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Volumn 224, Issue 2, 2005, Pages 171-184

Nrf2 as a novel molecular target for chemoprevention

Author keywords

Antioxidant response element (ARE) electrophile response element (EpRE); Chemoprevention; Kelch like ECH associated protein 1 (Keap1); Nuclear transcription factor erythroid 2p45 (NF E2) related factor 2 (Nrf2)

Indexed keywords

1,2 DITHIOLE 3 THIONE DERIVATIVE; 3H 1,2 DITHIOL 3 THIONE; 4' BROMOFLAVONE; 6 (METHYLSULFINYL)HEXYLISOTHIOCYANATE; ACETYLCYSTEINE; ANETHOLE TRITHIONE; ANTINEOPLASTIC AGENT; ANTIOXIDANT; BETA NAPHTHOFLAVONE; CAFFEIC ACID PHENETHYL ESTER; CURCUMIN; DNA; EPICATECHIN GALLATE; EPIGALLOCATECHIN GALLATE; FLAVONE DERIVATIVE; ISOTHIOCYANIC ACID DERIVATIVE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; LEUCINE ZIPPER PROTEIN; OLTIPRAZ; PROTEIN; RETINOIC ACID; SULFORAPHANE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; ZERUMBONE;

EID: 19444379739     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2004.09.042     Document Type: Review
Times cited : (471)

References (118)
  • 1
    • 0142166328 scopus 로고    scopus 로고
    • Cancer chemoprevention with dietary phytochemicals
    • Y.-J. Surh Cancer chemoprevention with dietary phytochemicals Nature Rev. Cancer 3 2003 768 780
    • (2003) Nature Rev. Cancer , vol.3 , pp. 768-780
    • Surh, Y.-J.1
  • 2
    • 0017809827 scopus 로고
    • The multistage theory of carcinogenesis and the age distribution of cancer in man
    • S.H. Moolgavkar The multistage theory of carcinogenesis and the age distribution of cancer in man J. Natl. Cancer Inst. 61 1978 49 52
    • (1978) J. Natl. Cancer Inst. , vol.61 , pp. 49-52
    • Moolgavkar, S.H.1
  • 3
    • 84965088319 scopus 로고
    • A two-stage theory of carcinogenesis in relation to the age distribution of human cancer
    • P. Armitage, and R. Doll A two-stage theory of carcinogenesis in relation to the age distribution of human cancer Br. J. Cancer 11 1957 161 169
    • (1957) Br. J. Cancer , vol.11 , pp. 161-169
    • Armitage, P.1    Doll, R.2
  • 4
    • 0036637235 scopus 로고    scopus 로고
    • Chemoprevention: An essential approach to controlling cancer
    • M.B. Sporn, and N. Suh Chemoprevention: an essential approach to controlling cancer Nature Rev. Cancer 2 2002 537 543
    • (2002) Nature Rev. Cancer , vol.2 , pp. 537-543
    • Sporn, M.B.1    Suh, N.2
  • 5
    • 0032739622 scopus 로고    scopus 로고
    • Cancer chemoprevention: Progress and promise
    • G.J. Kelloff, C.C. Sigman, and P. Greenwald Cancer chemoprevention: progress and promise Eur. J. Cancer 35 1999 1755 1762
    • (1999) Eur. J. Cancer , vol.35 , pp. 1755-1762
    • Kelloff, G.J.1    Sigman, C.C.2    Greenwald, P.3
  • 6
    • 0037105738 scopus 로고    scopus 로고
    • Cancer prevention science and practice
    • S.M. Lippman, and W.K. Hong Cancer prevention science and practice Cancer Res. 62 2002 5119 5125
    • (2002) Cancer Res. , vol.62 , pp. 5119-5125
    • Lippman, S.M.1    Hong, W.K.2
  • 7
  • 8
    • 0034011263 scopus 로고    scopus 로고
    • Chemoprevention of cancer
    • M.B. Sporn, and N. Suh Chemoprevention of cancer Carcinogenesis 21 2000 525 530
    • (2000) Carcinogenesis , vol.21 , pp. 525-530
    • Sporn, M.B.1    Suh, N.2
  • 9
    • 0026323687 scopus 로고
    • Carcinogenesis and cancer: Different perspectives on the same disease
    • M.B. Sporn Carcinogenesis and cancer: different perspectives on the same disease Cancer Res. 51 1991 6215 6218
    • (1991) Cancer Res. , vol.51 , pp. 6215-6218
    • Sporn, M.B.1
  • 10
    • 0021934758 scopus 로고
    • Chemoprevention of cancer
    • L.W. Wattenberg Chemoprevention of cancer Cancer Res. 45 1985 1 8
    • (1985) Cancer Res. , vol.45 , pp. 1-8
    • Wattenberg, L.W.1
  • 12
    • 2942568014 scopus 로고    scopus 로고
    • Dietary chemopreventive compounds and ARE/EpRE signaling
    • C. Chen, and A.N. Kong Dietary chemopreventive compounds and ARE/EpRE signaling Free Radic. Biol. Med. 36 2004 1505 1516
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1505-1516
    • Chen, C.1    Kong, A.N.2
  • 13
    • 0035965945 scopus 로고    scopus 로고
    • Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention
    • J.D. Hayes, and M. McMahon Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention Cancer Lett. 174 2001 103 113
    • (2001) Cancer Lett. , vol.174 , pp. 103-113
    • Hayes, J.D.1    McMahon, M.2
  • 14
    • 4444315787 scopus 로고    scopus 로고
    • A strategy for cancer prevention: Stimulation of the Nrf2-ARE signaling pathway
    • Y. Zhang, and B. Gordon A strategy for cancer prevention: stimulation of the Nrf2-ARE signaling pathway Mol. Cancer Ther. 3 2004 885 893
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 885-893
