메뉴 건너뛰기




Volumn 36, Issue 10-11, 2006, Pages 1081-1121

Tissue and species distribution of the glutathione pathway transcriptome

Author keywords

Antioxidant; Basal tissue gene expression; Glutathione; Glutathione S transferases; Species differences

Indexed keywords

GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE P1; N ACETYL 1,4 BENZOQUINONE IMINE; PARACETAMOL; PROTEIN GPX3; PROTEIN MGST1; TRANSCRIPTOME; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 33748987972     PISSN: 00498254     EISSN: 13665928     Source Type: Journal    
DOI: 10.1080/00498250600861793     Document Type: Article
Times cited : (17)

References (143)
  • 1
    • 0024581914 scopus 로고
    • Activation of rat liver microsomal glutathione S-transferase by reduced oxygen species
    • Aniya Y, Anders MW. 1989. Activation of rat liver microsomal glutathione S-transferase by reduced oxygen species. Journal of Biology and Chemistry 264(4):1998-2002.
    • (1989) Journal of Biology and Chemistry , vol.264 , Issue.4 , pp. 1998-2002
    • Aniya, Y.1    Anders, M.W.2
  • 2
    • 0026726105 scopus 로고
    • Activation of rat liver microsomal glutathione S-transferase by hydrogen peroxide: Role for protein-dimer formation
    • Aniya Y, Anders MW. 1992. Activation of rat liver microsomal glutathione S-transferase by hydrogen peroxide: Role for protein-dimer formation. Archives in Biochemistry and Biophysics 296(2):611-616.
    • (1992) Archives in Biochemistry and Biophysics , vol.296 , Issue.2 , pp. 611-616
    • Aniya, Y.1    Anders, M.W.2
  • 4
    • 0016769483 scopus 로고
    • Purification and properties of human erythrocyte glutathione peroxidase
    • Awasthi YC, Beutler E, Srivastava SK. 1975. Purification and properties of human erythrocyte glutathione peroxidase. Journal of Biology and Chemistry 250(13):5144-5149.
    • (1975) Journal of Biology and Chemistry , vol.250 , Issue.13 , pp. 5144-5149
    • Awasthi, Y.C.1    Beutler, E.2    Srivastava, S.K.3
  • 6
    • 0028036292 scopus 로고
    • Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
    • Berhane K, Widersten M, Engstrom A, Kozarich JW, Mannervik B. (1994). Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proceedings of the National Academy of Sciences, USA 91(4): 1480-1484.
    • (1994) Proceedings of the National Academy of Sciences, USA , vol.91 , Issue.4 , pp. 1480-1484
    • Berhane, K.1    Widersten, M.2    Engstrom, A.3    Kozarich, J.W.4    Mannervik, B.5
  • 7
    • 0022570709 scopus 로고
    • Erythrocyte glutathione synthetase deficiency leads not only to glutathione but also to glutathione-S-transferase deficiency
    • Beutler E, Gelbart T, Pegelow C. 1986. Erythrocyte glutathione synthetase deficiency leads not only to glutathione but also to glutathione-S-transferase deficiency. Journal of Clinical Investigation 77(1):38-41.
    • (1986) Journal of Clinical Investigation , vol.77 , Issue.1 , pp. 38-41
    • Beutler, E.1    Gelbart, T.2    Pegelow, C.3
  • 8
    • 0025095668 scopus 로고
    • Gamma-glutamylcysteine synthetase deficiency and hemolytic anemia
    • Beutler E, Moroose R, Kramer L, Gelbart T, Forman L. 1990. Gamma-glutamylcysteine synthetase deficiency and hemolytic anemia. Blood 75(1):271-273.
    • (1990) Blood , vol.75 , Issue.1 , pp. 271-273
    • Beutler, E.1    Moroose, R.2    Kramer, L.3    Gelbart, T.4    Forman, L.5
  • 9
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt M, Xue J, Huang W, Akesson B, Holmgren A. 1994. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. Journal of Biology and Chemistry 269(47):29382-29384.
    • (1994) Journal of Biology and Chemistry , vol.269 , Issue.47 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 11
    • 0034802547 scopus 로고    scopus 로고
    • Cholestasis and regulation of genes related to drug metabolism and biliary transport in rat liver following treatment with cyclosporine A and sirolimus (Rapamycin)
    • Bramow S, Ott P, Thomsen Nielsen F, Bangert K, Tygstrup N, Dalhoff K. 2001. Cholestasis and regulation of genes related to drug metabolism and biliary transport in rat liver following treatment with cyclosporine A and sirolimus (Rapamycin). Pharmacology and Toxicology 89(3):133-139.
    • (2001) Pharmacology and Toxicology , vol.89 , Issue.3 , pp. 133-139
    • Bramow, S.1    Ott, P.2    Thomsen Nielsen, F.3    Bangert, K.4    Tygstrup, N.5    Dalhoff, K.6
  • 12
    • 0036884167 scopus 로고    scopus 로고
    • The use and analysis of microarray data
    • Butte A. 2002. The use and analysis of microarray data. Nature Reviews in Drug Discovery 1(12):951-960.
    • (2002) Nature Reviews in Drug Discovery , vol.1 , Issue.12 , pp. 951-960
    • Butte, A.1
  • 13
    • 0025801691 scopus 로고
    • Immunohistologic localization of alpha, mu, and pi class glutathione S-transferases in human tissues
    • Campbell JA, Corrigall AV, Guy A, Kirsch RE. 1991. Immunohistologic localization of alpha, mu, and pi class glutathione S-transferases in human tissues. Cancer 67(6):1608-1613.
    • (1991) Cancer , vol.67 , Issue.6 , pp. 1608-1613
    • Campbell, J.A.1    Corrigall, A.V.2    Guy, A.3    Kirsch, R.E.4
  • 14
    • 0037101768 scopus 로고    scopus 로고
    • Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice
    • Chanas S, Jiang Q, McMahon M, McWalter GK, McLellan LI, Elcombe CR, Henderson CJ, Wolf CR, Moffat GJ, Itoh K, Yamamoto M, Hayes JD. 2002. Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice. Biochemistry Journal 365(2):405-416.
