Eds. C.P. Downes, C.R. Wolf and D.P. Lane) Biochemical Society Symposium, 64, Portland Press, London, pp. 141-168.
    • (1999) Biochemical Society Symposium , vol.64 , pp. 141-168
    • Hayes, J.D.1    Ellis, E.M.2    Neal, G.E.3    Harrison, D.J.4    Manson, M.M.5
  • 122
    • 0031577332 scopus 로고    scopus 로고
    • Cellular response to the redox active lipid peroxidation products: Induction of glutathione S-transferase P by 4-hydroxy-2-nonenal
    • A. Fukuda, Y. Nakamura, H. Ohigashi, T. Osawa and K. Uchida (1997) Cellular response to the redox active lipid peroxidation products: induction of glutathione S-transferase P by 4-hydroxy-2-nonenal. Biochemical and Biophysical Research Communications, 236, 505-509.
    • (1997) Biochemical and Biophysical Research Communications , vol.236 , pp. 505-509
    • Fukuda, A.1    Nakamura, Y.2    Ohigashi, H.3    Osawa, T.4    Uchida, K.5
  • 123
    • 85069429082 scopus 로고    scopus 로고
    • Rat skin glutathione S-transferases: Age-dependent accumulation of the toxic steroids, cholesterol 7-hydroperoxides, by deficiency of A1-2 and A1-3 and marked expression of A4-4 by UVB irradiation in the skin
    • Rome
    • T. Watabe, A. Hiratsuka, H. Yamane, S. Yamazaki and N. Ozawa (1997) Rat skin glutathione S-transferases: age-dependent accumulation of the toxic steroids, cholesterol 7-hydroperoxides, by deficiency of A1-2 and A1-3 and marked expression of A4-4 by UVB irradiation in the skin. International Workshop on Glutathione Transferases, Rome, O16.
    • (1997) International Workshop on Glutathione Transferases
    • Watabe, T.1    Hiratsuka, A.2    Yamane, H.3    Yamazaki, S.4    Ozawa, N.5
  • 125
    • 0021138883 scopus 로고
    • On the stoichiometry of the oxidase of monooxygenase reactions catalysed by liver microsomal cytochrome P-450. Products of oxygen reduction
    • L.D. Gorsky, D.R. Koop and M.J. Coon (1984) On the stoichiometry of the oxidase of monooxygenase reactions catalysed by liver microsomal cytochrome P-450. Products of oxygen reduction. The Journal of Biological Chemistry, 259, 6812-6817.
    • (1984) The Journal of Biological Chemistry , vol.259 , pp. 6812-6817
    • Gorsky, L.D.1    Koop, D.R.2    Coon, M.J.3
  • 126
    • 0024386439 scopus 로고
    • Cytochrome P-450 and oxygen toxicity. Oxygen-dependent induction of ethanol-inducible cytochrome P-450 (IIE1) in rat liver and lung
    • N. Tindberg and M. Ingelman-Sundberg (1989) Cytochrome P-450 and oxygen toxicity. Oxygen-dependent induction of ethanol-inducible cytochrome P-450 (IIE1) in rat liver and lung. Biochemistry, 28, 4499-4504.
    • (1989) Biochemistry , vol.28 , pp. 4499-4504
    • Tindberg, N.1    Ingelman-Sundberg, M.2
  • 127
    • 0030006304 scopus 로고    scopus 로고
    • Induction of cytochrome P4501A1 by 2,3,7,8-tetrachlorodibenzo-p-dioxin or indolo(3,2-b)carbazole is associated with oxidative DNA damage
    • J.-Y. K. Park, M.K. Shigenaga and B.N. Ames (1996) Induction of cytochrome P4501A1 by 2,3,7,8-tetrachlorodibenzo-p-dioxin or indolo(3,2-b)carbazole is associated with oxidative DNA damage. Proceedings of the National Academy of Sciences USA, 93, 2322-2327.
    • (1996) Proceedings of the National Academy of Sciences USA , vol.93 , pp. 2322-2327
    • Park, J.-Y.K.1    Shigenaga, M.K.2    Ames, B.N.3
  • 128
    • 0344915418 scopus 로고
    • Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis
    • P. Talalay, M.J. De Long and H.J. Prochaska (1988) Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proceedings of the National Academy of Sciences USA, 85, 8261-8265.