    • Zhang, Y.1    Gordon, B.2
  • 16
    • 0016573535 scopus 로고
    • Effects of dietary constituents on the metabolism of chemical carcinogens
    • L.W. Wattenberg Effects of dietary constituents on the metabolism of chemical carcinogens Cancer Res. 35 1975 3326 3331
    • (1975) Cancer Res. , vol.35 , pp. 3326-3331
    • Wattenberg, L.W.1
  • 18
    • 0018116175 scopus 로고
    • Elevation of hepatic glutathione S-transferase activities and protection against mutagenic metabolites of benzo(a)pyrene by dietary antioxidants
    • A.M. Benson, R.P. Batzinger, S.Y. Ou, E. Bueding, Y.N. Cha, and P. Talalay Elevation of hepatic glutathione S-transferase activities and protection against mutagenic metabolites of benzo(a)pyrene by dietary antioxidants Cancer Res. 38 1978 4486 4495
    • (1978) Cancer Res. , vol.38 , pp. 4486-4495
    • Benson, A.M.1    Batzinger, R.P.2    Ou, S.Y.3    Bueding, E.4    Cha, Y.N.5    Talalay, P.6
  • 19
    • 0019142866 scopus 로고
    • Increase of NAD(P)H:quinone reductase by dietary antioxidants: Possible role in protection against carcinogenesis and toxicity
    • A.M. Benson, M.J. Hunkeler, and P. Talalay Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity Proc. Natl. Acad. Sci. USA 77 1980 5216 5220
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5216-5220
    • Benson, A.M.1    Hunkeler, M.J.2    Talalay, P.3
  • 20
    • 0019955793 scopus 로고
    • Comparative effects of dietary administration of 2(3)-tert-butyl-4- hydroxyanisole and 3,5-di-tert-butyl-4-hydroxytoluene on several hepatic enzyme activities in mice and rats
    • Y.N. Cha, and S. Heine Comparative effects of dietary administration of 2(3)-tert-butyl-4-hydroxyanisole and 3,5-di-tert-butyl-4-hydroxytoluene on several hepatic enzyme activities in mice and rats Cancer Res. 42 1982 2609 2615
    • (1982) Cancer Res. , vol.42 , pp. 2609-2615
    • Cha, Y.N.1    Heine, S.2
  • 21
    • 0018760217 scopus 로고
    • Elevation of extrahepatic glutathione S-transferase and epoxide hydratase activities by 2(3)-tert-butyl-4-hydroxyanisole
    • A.M. Benson, Y.N. Cha, E. Bueding, H.S. Heine, and P. Talalay Elevation of extrahepatic glutathione S-transferase and epoxide hydratase activities by 2(3)-tert-butyl-4-hydroxyanisole Cancer Res. 39 1979 2971 2977
    • (1979) Cancer Res. , vol.39 , pp. 2971-2977
    • Benson, A.M.1    Cha, Y.N.2    Bueding, E.3    Heine, H.S.4    Talalay, P.5
  • 22
    • 0021695489 scopus 로고
    • New aspects of glutathione biochemistry and transport - Selective alteration of glutathione metabolism
    • A. Meister New aspects of glutathione biochemistry and transport - selective alteration of glutathione metabolism Nutr. Rev. 42 1984 397 410
    • (1984) Nutr. Rev. , vol.42 , pp. 397-410
    • Meister, A.1
  • 23
    • 0029019008 scopus 로고
    • Identification of a second region upstream of the mouse hemeoxygenase-1 gene that functions as a basal level and inducer-dependent transcription enhancer
    • J. Alam, S. Camhi, and M. Choi Identification of a second region upstream of the mouse hemeoxygenase-1 gene that functions as a basal level and inducer-dependent transcription enhancer J. Biol. Chem. 270 1995 11977 11984
    • (1995) J. Biol. Chem. , vol.270 , pp. 11977-11984
    • Alam, J.1    Camhi, S.2    Choi, M.3
  • 24
    • 0029830816 scopus 로고    scopus 로고
    • Induction of hepatic hemeoxygenase-1 and ferritin in rats by cancer chemopreventive dithiolethiones
    • T. Primiano, T.W. Kensler, P. Kuppusamy, J.L. Zweier, and R. Sutter Induction of hepatic hemeoxygenase-1 and ferritin in rats by cancer chemopreventive dithiolethiones Carcinogenesis 17 1996 2291 2296
    • (1996) Carcinogenesis , vol.17 , pp. 2291-2296
    • Primiano, T.1    Kensler, T.W.2    Kuppusamy, P.3    Zweier, J.L.4    Sutter, R.5
  • 25
    • 0031950013 scopus 로고    scopus 로고
    • Identification of dithiolethione-inducible gene-1 as a leukotriene B4 12-hydroxydehydrogenase: Implications for chemoprevention
    • T. Primiano, Y. Li, T.W. Kensler, M.A. Trush, and R. Sutter Identification of dithiolethione-inducible gene-1 as a leukotriene B4 12-hydroxydehydrogenase: implications for chemoprevention Carcinogenesis 19 1998 999 1005
    • (1998) Carcinogenesis , vol.19 , pp. 999-1005
    • Primiano, T.1    Li, Y.2    Kensler, T.W.3    Trush, M.A.4    Sutter, R.5
  • 26
    • 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 B. Pickett The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity J. Biol. Chem. 266 1991 11632 11639
    • (1991) J. Biol. Chem. , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, B.3
  • 27
    • 0025368036 scopus 로고
    • Regulation of glutathione S-transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds
    • T.H. Rushmore, R.G. King, K.E. Paulson, and B. Pickett Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds Proc. Natl. Acad. Sci. USA 87 1990 3826 3830
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3826-3830
    • Rushmore, T.H.1    King, R.G.2    Paulson, K.E.3    Pickett, B.4
  • 28
    • 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
    • S.A. Chanas, Q. Jiang, M. McMahon, G.K. McWalter, L.I. McLellan, and C.R. Elcombe 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 Biochem. J. 365 2002 405 416
    • (2002) Biochem. J. , vol.365 , pp. 405-416
    • Chanas, S.A.1    Jiang, Q.2    McMahon, M.3    McWalter, G.K.4    McLellan, L.I.5    Elcombe, C.R.6
  • 29
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • K. Itoh, T. Chiba, S. Takahashi, T. Ishii, K. Igarashi, and Y. Katoh An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements Biochem. Biophys. Res. Commun. 236 1997 313 322
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 313-322
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3    Ishii, T.4    Igarashi, K.5    Katoh, Y.6
  • 30
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
    • M. Ramos-Gomez, M.K. Kwak, P.M. Dolan, K. Itoh, M. Yamamoto, and P. Talalay Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice Proc. Natl. Acad. Sci. USA 98 2001 3410 3415
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3410-3415
    • Ramos-Gomez, M.1    Kwak, M.K.2    Dolan, P.M.3    Itoh, K.4    Yamamoto, M.5    Talalay, P.6
  • 31
    • 0036479330 scopus 로고    scopus 로고
    • A sulforaphane analogue that potently activates the Nrf2-dependent detoxification pathway
    • Y. Morimitsu, Y. Nakagawa, K. Hayashi, H. Fujii, T. Kumagai, and Y. Nakamura A sulforaphane analogue that potently activates the Nrf2-dependent detoxification pathway J. Biol. Chem. 277 2002 3456 3463
    • (2002) J. Biol. Chem. , vol.277 , pp. 3456-3463
    • Morimitsu, Y.1    Nakagawa, Y.2    Hayashi, K.3    Fujii, H.4    Kumagai, T.5    Nakamura, Y.6
  • 32
    • 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
    • J.M. Lee, M.J. Calkins, K. Chan, Y.W. Kan, and J.A. Johnson Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis J. Biol. Chem. 278 2003 12029 12038
    • (2003) J. Biol. Chem. , vol.278 , pp. 12029-12038
    • Lee, J.M.1    Calkins, M.J.2    Chan, K.3    Kan, Y.W.4    Johnson, J.A.5
  • 33
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • R.K. Thimmulappa, K.H. Mai, S. Srisuma, T.W. Kensler, M. Yamamoto, and S. Biswal Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray Cancer Res. 62 2002 5196 5203
    • (2002) Cancer Res. , vol.62 , pp. 5196-5203
    • Thimmulappa, R.K.1    Mai, K.H.2    Srisuma, S.3    Kensler, T.W.4    Yamamoto, M.5    Biswal, S.6
  • 34
    • 0036890106 scopus 로고    scopus 로고
    • Expression and regulation of glutathione S-transferase P1-1 in cultured human epidermal cells
    • Y. Zhang, V. Gonzalez, and J. Xu Expression and regulation of glutathione S-transferase P1-1 in cultured human epidermal cells J. Dermatol. Sci. 30 2002 205 214
    • (2002) J. Dermatol. Sci. , vol.30 , pp. 205-214
    • Zhang, Y.1    Gonzalez, V.2    Xu, J.3
  • 35
    • 0042330074 scopus 로고    scopus 로고
    • Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: Reassessment of the ARE consensus sequence
    • P. Nioi, M. McMahon, K. Itoh, M. Yamamoto, and J.D. Hayes Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence Biochem. J. 374 2003 337 348
    • (2003) Biochem. J. , vol.374 , pp. 337-348
    • Nioi, P.1    McMahon, M.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 36
    • 0037424262 scopus 로고    scopus 로고
    • Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival
    • M.K. Kwak, N. Wakabayashi, K. Itoh, H. Motohashi, M. Yamamoto, and T.W. Kensler Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival J. Biol. Chem. 278 2003 8135 8145
    • (2003) J. Biol. Chem. , vol.278 , pp. 8135-8145
    • Kwak, M.K.1    Wakabayashi, N.2    Itoh, K.3    Motohashi, H.4    Yamamoto, M.5    Kensler, T.W.6
  • 37
    • 0037016759 scopus 로고    scopus 로고
    • Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells
    • J. Li, J.M. Lee, and J.A. Johnson Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells J. Biol. Chem. 277 2002 388 394
    • (2002) J. Biol. Chem. , vol.277 , pp. 388-394
    • Li, J.1    Lee, J.M.2    Johnson, J.A.3
  • 39
    • 0001143581 scopus 로고
    • On the mechanisms of induction of cancer-protective enzymes: A unifying proposal
    • H.J. Prochaska, M.J. De Long, and P. Talalay On the mechanisms of induction of cancer-protective enzymes: a unifying proposal Proc. Natl. Acad. Sci. USA 82 1985 8232 8236
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8232-8236
    • Prochaska, H.J.1    De Long, M.J.2    Talalay, P.3
  • 40