    • (2002) Biochemistry Journal , vol.365 , Issue.2 , pp. 405-416
    • Chanas, S.1    Jiang, Q.2    McMahon, M.3    McWalter, G.K.4    McLellan, L.I.5    Elcombe, C.R.6    Henderson, C.J.7    Wolf, C.R.8    Moffat, G.J.9    Itoh, K.10    Yamamoto, M.11    Hayes, J.D.12
  • 15
    • 26644449682 scopus 로고    scopus 로고
    • Glutamate cysteine ligase catalysis: Dependence on ATP and modifier subunit for regulation of tissue glutathione levels
    • Chen Y, Shertzer HG, Schneider SN, Nebert DW, Dalton TP. 2005. Glutamate cysteine ligase catalysis: Dependence on ATP and modifier subunit for regulation of tissue glutathione levels. Journal of Biology and Chemistry 280(40):33766-33774.
    • (2005) Journal of Biology and Chemistry , vol.280 , Issue.40 , pp. 33766-33774
    • Chen, Y.1    Shertzer, H.G.2    Schneider, S.N.3    Nebert, D.W.4    Dalton, T.P.5
  • 16
    • 0031050301 scopus 로고    scopus 로고
    • Food restriction reduces aflatoxin B1 (AFB1)-DNA adduct formation, AFB1-glutathione conjugation, and DNA damage in AFB1-treated male F344 rats and B6C3F1 mice
    • Chou M, Chen W. 1997. Food restriction reduces aflatoxin B1 (AFB1)-DNA adduct formation, AFB1-glutathione conjugation, and DNA damage in AFB1-treated male F344 rats and B6C3F1 mice. Journal of Nutrition 127(2):210-217.
    • (1997) Journal of Nutrition , vol.127 , Issue.2 , pp. 210-217
    • Chou, M.1    Chen, W.2
  • 17
    • 0041529819 scopus 로고    scopus 로고
    • Resistance to tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis in rat hepatoma cells expressing TNF-alpha is linked to low antioxidant enzyme expression
    • Chovolou Y, Watjen W, Kampkotter A, Kahl R. 2003. Resistance to tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis in rat hepatoma cells expressing TNF-alpha is linked to low antioxidant enzyme expression. Journal of Biology and Chemistry 278(32):29626-29632.
    • (2003) Journal of Biology and Chemistry , vol.278 , Issue.32 , pp. 29626-29632
    • Chovolou, Y.1    Watjen, W.2    Kampkotter, A.3    Kahl, R.4
  • 18
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu FF, Doroshow JH, Esworthy RS. 1993. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. Journal of Biology and Chemistry 268(4):2571-2576.
    • (1993) Journal of Biology and Chemistry , vol.268 , Issue.4 , pp. 2571-2576
    • Chu, F.F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 19
    • 0026773732 scopus 로고
    • Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents
    • Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF. 1992. Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood 79(12):3233-3238.
    • (1992) Blood , vol.79 , Issue.12 , pp. 3233-3238
    • Chu, F.F.1    Esworthy, R.S.2    Doroshow, J.H.3    Doan, K.4    Liu, X.F.5
  • 20
    • 0030586798 scopus 로고    scopus 로고
    • Protein S-thiolation and regulation of microsomal glutathione transferase activity by the glutathione redox couple
    • Dafre AL, Sies H, Akerboom T. 1996. Protein S-thiolation and regulation of microsomal glutathione transferase activity by the glutathione redox couple. Archives in Biochemistry and Biophysics 332(2):288-294.
    • (1996) Archives in Biochemistry and Biophysics , vol.332 , Issue.2 , pp. 288-294
    • Dafre, A.L.1    Sies, H.2    Akerboom, T.3
  • 22
    • 0034694871 scopus 로고    scopus 로고
    • Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: Embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous
    • Dalton TP, Dieter MZ, Yang Y, Shertzer HG, Nebert DW. 2000. Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: Embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous. Biochemical and Biophysical Research Communications 279(2):324-329.
    • (2000) Biochemical and Biophysical Research Communications , vol.279 , Issue.2 , pp. 324-329
    • Dalton, T.P.1    Dieter, M.Z.2    Yang, Y.3    Shertzer, H.G.4    Nebert, D.W.5
  • 23
    • 0027318721 scopus 로고
    • Glutathione S-transferases: Gene structure and regulation of expression
    • Daniel V. 1993. Glutathione S-transferases: Gene structure and regulation of expression. Critical Reviews in Biochemistry and Molecular Biology 28(3):173-207.
    • (1993) Critical Reviews in Biochemistry and Molecular Biology , vol.28 , Issue.3 , pp. 173-207
    • Daniel, V.1
  • 29
    • 0024202758 scopus 로고
    • Purification and characterization of a novel monomeric glutathione peroxidase from rat liver
    • Duan YJ, Komura S, Fiszer-Szafarz B, Szafarz D, Yagi K. 1988. Purification and characterization of a novel monomeric glutathione peroxidase from rat liver. Journal of Biology and Chemistry 263(35):19003-19008.
    • (1988) Journal of Biology and Chemistry , vol.263 , Issue.35 , pp. 19003-19008
    • Duan, Y.J.1    Komura, S.2    Fiszer-Szafarz, B.3    Szafarz, D.4    Yagi, K.5
  • 32
    • 0033106138 scopus 로고    scopus 로고
    • Distribution of microsomal glutathione transferase 1 in mammalian tissues. A predominant alternate first exon in human tissues
    • Estonius M, Forsberg L, Danielsson O, Weinander R, Kelner MJ, Morgenstern R. 1999. Distribution of microsomal glutathione transferase 1 in mammalian tissues. A predominant alternate first exon in human tissues. European Journal of Biochemistry 260(2):409-413.
    • (1999) European Journal of Biochemistry , vol.260 , Issue.2 , pp. 409-413
    • Estonius, M.1    Forsberg, L.2    Danielsson, O.3    Weinander, R.4    Kelner, M.J.5    Morgenstern, R.6
  • 33
    • 4744351527 scopus 로고    scopus 로고
    • Selenoprotein mRNA is expressed in blood at levels comparable to major tissues in rats
    • Evenson JK, Wheeler AD, Blake SM, Sunde RA. 2004. Selenoprotein mRNA is expressed in blood at levels comparable to major tissues in rats. Journal of Nutrition 134(10):2640-2645.