    • (1988) Proceedings of the National Academy of Sciences USA , vol.85 , pp. 8261-8265
    • Talalay, P.1    De Long, M.J.2    Prochaska, H.J.3
  • 129
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • T.H. Rushmore, M.R. Morton and C.B. Pickett (1991) The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. The Journal of Biological Chemistry, 266, 11632-11639.
    • (1991) The Journal of Biological Chemistry , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 130
    • 0028364075 scopus 로고
    • Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate
    • T. Nguyen, T.H. Rushmore and C.B. Pickett (1994) Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate. The Journal of Biological Chemistry, 269, 13656-13662.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 13656-13662
    • Nguyen, T.1    Rushmore, T.H.2    Pickett, C.B.3
  • 134
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents
    • A. Knebel, H.J. Rahmsdorf, A. Ullrich and P. Herrlich (1996) Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. The EMBO Journal, 15, 5314-5325.
    • (1996) The EMBO Journal , vol.15 , pp. 5314-5325
    • Knebel, A.1    Rahmsdorf, H.J.2    Ullrich, A.3    Herrlich, P.4
  • 135
    • 0029953164 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate, a natural chemopreventive agent, activates c-Jun N-terminal kinase 1
    • R. Yu, J.-J. Jiao, J.-L. Duh, T.-H. Tan and A.-N.T. Kong (1996) Phenethyl isothiocyanate, a natural chemopreventive agent, activates c-Jun N-terminal kinase 1. Cancer Research, 56, 2954-2959.
    • (1996) Cancer Research , vol.56 , pp. 2954-2959
    • Yu, R.1    Jiao, J.-J.2    Duh, J.-L.3    Tan, T.-H.4    Kong, A.-N.T.5
  • 136
    • 0031408813 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases by green tea polyphenols: Potential signaling pathways in the regulation of antioxidant responsive element-mediated phase II enzyme gene expression
    • R. Yu, J.-J. Jiao, J.-L. Duh, K. Gudehithlu, T.-H. Tan and A.-N.T. Kong (1997) Activation of mitogen-activated protein kinases by green tea polyphenols: potential signaling pathways in the regulation of antioxidant responsive element-mediated phase II enzyme gene expression. Carcinogenesis, 18, 451-456.
    • (1997) Carcinogenesis , vol.18 , pp. 451-456
    • Yu, R.1    Jiao, J.-J.2    Duh, J.-L.3    Gudehithlu, K.4    Tan, T.-H.5    Kong, A.-N.T.6
  • 137
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • K. Itoh, N. Wakabayashi, Y. Katoh, T. Ishii, K. Igarashi, J.D. Engel and M. Yamamoto (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes and Development, 13, 76-86.
    • (1999) Genes and Development , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 138
    • 0026631529 scopus 로고
    • Regulation of rat glutathione S-transferase Ya subunit gene expression. DNA-protein interaction at the antioxidant responsive element
    • T. Nguyen and C.B. Pickett (1992) Regulation of rat glutathione S-transferase Ya subunit gene expression. DNA-protein interaction at the antioxidant responsive element. The Journal of Biological Chemistry, 267, 13535-13539.
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 13535-13539
    • Nguyen, T.1    Pickett, C.B.2
  • 139
    • 0029758241 scopus 로고    scopus 로고
    • The rat liver glutathione S-transferase Ya subunit gene: Characterization of the binding properties of a nuclear protein from HepG2 cells that has high affinity for the antioxidant response element
    • S. Liu and C.B. Pickett (1996) The rat liver glutathione S-transferase Ya subunit gene: characterization of the binding properties of a nuclear protein from HepG2 cells that has high affinity for the antioxidant response element. Biochemistry, 35, 11517-11521.
    • (1996) Biochemistry , vol.35 , pp. 11517-11521
    • Liu, S.1    Pickett, C.B.2
  • 142
    • 0024463596 scopus 로고
    • Structural and functional analysis of an enhancer GPEI having a phorbol 12-O-tetradecanoate 13-acetate responsive element-like sequence found in the rat glutathione transferase P gene
    • A. Okuda, M. Imagawa, Y. Maeda, M. Sakai and M. Muramatsu (1989) Structural and functional analysis of an enhancer GPEI having a phorbol 12-O-tetradecanoate 13-acetate responsive element-like sequence found in the rat
    • (1989) The Journal of Biological Chemistry , vol.264 , pp. 16919-16926
    • Okuda, A.1    Imagawa, M.2    Maeda, Y.3    Sakai, M.4    Muramatsu, M.5
  • 144
    • 0025268888 scopus 로고
    • Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene
    • K.E. Paulson, Jr. J.E. Darnell, T. Rushmore and C.B. Pickett (1990) Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene. Molecular and Cellular Biology, 10, 1841-1852.