    • 0026022976 scopus 로고
    • The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations
    • S.R. Spencer, L.A. Xue, E.M. Klenz, and P. Talalay The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations Biochem. J. 273 1991 711 717
    • (1991) Biochem. J. , vol.273 , pp. 711-717
    • Spencer, S.R.1    Xue, L.A.2    Klenz, E.M.3    Talalay, P.4
  • 41
    • 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 J. Prochaska Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis Proc. Natl. Acad. Sci. USA 85 1988 8261 8265
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8261-8265
    • Talalay, P.1    De Long, M.J.2    Prochaska, J.3
  • 42
    • 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, and J.D. Engel Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain Genes Dev. 13 1999 76 86
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6
  • 43
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • P. Moi, K. Chan, I. Asunis, A. Cao, and W. Kan Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region Proc. Natl. Acad. Sci. USA 91 1994 9926 9930
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, W.5
  • 45
    • 0035836698 scopus 로고    scopus 로고
    • An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen
    • K. Chan, X.D. Han, and W. Kan An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen Proc. Natl. Acad. Sci. USA 98 2001 4611 4616
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4611-4616
    • Chan, K.1    Han, X.D.2    Kan, W.3
  • 46
    • 0035870298 scopus 로고    scopus 로고
    • The Cap'n'Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes
    • M. McMahon, K. Itoh, M. Yamamoto, S.A. Chanas, C.J. Henderson, and L.I. McLellan The Cap'n'Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes Cancer Res. 61 2001 3299 3307
    • (2001) Cancer Res. , vol.61 , pp. 3299-3307
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Chanas, S.A.4    Henderson, C.J.5    McLellan, L.I.6
  • 47
    • 0035153227 scopus 로고    scopus 로고
    • High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes
    • A. Enomoto, K. Itoh, E. Nagayoshi, J. Haruta, T. Kimura, and T. O'Connor High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes Toxicol. Sci. 59 2001 169 177
    • (2001) Toxicol. Sci. , vol.59 , pp. 169-177
    • Enomoto, A.1    Itoh, K.2    Nagayoshi, E.3    Haruta, J.4    Kimura, T.5    O'Connor, T.6
  • 48
    • 13044304201 scopus 로고    scopus 로고
    • Nrf2 is essential for protection against acute pulmonary injury in mice
    • K. Chan, and W. Kan Nrf2 is essential for protection against acute pulmonary injury in mice Proc. Natl. Acad. Sci. USA 96 1999 12731 12736
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12731-12736
    • Chan, K.1    Kan, W.2
  • 49
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • T. Ishii, K. Itoh, S. Takahashi, H. Sato, T. Yanagawa, and Y. Katoh Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages J. Biol. Chem. 275 2000 16023 16029
    • (2000) J. Biol. Chem. , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6
  • 50
    • 0037356451 scopus 로고    scopus 로고
    • Interactive effects of nrf2 genotype and oltipraz on benzo[a]pyrene-DNA adducts and tumor yield in mice
    • M. Ramos-Gomez, P.M. Dolan, K. Itoh, M. Yamamoto, and T.W. Kensler Interactive effects of nrf2 genotype and oltipraz on benzo[a]pyrene-DNA adducts and tumor yield in mice Carcinogenesis 24 2003 461 467
    • (2003) Carcinogenesis , vol.24 , pp. 461-467
    • Ramos-Gomez, M.1    Dolan, P.M.2    Itoh, K.3    Yamamoto, M.4    Kensler, T.W.5
  • 51
    • 0037188518 scopus 로고    scopus 로고
    • Sulforaphane inhibits extracellular, intracellular, and antibiotic-resistant strains of Helicobacter pylori and prevents benzo[a]pyrene-induced stomach tumors
    • J.W. Fahey, X. Haristoy, P.M. Dolan, T.W. Kensler, I. Scholtus, and K.K. Stephenson Sulforaphane inhibits extracellular, intracellular, and antibiotic-resistant strains of Helicobacter pylori and prevents benzo[a]pyrene-induced stomach tumors Proc. Natl. Acad. Sci. USA 99 2002 7610 7615
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7610-7615
    • Fahey, J.W.1    Haristoy, X.2    Dolan, P.M.3    Kensler, T.W.4    Scholtus, I.5    Stephenson, K.K.6
  • 53
    • 0034672595 scopus 로고    scopus 로고
    • Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein
    • J.Y. Chan, and M. Kwong Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein Biochim. Biophys. Acta 1517 2000 19 26
    • (2000) Biochim. Biophys. Acta , vol.1517 , pp. 19-26
    • Chan, J.Y.1    Kwong, M.2
  • 54
    • 3042752557 scopus 로고    scopus 로고
    • Nrf2-dependent gene expressions: A molecular toxicological aspect
    • S. Numazawa, and T. Yoshida Nrf2-dependent gene expressions: a molecular toxicological aspect J. Toxicol. Sci. 29 2004 81 89