    • (2004) Journal of Nutrition , vol.134 , Issue.10 , pp. 2640-2645
    • Evenson, J.K.1    Wheeler, A.D.2    Blake, S.M.3    Sunde, R.A.4
  • 37
    • 0029080925 scopus 로고
    • The effects of diquat and ciprofibrate on mRNA expression and catalytic activities of hepatic xenobiotic metabolizing and antioxidant enzymes in rat liver
    • Gallagher EP, Buetler TM, Stapleton PL, Wang C, Stahl DL, Eaton DL. 1995. The effects of diquat and ciprofibrate on mRNA expression and catalytic activities of hepatic xenobiotic metabolizing and antioxidant enzymes in rat liver. Toxicology and Applied Pharmacology 134(1):81-91.
    • (1995) Toxicology and Applied Pharmacology , vol.134 , Issue.1 , pp. 81-91
    • Gallagher, E.P.1    Buetler, T.M.2    Stapleton, P.L.3    Wang, C.4    Stahl, D.L.5    Eaton, D.L.6
  • 38
    • 0035154555 scopus 로고    scopus 로고
    • The dark side of a 'detoxification' mechanism
    • Gillam E. 2001. The dark side of a 'detoxification' mechanism. Trends in Pharmacology Sciences 22(1):11.
    • (2001) Trends in Pharmacology Sciences , vol.22 , Issue.1 , pp. 11
    • Gillam, E.1
  • 40
    • 0036304261 scopus 로고    scopus 로고
    • Mode of cell death after acetaminophen overdose in mice: Apoptosis or oncotic necrosis?
    • Gujral JS, Knight TR, Farhood A, Bajt ML, Jaeschke H. 2002, Mode of cell death after acetaminophen overdose in mice: Apoptosis or oncotic necrosis? Toxicology Sciences 67(2):322-328.
    • (2002) Toxicology Sciences , vol.67 , Issue.2 , pp. 322-328
    • Gujral, J.S.1    Knight, T.R.2    Farhood, A.3    Bajt, M.L.4    Jaeschke, H.5
  • 41
    • 0021287414 scopus 로고
    • Toxicity of aflatoxin B1 in rat and mouse hepatocytes in vivo and in vitro
    • Hanigan H, Laishes BA. 1984. Toxicity of aflatoxin B1 in rat and mouse hepatocytes in vivo and in vitro. Toxicology 30(3):185-193.
    • (1984) Toxicology , vol.30 , Issue.3 , pp. 185-193
    • Hanigan, H.1    Laishes, B.A.2
  • 42
    • 8444228527 scopus 로고    scopus 로고
    • Compartmentation of Nrf-2 redox control: Regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1
    • Hansen JM, Watson WH, Jones DP. 2004. Compartmentation of Nrf-2 redox control: Regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicology Sciences 82(1):308-317.
    • (2004) Toxicology Sciences , vol.82 , Issue.1 , pp. 308-317
    • Hansen, J.M.1    Watson, W.H.2    Jones, D.P.3
  • 43
    • 0024333641 scopus 로고
    • Distribution of glutathione S-transferase isoenzymes in human kidney: Basis for possible markers of renal injury
    • Harrison D, Kharbanda R, Cunningham DS, McLellan LI, Hayes JD. 1989. Distribution of glutathione S-transferase isoenzymes in human kidney: Basis for possible markers of renal injury. Journal of Clinical Pathology 42(6):624-628.
    • (1989) Journal of Clinical Pathology , vol.42 , Issue.6 , pp. 624-628
    • Harrison, D.1    Kharbanda, R.2    Cunningham, D.S.3    McLellan, L.I.4    Hayes, J.D.5
  • 44
    • 0027235542 scopus 로고
    • Sex-dependent expression of class pi glutathione S-transferase during chemical hepatocarcinogenesis in B6C3F1 mice
    • Hatayama I, Nishimura S, Narita T, Sato K. 1993. Sex-dependent expression of class pi glutathione S-transferase during chemical hepatocarcinogenesis in B6C3F1 mice. Carcinogenesis 14(3):537-538.
    • (1993) Carcinogenesis , vol.14 , Issue.3 , pp. 537-538
    • Hatayama, I.1    Nishimura, S.2    Narita, T.3    Sato, K.4
  • 46
    • 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, Judah DJ, McLellan LI, Kerr LA, Peacock SD, Neal GE. 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. Biochemistry Journal 279(2):385-398.
    • (1991) Biochemistry Journal , vol.279 , Issue.2 , pp. 385-398
    • Hayes, J.1    Judah, D.J.2    McLellan, L.I.3    Kerr, L.A.4    Peacock, S.D.5    Neal, G.E.6
  • 47
    • 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, Judah DJ, Neal GE, 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. Biochemistry Journal 285(1):173-180.
    • (1992) Biochemistry Journal , vol.285 , Issue.1 , pp. 173-180
    • Hayes, J.1    Judah, D.J.2    Neal, G.E.3    Nguyen, T.4
  • 48
    • 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, Nguyen T, Judah DJ, Petersson DG, Neal GE. 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. Journal of Biology and Chemistry 269(32):20707-20717.
    • (1994) Journal of Biology and Chemistry , vol.269 , Issue.32 , pp. 20707-20717
    • Hayes, J.1    Nguyen, T.2    Judah, D.J.3    Petersson, D.G.4    Neal, G.E.5
  • 49
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J, Pulford DJ. 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(6):445-600.
    • (1995) Critical Reviews in Biochemistry and Molecular Biology , vol.30 , Issue.6 , pp. 445-600
    • Hayes, J.1    Pulford, D.J.2
  • 54
    • 5144220196 scopus 로고    scopus 로고
    • Molecular detection of prostate cancer: A role for GSTP1 hypermethylation
    • Henrique R, Jeronimo C. 2004. Molecular detection of prostate cancer: A role for GSTP1 hypermethylation. European Journal of Urology 46(5):660-669.
    • (2004) European Journal of Urology 46 , Issue.5 , pp. 660-669
    • Henrique, R.1    Jeronimo, C.2
  • 55
    • 0030296758 scopus 로고    scopus 로고
    • Seleno compounds and glutathione peroxidase catalysed decomposition of S-nitrosothiols
    • Hou Y, Guo Z, Li J, Wang PG. 1996. Seleno compounds and glutathione peroxidase catalysed decomposition of S-nitrosothiols. Biochemical and Biophysical Research Communications 228(1):88-93.
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.1 , pp. 88-93
    • Hou, Y.1    Guo, Z.2    Li, J.3    Wang, P.G.4
  • 56
    • 0027227925 scopus 로고
    • Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase
    • Huang C, Anderson M, Meister A. 1993a. Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase. Journal of Biology and Chemistry 268(27):20578-20583.