    • (1990) Molecular and Cellular Biology , vol.10 , pp. 1841-1852
    • Paulson K.E., Jr.1    Darnell, J.E.2    Rushmore, T.3    Pickett, C.B.4
  • 145
    • 0027497708 scopus 로고
    • Preferential increase of glutathione S-transferase class α transcripts in cultured human hepatocytes by phenobarbital, 3-methylcholanthrene, and dithiolethiones
    • F. Morel, O. Fardel, D.J. Meyer, S. Langouet, K.S. Gilmore, B. Meunier, C.-P.D. Tu, T.W. Kensler, B. Ketterer and A. Guillouzo (1993) Preferential increase of glutathione S-transferase class α transcripts in cultured human hepatocytes by phenobarbital, 3-methylcholanthrene, and dithiolethiones. Cancer Research, 53, 231-234.
    • (1993) Cancer Research , vol.53 , pp. 231-234
    • Morel, F.1    Fardel, O.2    Meyer, D.J.3    Langouet, S.4    Gilmore, K.S.5    Meunier, B.6    Tu, C.-P.D.7    Kensler, T.W.8    Ketterer, B.9    Guillouzo, A.10
  • 146
    • 0031682988 scopus 로고    scopus 로고
    • The nuclear orphan receptor CAR-retinoid X receptor heterodimer activates the phenobarbital-responsive enhancer module of the CYP2B gene
    • P. Honkakoski, I. Zelko, T. Sueyoshi and M. Negishi (1998) The nuclear orphan receptor CAR-retinoid X receptor heterodimer activates the phenobarbital-responsive enhancer module of the CYP2B gene. Molecular and Cellular Biology, 18, 5652-5658.
    • (1998) Molecular and Cellular Biology , vol.18 , pp. 5652-5658
    • Honkakoski, P.1    Zelko, I.2    Sueyoshi, T.3    Negishi, M.4
  • 147
    • 0031865753 scopus 로고    scopus 로고
    • Negative regulation of the rat glutathione S-transferase A2 gene by glucocorticoids involves a canonical glucocorticoid consensus sequence
    • K.C. Falkner, T.H. Rushmore, M.W. Linder and R.A. Prough (1998) Negative regulation of the rat glutathione S-transferase A2 gene by glucocorticoids involves a canonical glucocorticoid consensus sequence. Molecular Pharmacology, 53, 1016-1026.
    • (1998) Molecular Pharmacology , vol.53 , pp. 1016-1026
    • Falkner, K.C.1    Rushmore, T.H.2    Linder, M.W.3    Prough, R.A.4
  • 148
    • 0022569863 scopus 로고
    • Nonhistone protein BA is a glutathione S-transferase localized to interchromatinic regions of the cell nucleus
    • C.F. Bennett, D.L. Spector and L.C. Yeoman (1986) Nonhistone protein BA is a glutathione S-transferase localized to interchromatinic regions of the cell nucleus. The Journal of Cell Biology, 102, 600-609.
    • (1986) The Journal of Cell Biology , vol.102 , pp. 600-609
    • Bennett, C.F.1    Spector, D.L.2    Yeoman, L.C.3
  • 150
    • 0027451261 scopus 로고
    • m for glutathione in glutathione transferases of the α, μ and π classes
    • m for glutathione in glutathione transferases of the α, μ and π classes. Xenobiotica, 23, 823-834.
    • (1993) Xenobiotica , vol.23 , pp. 823-834
    • Meyer, D.J.1
  • 152
    • 0030570805 scopus 로고    scopus 로고
    • Transport of the glutathione conjugate of ethacrynic acid by the human multidrug resistance protein MRP
    • G.J.R. Zaman, N.H.P. Cnubben, P.J. van Bladeren, R. Evers and P. Borst (1996) Transport of the glutathione conjugate of ethacrynic acid by the human multidrug resistance protein MRP. FEBS Letters, 391, 126-130.
    • (1996) FEBS Letters , vol.391 , pp. 126-130
    • Zaman, G.J.R.1    Cnubben, N.H.P.2    Van Bladeren, P.J.3    Evers, R.4    Borst, P.5
  • 155
    • 0000510572 scopus 로고    scopus 로고
    • The influence of glutathione metabolism on multidrug resistance in MRP-overexpressing cells
    • P. Twentyman and T. Bagrij (1998) The influence of glutathione metabolism on multidrug resistance in MRP-overexpressing cells. Drug Resistance Updates, 1, 121-127.