    • (2004) J. Toxicol. Sci. , vol.29 , pp. 81-89
    • Numazawa, S.1    Yoshida, T.2
  • 55
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • A.T. Dinkova-Kostova, W.D. Holtzclaw, R.N. Cole, K. Itoh, N. Wakabayashi, and Y. Katoh Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants Proc. Natl. Acad. Sci. USA 99 2002 11908 11913
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6
  • 56
    • 0037183998 scopus 로고    scopus 로고
    • The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • L.M. Zipper, and T. Mulcahy The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm J. Biol. Chem. 277 2002 36544 36552
    • (2002) J. Biol. Chem. , vol.277 , pp. 36544-36552
    • Zipper, L.M.1    Mulcahy, T.2
  • 57
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • M.I. Kang, A. Kobayashi, N. Wakabayashi, S.G. Kim, and M. Yamamoto Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes Proc. Natl. Acad. Sci. USA 101 2004 2046 2051
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 58
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • D.D. Zhang, and M. Hannink Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress Mol. Cell. Biol. 23 2003 8137 8151
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 59
    • 1242296811 scopus 로고    scopus 로고
    • Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers
    • N. Wakabayashi, A.T. Dinkova-Kostova, W.D. Holtzclaw, M.I. Kang, A. Kobayashi, and M. Yamamoto Protection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the Keap1 sensor modified by inducers Proc. Natl. Acad. Sci. USA 101 2004 2040 2045
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2040-2045
    • Wakabayashi, N.1    Dinkova-Kostova, A.T.2    Holtzclaw, W.D.3    Kang, M.I.4    Kobayashi, A.5    Yamamoto, M.6
  • 60
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • D. Stewart, E. Killeen, R. Naquin, S. Alam, and J. Alam Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium J. Biol. Chem. 278 2003 2396 2402
    • (2003) J. Biol. Chem. , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 61
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome
    • T. Nguyen, P.J. Sherratt, H.C. Huang, C.S. Yang, and B. Pickett Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome J. Biol. Chem. 278 2003 4536 4541
    • (2003) J. Biol. Chem. , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3    Yang, C.S.4    Pickett, B.5
  • 62
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • M. McMahon, K. Itoh, M. Yamamoto, and J.D. Hayes Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression J. Biol. Chem. 278 2003 21592 21600
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 63
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • K. Itoh, N. Wakabayashi, Y. Katoh, T. Ishii, T. O'Connor, and M. Yamamoto Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles Genes Cells 8 2003 379 391
    • (2003) Genes Cells , vol.8 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 64
    • 0029890442 scopus 로고    scopus 로고
    • Control of gene expression by proteolysis
    • H.L. Pahl, and A. Baeuerle Control of gene expression by proteolysis Curr. Opin. Cell Biol. 8 1996 340 347
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 340-347
    • Pahl, H.L.1    Baeuerle, A.2
  • 65
    • 0034723357 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase negatively regulates the induction of phase II drug-metabolizing enzymes that detoxify carcinogens
    • R. Yu, S. Mandlekar, W. Lei, W.E. Fahl, T.H. Tan, and A.N. Kong p38 mitogen-activated protein kinase negatively regulates the induction of phase II drug-metabolizing enzymes that detoxify carcinogens J. Biol. Chem. 275 2000 2322 2327
    • (2000) J. Biol. Chem. , vol.275 , pp. 2322-2327
    • Yu, R.1    Mandlekar, S.2    Lei, W.3    Fahl, W.E.4    Tan, T.H.5    Kong, A.N.6
  • 66
    • 0037569694 scopus 로고    scopus 로고
    • Curcumin activates the haemoxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element
    • E. Balogun, M. Hoque, P. Gong, E. Killeen, C.J. Green, and R. Foresti Curcumin activates the haemoxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element Biochem. J. 371 2003 887 895
    • (2003) Biochem. J. , vol.371 , pp. 887-895
    • Balogun, E.1    Hoque, M.2    Gong, P.3    Killeen, E.4    Green, C.J.5    Foresti, R.6
  • 67
    • 0033731182 scopus 로고    scopus 로고
    • Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2
    • H.C. Huang, T. Nguyen, and B. Pickett Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2 Proc. Natl. Acad. Sci. USA 97 2000 12475 12480
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12475-12480
    • Huang, H.C.1    Nguyen, T.2    Pickett, B.3
  • 68