    • (1993) Journal of Biology and Chemistry , vol.268 , Issue.27 , pp. 20578-20583
    • Huang, C.1    Anderson, M.2    Meister, A.3
  • 57
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase
    • Huang C, Chang L, Anderson M, Meister A. 1993b. Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase. Journal of Biology and Chemistry 268(26):19675-19680.
    • (1993) Journal of Biology and Chemistry , vol.268 , Issue.26 , pp. 19675-19680
    • Huang, C.1    Chang, L.2    Anderson, M.3    Meister, A.4
  • 58
    • 0035227318 scopus 로고    scopus 로고
    • Mechanism and significance of increased glutathione level in human hepatocellular carcinoma and liver regeneration
    • Huang Z-Z, Chen C, Zeng Z, Yang H, Oh J, Chen L, Lu SC. 2001. Mechanism and significance of increased glutathione level in human hepatocellular carcinoma and liver regeneration. FASEB Journal 15(1):19-21.
    • (2001) FASEB Journal , vol.15 , Issue.1 , pp. 19-21
    • Huang, Z.-Z.1    Chen, C.2    Zeng, Z.3    Yang, H.4    Oh, J.5    Chen, L.6    Lu, S.C.7
  • 59
    • 0031961850 scopus 로고    scopus 로고
    • Changes in glutathione homeostasis during liver regeneration in the rat
    • Huang ZZ, Li H, Cai J, Kuhlenkamp J, Kaplowitz N, Lu SC. 1998. Changes in glutathione homeostasis during liver regeneration in the rat. Hepatology 27(1):147-153.
    • (1998) Hepatology , vol.27 , Issue.1 , pp. 147-153
    • Huang, Z.Z.1    Li, H.2    Cai, J.3    Kuhlenkamp, J.4    Kaplowitz, N.5    Lu, S.C.6
  • 60
    • 2942746263 scopus 로고    scopus 로고
    • Transcription factor Nrf2/MafK regulates rat placental glutathione S-transferase gene during hepatocarcinogenesis
    • Ikeda H, Nishi S, Sakai M. 2004. Transcription factor Nrf2/MafK regulates rat placental glutathione S-transferase gene during hepatocarcinogenesis. Biochemistry Journal 380(2):515-521.
    • (2004) Biochemistry Journal , vol.380 , Issue.2 , pp. 515-521
    • Ikeda, H.1    Nishi, S.2    Sakai, M.3
  • 61
    • 29544448331 scopus 로고    scopus 로고
    • Intracellular signaling mechanisms of acetaminophen-induced liver cell death
    • Jaeschke H, Bajt ML. 2006. Intracellular signaling mechanisms of acetaminophen-induced liver cell death. Toxicology Sciences 89(1):31-41.
    • (2006) Toxicology Sciences , vol.89 , Issue.1 , pp. 31-41
    • Jaeschke, H.1    Bajt, M.L.2
  • 65
    • 6444242332 scopus 로고    scopus 로고
    • Microarray analysis of altered gene expression in kidneys of adult spontaneously hypertensive rats
    • Koo J-R, Liang KH, Vaziri ND. 2004. Microarray analysis of altered gene expression in kidneys of adult spontaneously hypertensive rats. Journal of Applied Research 4(1):111-126.
    • (2004) Journal of Applied Research , vol.4 , Issue.1 , pp. 111-126
    • Koo, J.-R.1    Liang, K.H.2    Vaziri, N.D.3
  • 67
    • 0036265997 scopus 로고    scopus 로고
    • Immunohistochemical localization and activity of glutathione transferase zeta (GSTZ1-1) in rat tissues
    • Lantum HB, Baggs RB, Krenitsky DM, Board PG, Anders MW. 2002. Immunohistochemical localization and activity of glutathione transferase zeta (GSTZ1-1) in rat tissues. Drug Metabolism and Disposition 30(6):616-625.
    • (2002) Drug Metabolism and Disposition , vol.30 , Issue.6 , pp. 616-625
    • Lantum, H.B.1    Baggs, R.B.2    Krenitsky, D.M.3    Board, P.G.4    Anders, M.W.5
  • 68
    • 17444419341 scopus 로고    scopus 로고
    • Role of glutathione transport processes in kidney function
    • Lash LH. 2005. Role of glutathione transport processes in kidney function. Toxicology and Applied Pharmacology 204(3):329-342.
    • (2005) Toxicology and Applied Pharmacology , vol.204 , Issue.3 , pp. 329-342
    • Lash, L.H.1
  • 70
    • 0038146898 scopus 로고    scopus 로고
    • Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis
    • Lee JM, Calkins MJ, Chan K, Kan YW, Johnson JA. 2003. Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis. Journal of Biology and Chemistry 278(14):12029-12038.
    • (2003) Journal of Biology and Chemistry , vol.278 , Issue.14 , pp. 12029-12038
    • Lee, J.M.1    Calkins, M.J.2    Chan, K.3    Kan, Y.W.4    Johnson, J.A.5
  • 71
    • 2342514015 scopus 로고    scopus 로고
    • An important role of Nrf2-ARE pathway in the cellular defense mechanism
    • Lee JM, Johnson JA. 2004. An important role of Nrf2-ARE pathway in the cellular defense mechanism. Journal of Biochemistry and Molecular Biology 37(2):139-143.
    • (2004) Journal of Biochemistry and Molecular Biology , vol.37 , Issue.2 , pp. 139-143
    • Lee, J.M.1    Johnson, J.A.2
  • 73
    • 30144433377 scopus 로고    scopus 로고
    • A subclass of mu glutathione S-transferases selectively expressed in testis and brain
    • Listowsky I. 2005. A subclass of mu glutathione S-transferases selectively expressed in testis and brain. Methods in Enzymology 401:278-287.
    • (2005) Methods in Enzymology , vol.401 , pp. 278-287
    • Listowsky, I.1
  • 74
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: Current concepts and controversies
    • Lu SC. 1999. Regulation of hepatic glutathione synthesis: Current concepts and controversies. FASEB Journal 13(10):1169-1183.