    • (1998) Drug Resistance Updates , vol.1 , pp. 121-127
    • Twentyman, P.1    Bagrij, T.2
  • 156
    • 0032534064 scopus 로고    scopus 로고
    • r 190,000 multidrug resistance protein (MRP): Evidence for cotransport with reduced glutathione
    • r 190,000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Research, 58, 5130-5136.
    • (1998) Cancer Research , vol.58 , pp. 5130-5136
    • Loe, D.W.1    Deeley, R.G.2    Cole, S.P.C.3
  • 157
    • 0032493638 scopus 로고    scopus 로고
    • Coordinated action of glutathione S-transferases (GSTs) and Multidrug Resistance Protein 1 (MRP1) in antineoplastic drug detoxification
    • C.S. Morrow, P.K. Smitherman, S.K. Diah, E. Schneider and A.J. Townsend (1998) Coordinated action of glutathione S-transferases (GSTs) and Multidrug Resistance Protein 1 (MRP1) in antineoplastic drug detoxification. The Journal of Biological Chemistry, 273, 20114-20120.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 20114-20120
    • Morrow, C.S.1    Smitherman, P.K.2    Diah, S.K.3    Schneider, E.4    Townsend, A.J.5
  • 158
    • 0031867669 scopus 로고    scopus 로고
    • Multidrug resistance protein and glutathione S-transferase P1-1 act in synergy to confer protection from 4-nitroquinoline 1-oxide toxicity
    • C.S. Morrow, S. Diah, P.K. Smitherman, E. Schneider and A.J. Townsend (1998) Multidrug resistance protein and glutathione S-transferase P1-1 act in synergy to confer protection from 4-nitroquinoline 1-oxide toxicity. Carcinogenesis, 19, 109-115.
    • (1998) Carcinogenesis , vol.19 , pp. 109-115
    • Morrow, C.S.1    Diah, S.2    Smitherman, P.K.3    Schneider, E.4    Townsend, A.J.5
  • 159
    • 0032532339 scopus 로고    scopus 로고
    • Glutathione-dependent biotransformation of the alkylating drug thiotepa and transport of its metabolite monoglutathionylthiotepa in human MCF-7 breast cancer cells
    • N.H.P. Cnubben, A.J.M. Rommens, M.J. Oudshoorn and P.J. van Bladeren (1998) Glutathione-dependent biotransformation of the alkylating drug thiotepa and transport of its metabolite monoglutathionylthiotepa in human MCF-7 breast cancer cells. Cancer Research, 58, 4616-4623.
    • (1998) Cancer Research , vol.58 , pp. 4616-4623
    • Cnubben, N.H.P.1    Rommens, A.J.M.2    Oudshoorn, M.J.3    Van Bladeren, P.J.4
  • 160
    • 0030841332 scopus 로고    scopus 로고
    • Analysis of expression of cMOAT(MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines
    • M. Kool, M. de Haas, G.L. Scheffer, R.J. Scheper, M.J.T. van Eijk, J.A. Juijn, F. Baas and P. Borst (1997) Analysis of expression of cMOAT(MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines. Cancer Research, 57, 3537-3547.
    • (1997) Cancer Research , vol.57 , pp. 3537-3547
    • Kool, M.1    De Haas, M.2    Scheffer, G.L.3    Scheper, R.J.4    Van Eijk, M.J.T.5    Juijn, J.A.6    Baas, F.7    Borst, P.8
  • 161
    • 0029760088 scopus 로고    scopus 로고
    • Frequent coordinated overexpression of the MRP/GS-X pump and γ-glutamylcysteine synthetase genes in human colorectal cancer
    • M.T. Kuo, J.J. Bao, S.A. Curley, M. Ikeguchi, D.A. Johnston and T. Ishikawa (1996) Frequent coordinated overexpression of the MRP/GS-X pump and γ-glutamylcysteine synthetase genes in human colorectal cancer. Cancer Research, 56, 3642-3644.