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • H.C. Huang, T. Nguyen, and B. Pickett Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription J. Biol. Chem. 277 2002 42769 42774
    • (2002) J. Biol. Chem. , vol.277 , pp. 42769-42774
    • Huang, H.C.1    Nguyen, T.2    Pickett, B.3
  • 69
    • 0041742490 scopus 로고    scopus 로고
    • Atypical protein kinase C mediates activation of NF-E2-related factor 2 in response to oxidative stress
    • S. Numazawa, M. Ishikawa, A. Yoshida, S. Tanaka, and T. Yoshida Atypical protein kinase C mediates activation of NF-E2-related factor 2 in response to oxidative stress Am. J. Physiol. Cell Physiol. 285 2003 C334 C342
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Numazawa, S.1    Ishikawa, M.2    Yoshida, A.3    Tanaka, S.4    Yoshida, T.5
  • 70
    • 0242666198 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression
    • D.A. Bloom, and K. Jaiswal Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression J. Biol. Chem. 278 2003 44675 44682
    • (2003) J. Biol. Chem. , vol.278 , pp. 44675-44682
    • Bloom, D.A.1    Jaiswal, K.2
  • 71
    • 0036840585 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress
    • K.W. Kang, S.J. Lee, J.W. Park, and S.G. Kim Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress Mol. Pharmacol. 62 2002 1001 1010
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1001-1010
    • Kang, K.W.1    Lee, S.J.2    Park, J.W.3    Kim, S.G.4
  • 72
    • 0035827505 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase, not extracellular signal-regulated kinase, regulates activation of the antioxidant-responsive element in IMR-32 human neuroblastoma cells
    • J.M. Lee, J.M. Hanson, W.A. Chu, and J.A. Johnson Phosphatidylinositol 3-kinase, not extracellular signal-regulated kinase, regulates activation of the antioxidant-responsive element in IMR-32 human neuroblastoma cells J. Biol. Chem. 276 2001 20011 20016
    • (2001) J. Biol. Chem. , vol.276 , pp. 20011-20016
    • Lee, J.M.1    Hanson, J.M.2    Chu, W.A.3    Johnson, J.A.4
  • 73
    • 0036436025 scopus 로고    scopus 로고
    • Peroxynitrite activates NF-E2-related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat glutathione S-transferase A2 induction
    • K.W. Kang, S.H. Choi, and S.G. Kim Peroxynitrite activates NF-E2-related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: the role of nitric oxide synthase in rat glutathione S-transferase A2 induction Nitric Oxide 7 2002 244 253
    • (2002) Nitric Oxide , vol.7 , pp. 244-253
    • Kang, K.W.1    Choi, S.H.2    Kim, S.G.3
  • 74
    • 0038537298 scopus 로고    scopus 로고
    • PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells
    • K. Nakaso, H. Yano, Y. Fukuhara, T. Takeshima, K. Wada-Isoe, and K. Nakashima PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells Fed. Eur. Biochem. Soc. Lett. 546 2003 181 184
    • (2003) Fed. Eur. Biochem. Soc. Lett. , vol.546 , pp. 181-184
    • Nakaso, K.1    Yano, H.2    Fukuhara, Y.3    Takeshima, T.4    Wada-Isoe, K.5    Nakashima, K.6
  • 75
    • 0033789011 scopus 로고    scopus 로고
    • The essential role of phosphatidylinositol 3-kinase and of p38 mitogen-activated protein kinase activation in the antioxidant response element-mediated γgSTA2 induction by decreased glutathione in H4IIE hepatoma cells
    • K.W. Kang, J.H. Ryu, and S.G. Kim The essential role of phosphatidylinositol 3-kinase and of p38 mitogen-activated protein kinase activation in the antioxidant response element-mediated γGSTA2 induction by decreased glutathione in H4IIE hepatoma cells Mol. Pharmacol. 58 2000 1017 1025
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1017-1025
    • Kang, K.W.1    Ryu, J.H.2    Kim, S.G.3
  • 76
    • 0037357385 scopus 로고    scopus 로고
    • Activation of CCAAT/enhancer-binding protein beta by 2′-amino- 3′-methoxyflavone (PD98059) leads to the induction of glutathione S-transferase A2
    • K.W. Kang, E.Y. Park, and S.G. Kim Activation of CCAAT/enhancer-binding protein beta by 2′-amino-3′-methoxyflavone (PD98059) leads to the induction of glutathione S-transferase A2 Carcinogenesis 24 2003 475 482
    • (2003) Carcinogenesis , vol.24 , pp. 475-482
    • Kang, K.W.1    Park, E.Y.2    Kim, S.G.3
  • 77
    • 0037245333 scopus 로고    scopus 로고
    • Essential role of phosphatidylinositol 3-kinase-dependent CCAAT/enhancer binding protein beta activation in the induction of glutathione S-transferase by oltipraz
    • K.W. Kang, I.J. Cho, C.H. Lee, and S.G. Kim Essential role of phosphatidylinositol 3-kinase-dependent CCAAT/enhancer binding protein beta activation in the induction of glutathione S-transferase by oltipraz J. Natl. Cancer Inst. 95 2003 53 66
    • (2003) J. Natl. Cancer Inst. , vol.95 , pp. 53-66