    • (1999) FASEB Journal , vol.13 , Issue.10 , pp. 1169-1183
    • Lu, S.C.1
  • 75
    • 0026674198 scopus 로고
    • Insulin and glucocorticoid dependence of hepatic gamma-glutamylcysteine synthetase and glutathione synthesis in the rat. Studies in cultured hepatocytes and in vivo
    • Lu SC, Ge JL, Kuhlenkamp J, Kaplowitz N. 1992. Insulin and glucocorticoid dependence of hepatic gamma-glutamylcysteine synthetase and glutathione synthesis in the rat. Studies in cultured hepatocytes and in vivo. Journal of Clinical Investigation 90(2):524-532.
    • (1992) Journal of Clinical Investigation , vol.90 , Issue.2 , pp. 524-532
    • Lu, S.C.1    Ge, J.L.2    Kuhlenkamp, J.3    Kaplowitz, N.4
  • 76
    • 0037674922 scopus 로고    scopus 로고
    • Localization of glutamate cysteine ligase subunit mRNA within the rat ovary and relationship to follicular apoptosis
    • Luderer U, Diaz D, Faustman EM, Kavanagh TJ. 2003. Localization of glutamate cysteine ligase subunit mRNA within the rat ovary and relationship to follicular apoptosis. Molecules and Reproductive Development 65(3):254-261.
    • (2003) Molecules and Reproductive Development , vol.65 , Issue.3 , pp. 254-261
    • Luderer, U.1    Diaz, D.2    Faustman, E.M.3    Kavanagh, T.J.4
  • 79
    • 0023522192 scopus 로고
    • Characterization of the major hydroperoxide-reducing activity of human plasma. Purification and properties of a selenium-dependent glutathione peroxidase
    • Maddipati KR, Marnett LJ. 1987. Characterization of the major hydroperoxide-reducing activity of human plasma. Purification and properties of a selenium-dependent glutathione peroxidase. Journal of Biology and Chemistry 262(36):17398-17403.
    • (1987) Journal of Biology and Chemistry , vol.262 , Issue.36 , pp. 17398-17403
    • Maddipati, K.R.1    Marnett, L.J.2
  • 80
    • 0022982425 scopus 로고
    • Species differences in mutagenicity testing: I. Micronucleus and SCE tests in rats, mice, and Chinese hamsters with aflatoxin B1
    • Madle E, Korte A, Beek B. 1986, Species differences in mutagenicity testing: I. Micronucleus and SCE tests in rats, mice, and Chinese hamsters with aflatoxin B1. Teratogenesis, Carcinogenesis and Mutagenesis 6(1):1-13.
    • (1986) Teratogenesis, Carcinogenesis and Mutagenesis , vol.6 , Issue.1 , pp. 1-13
    • Madle, E.1    Korte, A.2    Beek, B.3
  • 81
    • 0029790153 scopus 로고    scopus 로고
    • The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human
    • Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T. 1996. The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochemistry Journal 318(1):297-303.
    • (1996) Biochemistry Journal , vol.318 , Issue.1 , pp. 297-303
    • Mainwaring, G.W.1    Williams, S.M.2    Foster, J.R.3    Tugwood, J.4    Green, T.5
  • 83
    • 0027320750 scopus 로고
    • Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular ciliary epithelium: Expression of the plasma and cellular forms within the mammalian eye
    • Martin-Alonso JM, Ghosh S, Coca-Prados M. 1993. Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular ciliary epithelium: Expression of the plasma and cellular forms within the mammalian eye. Journal of Biochemistry (Tokyo) 114(2):284-291.
    • (1993) Journal of Biochemistry (Tokyo) , vol.114 , Issue.2 , pp. 284-291
    • Martin-Alonso, J.M.1    Ghosh, S.2    Coca-Prados, M.3
  • 84
    • 0027993038 scopus 로고
    • Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion
    • Maser RL, Magenheimer BS, Calvet JP. 1994. Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion. Journal of Biology and Chemistry 269(43):27066-27073.
    • (1994) Journal of Biology and Chemistry , vol.269 , Issue.43 , pp. 27066-27073
    • Maser, R.L.1    Magenheimer, B.S.2    Calvet, J.P.3
  • 85
    • 1542331972 scopus 로고    scopus 로고
    • Annotation and cross-indexing of array elements on multiple platforms
    • Mattes WB. 2004. Annotation and cross-indexing of array elements on multiple platforms. Environmental Health Perspectives 112(4):506-510.
    • (2004) Environmental Health Perspectives , vol.112 , Issue.4 , pp. 506-510
    • Mattes, W.B.1
  • 86
    • 0028173901 scopus 로고
    • Regulation of aflatoxin B1-metabolizing aldehyde reductase and glutathione S-transferase by chemoprotectors
    • McLellan L, Judah DJ, Neal GE, Hayes JD. 1994. Regulation of aflatoxin B1-metabolizing aldehyde reductase and glutathione S-transferase by chemoprotectors. Biochemistry Journal 300(1):117-124.
    • (1994) Biochemistry Journal , vol.300 , Issue.1 , pp. 117-124
    • McLellan, L.1    Judah, D.J.2    Neal, G.E.3    Hayes, J.D.4
  • 88
    • 0032126145 scopus 로고    scopus 로고
    • Expression and purification of human gamma-glutamylcysteine synthetase
    • Misra I, Griffith OW. 1998. Expression and purification of human gamma-glutamylcysteine synthetase. Protein Expression and Purification 13(2):268-276.
    • (1998) Protein Expression and Purification , vol.13 , Issue.2 , pp. 268-276
    • Misra, I.1    Griffith, O.W.2
  • 89
    • 0030796729 scopus 로고    scopus 로고
    • Quantitative profiling of tissue- And gender-related expression of glutathione S-transferase isoenzymes in the mouse
    • Mitchell AE, Morin D, Lakritz J, Jones AD. 1997. Quantitative profiling of tissue- and gender-related expression of glutathione S-transferase isoenzymes in the mouse. Biochemistry Journal 325(1):207-216.
    • (1997) Biochemistry Journal , vol.325 , Issue.1 , pp. 207-216
    • Mitchell, A.E.1    Morin, D.2    Lakritz, J.3    Jones, A.D.4
  • 90
    • 2642671110 scopus 로고    scopus 로고
    • An electrophile responsive element (EpRE) regulates beta-naphthoflavone induction of the human gamma-glutamylcysteine synthetase regulatory subunit gene
    • Moinova HR, Mulcahy RT. 1998. An electrophile responsive element (EpRE) regulates beta-naphthoflavone induction of the human gamma-glutamylcysteine synthetase regulatory subunit gene. Journal of Biology and Chemistry 273:14683-14689.