    • (1996) Cancer Research , vol.56 , pp. 3642-3644
    • Kuo, M.T.1    Bao, J.J.2    Curley, S.A.3    Ikeguchi, M.4    Johnston, D.A.5    Ishikawa, T.6
  • 163
    • 0032473401 scopus 로고    scopus 로고
    • Co-ordinated over-expression of the MRP and γ-glutamylcysteine synthetase genes, but not MDR1, correlates with doxorubicin resistance in human malignant mesothelioma cell lines
    • B. Ogretmen, H.R. Bahadori, M.D. McCauley, A. Boylan, M.R. Green and A.R. Safa (1998) Co-ordinated over-expression of the MRP and γ-glutamylcysteine synthetase genes, but not MDR1, correlates with doxorubicin resistance in human malignant mesothelioma cell lines. International Journal of Cancer, 75, 757-761.
    • (1998) International Journal of Cancer , vol.75 , pp. 757-761
    • Ogretmen, B.1    Bahadori, H.R.2    McCauley, M.D.3    Boylan, A.4    Green, M.R.5    Safa, A.R.6
  • 164
    • 0032031395 scopus 로고    scopus 로고
    • Frequent coexpression of MRP/GS-X pump and γ-glutamylcysteine synthetase mRNA in drug-resistant cells, untreated tumour cells, and normal mouse tissues
    • M.T. Kuo, J.-J. Bao, M. Furuichi, Y. Yamane, A. Gomi, N. Savaraj, T. Masuzawa and T. Ishikawa (1998) Frequent coexpression of MRP/GS-X pump and γ-glutamylcysteine synthetase mRN A in drug-resistant cells, untreated tumour cells, and normal mouse tissues. Biochemical Pharmacology, 55, 605-615.
    • (1998) Biochemical Pharmacology , vol.55 , pp. 605-615
    • Kuo, M.T.1    Bao, J.-J.2    Furuichi, M.3    Yamane, Y.4    Gomi, A.5    Savaraj, N.6    Masuzawa, T.7    Ishikawa, T.8
  • 165
    • 0032553308 scopus 로고    scopus 로고
    • Expression of multidrug resistance protein/GS-X pump and γ-glutamylcysteine synthetase genes is regulated by oxidative stress
    • Y. Yamane, M. Furuichi, R. Song, N.T. Van, R.T. Mulcahy, T. Ishikawa and M.T. Kuo (1998) Expression of multidrug resistance protein/GS-X pump and γ-glutamylcysteine synthetase genes is regulated by oxidative stress. The Journal of Biological Chemistry, 273, 31075-31085.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 31075-31085
    • Yamane, Y.1    Furuichi, M.2    Song, R.3    Van, N.T.4    Mulcahy, R.T.5    Ishikawa, T.6    Kuo, M.T.7
  • 166
    • 0029052835 scopus 로고
    • Evidence for altered regulation of γ-glutamylcysteine synthetase gene expression among cisplatin-sensitive and cisplatin-resistant human ovarian cancer cell lines
    • K.-S. Yao, A.K. Godwin, S.W. Johnson, R.F. Ozols, P.J. O'Dwyer and T.C. Hamilton (1995) Evidence for altered regulation of γ-glutamylcysteine synthetase gene expression among cisplatin-sensitive and cisplatin-resistant human ovarian cancer cell lines. Cancer Research, 55, 4367-4374.
    • (1995) Cancer Research , vol.55 , pp. 4367-4374
    • Yao, K.-S.1    Godwin, A.K.2    Johnson, S.W.3    Ozols, R.F.4    O'Dwyer, P.J.5    Hamilton, T.C.6
  • 167
    • 0033582431 scopus 로고    scopus 로고
    • Molecular mechanism of the regulation of glutathione synthesis by tumour necrosis factor-α and dexamethasone in human alveolar epithelial cells
    • I. Rahman, F. Antonicelli and W. MacNee (1999) Molecular mechanism of the regulation of glutathione synthesis by tumour necrosis factor-α and dexamethasone in human alveolar epithelial cells. The Journal of Biological Chemistry, 274, 5088-5096.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 5088-5096
    • Rahman, I.1    Antonicelli, F.2    MacNee, W.3
  • 168
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1
    • R. Schreck, P. Rieber and P.A. Baeuerle (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. The EMBO Journal, 10, 2247-2258
    • (1991) The EMBO Journal , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 169
    • 0032535308 scopus 로고    scopus 로고
    • Transcriptional suppression of multidrug resistance-associated protein (MRP) gene expression by wild-type p53
    • Q. Wang and W.T. Beck (1998) Transcriptional suppression of multidrug resistance-associated protein (MRP) gene expression by wild-type p53. Cancer Research, 58, 5762-5769.