    • Kang, K.W.1    Cho, I.J.2    Lee, C.H.3    Kim, S.G.4
  • 78
    • 0033600914 scopus 로고    scopus 로고
    • Role of a mitogen-activated protein kinase pathway in the induction of phase II detoxifying enzymes by chemicals
    • R. Yu, W. Lei, S. Mandlekar, M.J. Weber, C.J. Der, and J. Wu Role of a mitogen-activated protein kinase pathway in the induction of phase II detoxifying enzymes by chemicals J. Biol. Chem. 274 1999 27545 27552
    • (1999) J. Biol. Chem. , vol.274 , pp. 27545-27552
    • Yu, R.1    Lei, W.2    Mandlekar, S.3    Weber, M.J.4    Der, C.J.5    Wu, J.6
  • 79
    • 0034704079 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase pathways induces antioxidant response element-mediated gene expression via a Nrf2-dependent mechanism
    • R. Yu, C. Chen, Y.Y. Mo, V. Hebbar, E.D. Owuor, and T.H. Tan Activation of mitogen-activated protein kinase pathways induces antioxidant response element-mediated gene expression via a Nrf2-dependent mechanism J. Biol. Chem. 275 2000 39907 39913
    • (2000) J. Biol. Chem. , vol.275 , pp. 39907-39913
    • Yu, R.1    Chen, C.2    Mo, Y.Y.3    Hebbar, V.4    Owuor, E.D.5    Tan, T.H.6
  • 80
    • 0034752461 scopus 로고    scopus 로고
    • Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription
    • Y. Katoh, K. Itoh, E. Yoshida, M. Miyagishi, A. Fukamizu, and M. Yamamoto Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription Genes Cells 6 2001 857 868
    • (2001) Genes Cells , vol.6 , pp. 857-868
    • Katoh, Y.1    Itoh, K.2    Yoshida, E.3    Miyagishi, M.4    Fukamizu, A.5    Yamamoto, M.6
  • 81
    • 0035940984 scopus 로고    scopus 로고
    • Functional characterization of transcription regulators that interact with the electrophile response element
    • M. Zhu, and E. Fahl Functional characterization of transcription regulators that interact with the electrophile response element Biochem. Biophys. Res. Commun. 289 2001 212 219
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 212-219
    • Zhu, M.1    Fahl, E.2
  • 82
    • 2542418930 scopus 로고    scopus 로고
    • Regulation of Nrf2 transactivation domain activity. the differential effects of mitogen-activated protein kinase cascades and synergistic stimulatory effect of Raf and CREB-binding protein
    • G. Shen, V. Hebbar, S. Nair, C. Xu, W. Li, and W. Lin Regulation of Nrf2 transactivation domain activity. The differential effects of mitogen-activated protein kinase cascades and synergistic stimulatory effect of Raf and CREB-binding protein J. Biol. Chem. 279 2004 23052 23060
    • (2004) J. Biol. Chem. , vol.279 , pp. 23052-23060
    • Shen, G.1    Hebbar, V.2    Nair, S.3    Xu, C.4    Li, W.5    Lin, W.6
  • 86
    • 0029095529 scopus 로고
    • Oltipraz: Clinical opportunities for cancer chemoprevention
    • T.W. Kensler, and J. Helzlsouer Oltipraz: clinical opportunities for cancer chemoprevention J. Cell. Biochem. Suppl. 22 1995 101 107
    • (1995) J. Cell. Biochem. Suppl. , vol.22 , pp. 101-107
    • Kensler, T.W.1    Helzlsouer, J.2
  • 88
    • 0033577057 scopus 로고    scopus 로고
    • Protective alterations in phase 1 and 2 metabolism of aflatoxin B1 by oltipraz in residents of Qidong, People's Republic of China
    • J.S. Wang, X. Shen, X. He, Y.R. Zhu, B.C. Zhang, and J.B. Wang Protective alterations in phase 1 and 2 metabolism of aflatoxin B1 by oltipraz in residents of Qidong, People's Republic of China J. Natl. Cancer Inst. 91 1999 347 354
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 347-354
    • Wang, J.S.1    Shen, X.2    He, X.3    Zhu, Y.R.4    Zhang, B.C.5    Wang, J.B.6
  • 89
    • 0343545529 scopus 로고    scopus 로고
    • Oltipraz chemoprevention trial in Qidong, People's Republic of China: Modulation of serum aflatoxin albumin adduct biomarkers
    • T.W. Kensler, X. He, M. Otieno, P.A. Egner, L.P. Jacobson, and B. Chen Oltipraz chemoprevention trial in Qidong, People's Republic of China: modulation of serum aflatoxin albumin adduct biomarkers Cancer Epidemiol. Biomarkers Prev. 7 1998 127 134
    • (1998) Cancer Epidemiol. Biomarkers Prev. , vol.7 , pp. 127-134
    • Kensler, T.W.1    He, X.2    Otieno, M.3    Egner, P.A.4    Jacobson, L.P.5    Chen, B.6
  • 90
    • 0034927845 scopus 로고    scopus 로고
    • Oltipraz chemoprevention trial in Qidong, People's Republic of China: Results of urine genotoxicity assays as related to smoking habits
    • A. Camoirano, M. Bagnasco, C. Bennicelli, C. Cartiglia, J.B. Wang, and B.C. Zhang Oltipraz chemoprevention trial in Qidong, People's Republic of China: results of urine genotoxicity assays as related to smoking habits Cancer Epidemiol. Biomarkers Prev. 10 2001 775 783
    • (2001) Cancer Epidemiol. Biomarkers Prev. , vol.10 , pp. 775-783
    • Camoirano, A.1    Bagnasco, M.2    Bennicelli, C.3    Cartiglia, C.4    Wang, J.B.5    Zhang, B.C.6