    • (1998) Journal of Biology and Chemistry , vol.273 , pp. 14683-14689
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 92
    • 0021677474 scopus 로고
    • The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms
    • Morgenstern R, Lundqvist G, Andersson G, Balk L, DePierre JW. 1984. The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms. Biochemistry and Pharmacology 33(22):3609-3614.
    • (1984) Biochemistry and Pharmacology , vol.33 , Issue.22 , pp. 3609-3614
    • Morgenstern, R.1    Lundqvist, G.2    Andersson, G.3    Balk, L.4    DePierre, J.W.5
  • 93
    • 0024321876 scopus 로고
    • Activation of rat liver microsomal glutathione transferase by limited proteolysis
    • Morgenstern R, Lundqvist G, Jornvall H, DePierre JW. 1989. Activation of rat liver microsomal glutathione transferase by limited proteolysis. Biochemistry Journal 260(2):577-582.
    • (1989) Biochemistry Journal , vol.260 , Issue.2 , pp. 577-582
    • Morgenstern, R.1    Lundqvist, G.2    Jornvall, H.3    DePierre, J.W.4
  • 96
    • 0028914295 scopus 로고
    • Identification of a putative antioxidant response element in the 50-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene
    • Mulcahy RT, Gipp JJ. 1995. Identification of a putative antioxidant response element in the 50-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochemical and Biophysical Research Communications 209:227-233.
    • (1995) Biochemical and Biophysical Research Communications , vol.209 , pp. 227-233
    • Mulcahy, R.T.1    Gipp, J.J.2
  • 97
    • 0037172653 scopus 로고    scopus 로고
    • Polymorphism in the 5′-flanking region of human glutamate-cysteine ligase modifier subunit gene is associated with myocardial infarction
    • Nakamura S, Kugiyama K, Sugiyama S, Miyamoto S, Koide S, Fukushima H, Honda O, Yoshimura M, Ogawa H. 2002. Polymorphism in the 5′-flanking region of human glutamate-cysteine ligase modifier subunit gene is associated with myocardial infarction. Circulation 105(25):2968-2973.
    • (2002) Circulation , vol.105 , Issue.25 , pp. 2968-2973
    • Nakamura, S.1    Kugiyama, K.2    Sugiyama, S.3    Miyamoto, S.4    Koide, S.5    Fukushima, H.6    Honda, O.7    Yoshimura, M.8    Ogawa, H.9
  • 98
    • 0026376260 scopus 로고
    • Proposed role of drug-metabolizing enzymes: Regulation of steady state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions
    • Nebert DW. 1991. Proposed role of drug-metabolizing enzymes: Regulation of steady state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions. Molecular Endocrinology 5(9):1203-1214.
    • (1991) Molecular Endocrinology , vol.5 , Issue.9 , pp. 1203-1214
    • Nebert, D.W.1
  • 100
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • Owuor ED, Kong AN. 2002. Antioxidants and oxidants regulated signal transduction pathways. Biochemistry and Pharmacology 64(5-6):765-770.
    • (2002) Biochemistry and Pharmacology , vol.64 , Issue.5-6 , pp. 765-770
    • Owuor, E.D.1    Kong, A.N.2
  • 102
  • 103
    • 0033534153 scopus 로고    scopus 로고
    • An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases
    • Patskovsky YV, Patskovska LN, Listowsky I. 1999. An asparagine- phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry 38(49):16187-16194.
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16187-16194
    • Patskovsky, Y.V.1    Patskovska, L.N.2    Listowsky, I.3
  • 104
    • 0021368690 scopus 로고
    • Rat liver glutathione S-transferases. Complete nucleotide sequence of a glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital
    • Pickett CB, Telakowski-Hopkins CA, Ding GJ, Argenbright L, Lu AY. 1984. Rat liver glutathione S-transferases. Complete nucleotide sequence of a glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital. Journal of Biology and Chemistry 259(8):5182-5188.
    • (1984) Journal of Biology and Chemistry , vol.259 , Issue.8 , pp. 5182-5188
    • Pickett, C.B.1    Telakowski-Hopkins, C.A.2    Ding, G.J.3    Argenbright, L.4    Lu, A.Y.5
  • 105
    • 0029859993 scopus 로고    scopus 로고
    • Hormonal regulation of hepatic enzymes involved in foreign compound metabolism
    • Prough RA, Linder MW, Pinaire JA, Xiao GH, Falkner KC. 1996. Hormonal regulation of hepatic enzymes involved in foreign compound metabolism. FASEB Journal 10(12):1369-1377.
    • (1996) FASEB Journal , vol.10 , Issue.12 , pp. 1369-1377
    • Prough, R.A.1    Linder, M.W.2    Pinaire, J.A.3    Xiao, G.H.4    Falkner, K.C.5
  • 106
    • 0029814158 scopus 로고    scopus 로고
    • Characterization of the rat glutathione S-transferase Yc2 subunit gene, GSTA5: Identification of a putative antioxidant-responsive element in the 5′-flanking region of rat GSTA5 that may mediate chemoprotection against aflatoxin B1
    • Pulford DJ, Hayes JD. 1996. Characterization of the rat glutathione S-transferase Yc2 subunit gene, GSTA5: Identification of a putative antioxidant-responsive element in the 5′-flanking region of rat GSTA5 that may mediate chemoprotection against aflatoxin B1. Biochemistry Journal 318(1):75-84.
    • (1996) Biochemistry Journal , vol.318 , Issue.1 , pp. 75-84
    • Pulford, D.J.1    Hayes, J.D.2
  • 109
    • 0022606742 scopus 로고
    • Differences in stereoselectivity and catalytic efficiency of three human glutathione transferases in the conjugation of glutathione with 7 beta,8 alpha-dihydroxy-9 alpha,10 alpha-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene
    • Robertson I, Guthenberg C, Mannervik B, Jernstrom B. 1986. Differences in stereoselectivity and catalytic efficiency of three human glutathione transferases in the conjugation of glutathione with 7 beta,8 alpha-dihydroxy-9 alpha,10 alpha-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene. Cancer Research 46(5):2220-2224.