    • (1998) Cancer Research , vol.58 , pp. 5762-5769
    • Wang, Q.1    Beck, W.T.2
  • 170
    • 0032127347 scopus 로고    scopus 로고
    • Isolation of MOAT-B, a widely expressed multidrug resistance-associated protein/canalicular multi-specific organic anion transporter-related transporter
    • K. Lee, M.G. Belinsky, D.W. Bell, J.R. Testa and G.D. Kruh (1998) Isolation of MOAT-B, a widely expressed multidrug resistance-associated protein/canalicular multi-specific organic anion transporter-related transporter. Cancer Research, 58, 2741-2747.
    • (1998) Cancer Research , vol.58 , pp. 2741-2747
    • Lee, K.1    Belinsky, M.G.2    Bell, D.W.3    Testa, J.R.4    Kruh, G.D.5
  • 171
    • 0028054888 scopus 로고
    • Overexpression of Multidrug Resistance-associated Protein (MRP) increases resistance to natural product drugs
    • C.E. Grant, G. Valdimarsson, D.R. Hipfner, K.C. Almquist, S.P.C. Cole and R.G. Deeley (1994) Overexpression of Multidrug Resistance-associated Protein (MRP) increases resistance to natural product drugs. Cancer Research, 54, 357-361.
    • (1994) Cancer Research , vol.54 , pp. 357-361
    • Grant, C.E.1    Valdimarsson, G.2    Hipfner, D.R.3    Almquist, K.C.4    Cole, S.P.C.5    Deeley, R.G.6
  • 173
    • 0031160517 scopus 로고    scopus 로고
    • Expression and localization of the conjugate export pump encoded by the MRP2 (cMRP/cMOAT) gene in liver
    • D. Kepplerand J. König (1997) Expression and localization of the conjugate export pump encoded by the MRP2 (cMRP/cMOAT) gene in liver. FASEB Journal, 11, 509-516.
    • (1997) FASEB Journal , vol.11 , pp. 509-516
    • Kepplerand, D.1    König, J.2
  • 174
    • 9544233652 scopus 로고    scopus 로고
    • A human canalicular multispecific organic anion transporter (cMOAT) gene is overexpressed in cisplatin-resistant human cancer cell lines with decreased drug accumulation
    • K. Taniguchi, M. Wada, K. Kohno, T. Nakamura, T. Kawabe, M. Kawakami, K. Kagotani, K. Okumura, S.-I. Akiyama and M. Kuwano (1996) A human canalicular multispecific organic anion transporter (cMOAT) gene is overexpressed in cisplatin-resistant human cancer cell lines with decreased drug accumulation. Cancer Research, 56, 4124-4129.
    • (1996) Cancer Research , vol.56 , pp. 4124-4129
    • Taniguchi, K.1    Wada, M.2    Kohno, K.3    Nakamura, T.4    Kawabe, T.5    Kawakami, M.6    Kagotani, K.7    Okumura, K.8    Akiyama, S.-I.9    Kuwano, M.10
  • 175
    • 0030747386 scopus 로고    scopus 로고
    • The GS-X pump in plant, yeast, and animal cells: Structure, function, and gene expression
    • T. Ishikawa, Z.-S. Li, Y-P. Lu and P.A. Rea (1997) The GS-X pump in plant, yeast, and animal cells: structure, function, and gene expression. Bioscience Reports, 17, 189-207.
    • (1997) Bioscience Reports , vol.17 , pp. 189-207
    • Ishikawa, T.1    Li, Z.-S.2    Lu, Y.-P.3    Rea, P.A.4
  • 176
    • 0027305406 scopus 로고
    • Glutathione-associated cis-diamrninedichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia cells
    • T. Ishikawa and F. Ali-Osman (1993) Glutathione-associated cis-diamrninedichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia cells. The Journal of Biological Chemistry, 268, 20116-20125.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 20116-20125
    • Ishikawa, T.1    Ali-Osman, F.2
  • 177
    • 0032893268 scopus 로고    scopus 로고
    • Expression of human MRP6, a homologue of the Multidrug Resistance Protein gene MRP1, in tissues and cancer cells
    • M. Kool, M. van der Linden, M. de Haas, F. Baas and P. Borst (1999) Expression of human MRP6, a homologue of the Multidrug Resistance Protein gene MRP1, in tissues and cancer cells. Cancer Research, 59, 175-182.
    • (1999) Cancer Research , vol.59 , pp. 175-182
    • Kool, M.1    Van Der Linden, M.2    De Haas, M.3    Baas, F.4    Borst, P.5


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