    • (1986) Cancer Research , vol.46 , Issue.5 , pp. 2220-2224
    • Robertson, I.1    Guthenberg, C.2    Mannervik, B.3    Jernstrom, B.4
  • 110
    • 28244483359 scopus 로고    scopus 로고
    • Urinary GSTP1-1 excretion is markedly increased in normotensive pregnancy as well as in preeclampsia
    • Roes E, Raijmakers MT, Roelofs HM, Peters WH, Steegers EA. 2005. Urinary GSTP1-1 excretion is markedly increased in normotensive pregnancy as well as in preeclampsia. Journal of Nephrology 18(4):405-408.
    • (2005) Journal of Nephrology , vol.18 , Issue.4 , pp. 405-408
    • Roes, E.1    Raijmakers, M.T.2    Roelofs, H.M.3    Peters, W.H.4    Steegers, E.A.5
  • 111
    • 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 JD, Nieves E, Listowsky I. 1997. Subunit diversity and tissue distribution of human glutathione S-transferases: Interpretations based on electrospray ionization-MS and peptide sequence-specific antisera. Biochemistry Journal 325(2):481-486.
    • (1997) Biochemistry Journal , vol.325 , Issue.2 , pp. 481-486
    • Rowe, J.D.1    Nieves, E.2    Listowsky, I.3
  • 112
    • 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
    • Rowe JD, Patskovsky YV, Patskovska LN, Novikova E, Listowsky I. 1998. Rationale for reclassification of a distinctive subdivision of mammalian class mu glutathione S-transferases that are primarily expressed in testis. Journal of Biology and Chemistry 273(16):9593-9601.
    • (1998) Journal of Biology and Chemistry , vol.273 , Issue.16 , pp. 9593-9601
    • Rowe, J.D.1    Patskovsky, Y.V.2    Patskovska, L.N.3    Novikova, E.4    Listowsky, I.5
  • 114
    • 23944491356 scopus 로고    scopus 로고
    • Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi, and theta glutathione S-transferases
    • Ruiz-Laguna J, Abril N, Prieto-Alamo MJ, Lopez-Barea J, Pueyo C. 2005. Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi, and theta glutathione S-transferases. Gene Expression 12(3):165-176.
    • (2005) Gene Expression , vol.12 , Issue.3 , pp. 165-176
    • Ruiz-Laguna, J.1    Abril, N.2    Prieto-Alamo, M.J.3    Lopez-Barea, J.4    Pueyo, C.5
  • 115
    • 0027300033 scopus 로고
    • Glutathione S-transferases, structure, regulation, and therapeutic implications
    • Rushmore T, Pickett C. 1993. Glutathione S-transferases, structure, regulation, and therapeutic implications. Journal of Biology and Chemistry 268(16):11475-11478.
    • (1993) Journal of Biology and Chemistry , vol.268 , Issue.16 , pp. 11475-11478
    • Rushmore, T.1    Pickett, C.2
  • 116
    • 23144451444 scopus 로고    scopus 로고
    • Oxidative stress: Molecular perception and transduction of signals triggering antioxidant gene defenses
    • Scandalios JG. 2005. Oxidative stress: Molecular perception and transduction of signals triggering antioxidant gene defenses. Brazilian Journal of Medicine and Biology Research 38(7):995-1014.
    • (2005) Brazilian Journal of Medicine and Biology Research , vol.38 , Issue.7 , pp. 995-1014
    • Scandalios, J.G.1
  • 117
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D, Meade G, Foley VM, Dowd CA. 2001. Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochemistry Journal 360(1):1-16.
    • (2001) Biochemistry Journal , vol.360 , Issue.1 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 119
    • 0034718969 scopus 로고    scopus 로고
    • Cadmium-induced elevations in the gene expression of the regulatory subunit of gamma-glutamylcysteine synthetase in rat lung and alveolar epithelial cells
    • Shukla GS, Chiu J, Hart BA. 2000a. Cadmium-induced elevations in the gene expression of the regulatory subunit of gamma-glutamylcysteine synthetase in rat lung and alveolar epithelial cells. Toxicology 151(1-3):45-54.
    • (2000) Toxicology , vol.151 , Issue.1-3 , pp. 45-54
    • Shukla, G.S.1    Chiu, J.2    Hart, B.A.3
  • 120
    • 0034481707 scopus 로고    scopus 로고
    • Cadmium-mediated oxidative stress in alveolar epithelial cells induces the expression of gamma-glutamylcysteine synthetase catalytic subunit and glutathione S-transferase alpha and pi isoforms: Potential role of activator protein-1
    • Shukla GS, Shukla A, Potts RJ, Osier M, Hart BA, Chiu JF. 2000b. Cadmium-mediated oxidative stress in alveolar epithelial cells induces the expression of gamma-glutamylcysteine synthetase catalytic subunit and glutathione S-transferase alpha and pi isoforms: Potential role of activator protein-1. Cell Biology and Toxicology 16(6):347-362.
    • (2000) Cell Biology and Toxicology , vol.16 , Issue.6 , pp. 347-362
    • Shukla, G.S.1    Shukla, A.2    Potts, R.J.3    Osier, M.4    Hart, B.A.5    Chiu, J.F.6
  • 122
    • 0030834975 scopus 로고    scopus 로고
    • Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase
    • Sies H, Sharov VS, Klotz LO, Briviba K. 1997. Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase. Journal of Biology and Chemistry 272(44):27812-27817.
    • (1997) Journal of Biology and Chemistry , vol.272 , Issue.44 , pp. 27812-27817
    • Sies, H.1    Sharov, V.S.2    Klotz, L.O.3    Briviba, K.4
  • 123
    • 0037371945 scopus 로고    scopus 로고
    • The expanding network of redox signaling: New observations, complexities, and perspectives
    • Soberman RJ. 2003. The expanding network of redox signaling: New observations, complexities, and perspectives. Journal of Clinical Investigation 111(5):571-574.
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.5 , pp. 571-574
    • Soberman, R.J.1
  • 124
    • 0037397016 scopus 로고    scopus 로고
    • The organization and consequences of eicosanoid signaling
    • Soberman RJ, Christmas P. 2003. The organization and consequences of eicosanoid signaling. Journal of Clinical Investigation 111(8):1107-1113.
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.8 , pp. 1107-1113
    • Soberman, R.J.1    Christmas, P.2
  • 126
    • 0036845192 scopus 로고    scopus 로고
    • Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels
    • Stipanuk MH, Londono M, Lee JI, Hu M, Yu AF. 2002. Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels. Journal of Nutrition 132(11):3369-3378.
    • (2002) Journal of Nutrition , vol.132 , Issue.11 , pp. 3369-3378
    • Stipanuk, M.H.1    Londono, M.2    Lee, J.I.3    Hu, M.4    Yu, A.F.5
  • 127
    • 19544372581 scopus 로고    scopus 로고
    • Pi class glutathione S-transferase genes are regulated by Nrf 2 through an evolutionarily conserved regulatory element in zebrafish
    • Suzuki T, Takagi Y, Osanai H, Li L, Takeuchi M, Katoh Y, Kobayashi M, Yamamoto M. 2005. Pi class glutathione S-transferase genes are regulated by Nrf 2 through an evolutionarily conserved regulatory element in zebrafish. Biochemistry Journal 388(1):65-73.
    • (2005) Biochemistry Journal , vol.388 , Issue.1 , pp. 65-73
    • Suzuki, T.1    Takagi, Y.2    Osanai, H.3    Li, L.4    Takeuchi, M.5    Katoh, Y.6    Kobayashi, M.7    Yamamoto, M.8
  • 128
    • 0023186348 scopus 로고
    • Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme
    • Takahashi K, Avissar N, Whitin J, Cohen H. 1987. Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme. Archives in Biochemistry and Biophysics 256(2):677-686.
    • (1987) Archives in Biochemistry and Biophysics , vol.256 , Issue.2 , pp. 677-686
    • Takahashi, K.1    Avissar, N.2    Whitin, J.3    Cohen, H.4
  • 129
    • 0027416417 scopus 로고
    • A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5
    • Takahashi Y, Campbell E, Hirata Y, Takayama T, Listowsky I. 1993. A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5. Journal of Biology and Chemistry 268(12):8893-8898.
    • (1993) Journal of Biology and Chemistry , vol.268 , Issue.12 , pp. 8893-8898
    • Takahashi, Y.1    Campbell, E.2    Hirata, Y.3    Takayama, T.4    Listowsky, I.5
  • 131
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew K. 1994. Glutathione-associated enzymes in anticancer drug resistance. Cancer Research 54(16):4313-4320.
    • (1994) Cancer Research , vol.54 , Issue.16 , pp. 4313-4320
    • Tew, K.1
  • 132
    • 0032429022 scopus 로고    scopus 로고
    • Expression of extracellular glutathione peroxidase in human and mouse gastrointestinal tract
    • Tham DM, Whitin JC, Kim KK, Zhu SX, Cohen HJ. 1998. Expression of extracellular glutathione peroxidase in human and mouse gastrointestinal tract. American Journal of Physiology 275(6/1):G1463-G1471.
    • (1998) American Journal of Physiology , vol.275 , Issue.1-6
    • Tham, D.M.1    Whitin, J.C.2    Kim, K.K.3    Zhu, S.X.4    Cohen, H.J.5
  • 133
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • Thimmulappa RK, Mai KH, Srisuma S, Kensler TW, Yamamoto M, Biswal S. 2002. Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray. Cancer Research 62(18):5196-5203.
    • (2002) Cancer Research , vol.62 , Issue.18 , pp. 5196-5203
    • Thimmulappa, R.K.1    Mai, K.H.2    Srisuma, S.3    Kensler, T.W.4    Yamamoto, M.5    Biswal, S.6
  • 135
    • 23944438362 scopus 로고    scopus 로고
    • Gonadotropin regulation of glutamate cysteine ligase catalytic and modifier subunit expression in rat ovary is subunit and follicle stage specific
    • Tsai-Turton M, Luderer U. 2005. Gonadotropin regulation of glutamate cysteine ligase catalytic and modifier subunit expression in rat ovary is subunit and follicle stage specific. American Journal of Physiology. Endocrinology and Metabolism 289(3):E391-E402.
    • (2005) American Journal of Physiology. Endocrinology and Metabolism , vol.289 , Issue.3
    • Tsai-Turton, M.1    Luderer, U.2
  • 136
    • 0029591133 scopus 로고
    • Mapping of the glutamate-cysteine ligase catalytic subunit gene (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22 and mouse chromosome 3H1-3
    • Tsuchiya K, Mulcahy RT, Reid LL, Disteche CM, Kavanagh TJ. 1995. Mapping of the glutamate-cysteine ligase catalytic subunit gene (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22 and mouse chromosome 3H1-3. Genomics 30(3):630-632.
    • (1995) Genomics , vol.30 , Issue.3 , pp. 630-632
    • Tsuchiya, K.1    Mulcahy, R.T.2    Reid, L.L.3    Disteche, C.M.4    Kavanagh, T.J.5
  • 137
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini F, Maiorino M, Gregolin C. 1985. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochimica et Biophysica Acta 839(1):62-70.
    • (1985) Biochimica et Biophysica Acta , vol.839 , Issue.1 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 139
    • 0034071372 scopus 로고    scopus 로고
    • Regulation of gamma-glutamylcysteine synthetase subunit gene expression: Insights into transcriptional control of antioxidant defenses
    • Wild AC, Mulcahy RT. 2000. Regulation of gamma-glutamylcysteine synthetase subunit gene expression: Insights into transcriptional control of antioxidant defenses. Free Radicals in Biology and Medicine 32:281-301.
    • (2000) Free Radicals in Biology and Medicine , vol.32 , pp. 281-301
    • Wild, A.C.1    Mulcahy, R.T.2
  • 141
    • 21944452087 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1
    • Yang H, Magilnick N, Lee C, Kalmaz D, Ou X, Chan JY, Lu SC. 2005. Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1. Molecular Cell Biology 25(14):5933-5946.
    • (2005) Molecular Cell Biology , vol.25 , Issue.14 , pp. 5933-5946
    • Yang, H.1    Magilnick, N.2    Lee, C.3    Kalmaz, D.4    Ou, X.5    Chan, J.Y.6    Lu, S.C.7
  • 142
    • 0037147240 scopus 로고    scopus 로고
    • Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouse. Novel model system for a severely compromised oxidative stress response
    • Yang Y, Dieter MZ, Chen Y, Shertzer HG, Nebert DW, Dalton TP. 2002. Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouse. Novel model system for a severely compromised oxidative stress response. Journal of Biology and Chemistry 277(51):49446-49452.
    • (2002) Journal of Biology and Chemistry , vol.277 , Issue.51 , pp. 49446-49452
    • Yang, Y.1    Dieter, M.Z.2    Chen, Y.3    Shertzer, H.G.4    Nebert, D.W.5    Dalton, T.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.