  • 91
    • 0027290648 scopus 로고
    • Chemoprevention of colon carcinogenesis by organosulfur compounds
    • B.S. Reddy, C.V. Rao, A. Rivenson, and G. Kelloff Chemoprevention of colon carcinogenesis by organosulfur compounds Cancer Res. 53 1993 3493 3498
    • (1993) Cancer Res. , vol.53 , pp. 3493-3498
    • Reddy, B.S.1    Rao, C.V.2    Rivenson, A.3    Kelloff, G.4
  • 92
    • 0023204238 scopus 로고
    • Mechanism of protection against aflatoxin tumorigenicity in rats fed 5-(2-pyrazinyl)-4-methyl-1,2-dithiol-3-thione (oltipraz) and related 1,2-dithiol-3-thiones and 1,2-dithiol-3-ones
    • T.W. Kensler, P.A. Egner, P.M. Dolan, J.D. Groopman, and D. Roebuck Mechanism of protection against aflatoxin tumorigenicity in rats fed 5-(2-pyrazinyl)-4-methyl-1,2-dithiol-3-thione (oltipraz) and related 1,2-dithiol-3-thiones and 1,2-dithiol-3-ones Cancer Res. 47 1987 4271 4277
    • (1987) Cancer Res. , vol.47 , pp. 4271-4277
    • Kensler, T.W.1    Egner, P.A.2    Dolan, P.M.3    Groopman, J.D.4    Roebuck, D.5
  • 93
    • 0031751308 scopus 로고    scopus 로고
    • Protective effects of anethole dithiolethione against oxidative stress-induced cytotoxicity in human Jurkat T cells
    • S. Khanna, C.K. Sen, S. Roy, M.O. Christen, and L. Packer Protective effects of anethole dithiolethione against oxidative stress-induced cytotoxicity in human Jurkat T cells Biochem. Pharmacol. 56 1998 61 69
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 61-69
    • Khanna, S.1    Sen, C.K.2    Roy, S.3    Christen, M.O.4    Packer, L.5
  • 96
    • 0026577605 scopus 로고
    • A major inducer of anticarcinogenic protective enzymes from broccoli: Isolation and elucidation of structure
    • Y. Zhang, P. Talalay, C.G. Cho, and H. Posner A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure Proc. Natl. Acad. Sci. USA 89 1992 2399 2403
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2399-2403
    • Zhang, Y.1    Talalay, P.2    Cho, C.G.3    Posner, H.4
  • 97
    • 0035681887 scopus 로고    scopus 로고
    • Total intracellular accumulation levels of dietary isothiocyanates determine their activity in elevation of cellular glutathione and induction of Phase 2 detoxification enzymes
    • L. Ye, and Y. Zhang Total intracellular accumulation levels of dietary isothiocyanates determine their activity in elevation of cellular glutathione and induction of Phase 2 detoxification enzymes Carcinogenesis 22 2001 1987 1992
    • (2001) Carcinogenesis , vol.22 , pp. 1987-1992
    • Ye, L.1    Zhang, Y.2
  • 98
    • 0030931522 scopus 로고    scopus 로고
    • Broccoli sprouts: An exceptionally rich source of inducers of enzymes that protect against chemical carcinogens
    • J.W. Fahey, Y. Zhang, and P. Talalay Broccoli sprouts: an exceptionally rich source of inducers of enzymes that protect against chemical carcinogens Proc. Natl. Acad. Sci. USA 94 1997 10367 10372
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10367-10372
    • Fahey, J.W.1    Zhang, Y.2    Talalay, P.3
  • 99
    • 0035212419 scopus 로고    scopus 로고
    • Induction of xenobiotic enzymes by the MAP kinase pathway and the antioxidant or electrophile response element (ARE/EpRE)
    • A.N. Kong, E. Owuor, R. Yu, V. Hebbar, C. Chen, and R. Hu Induction of xenobiotic enzymes by the MAP kinase pathway and the antioxidant or electrophile response element (ARE/EpRE) Drug Metab. Rev. 33 2001 255 271
    • (2001) Drug Metab. Rev. , vol.33 , pp. 255-271
    • Kong, A.N.1    Owuor, E.2    Yu, R.3    Hebbar, V.4    Chen, C.5    Hu, R.6
  • 100
    • 0028203252 scopus 로고
    • Anticarcinogenic activities of sulforaphane and structurally related synthetic norbornyl isothiocyanates
    • Y. Zhang, T.W. Kensler, C.G. Cho, G.H. Posner, and P. Talalay Anticarcinogenic activities of sulforaphane and structurally related synthetic norbornyl isothiocyanates Proc. Natl. Acad. Sci. USA 91 1994 3147 3150
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3147-3150
    • Zhang, Y.1    Kensler, T.W.2    Cho, C.G.3    Posner, G.H.4    Talalay, P.5
  • 101
    • 0034525122 scopus 로고    scopus 로고
    • Chemoprevention of colonic aberrant crypt foci in Fischer rats by sulforaphane and phenethyl isothiocyanate
    • F.L. Chung, C.C. Conaway, C.V. Rao, and B.S. Reddy Chemoprevention of colonic aberrant crypt foci in Fischer rats by sulforaphane and phenethyl isothiocyanate Carcinogenesis 21 2000 2287 2291
    • (2000) Carcinogenesis , vol.21 , pp. 2287-2291
    • Chung, F.L.1    Conaway, C.C.2    Rao, C.V.3    Reddy, B.S.4
  • 103
    • 0036357406 scopus 로고    scopus 로고
    • Inhibition of mouse skin tumor promotion by anti-inflammatory diarylheptanoids derived from Alpinia oxyphylla Miquel (Zingiberaceae)
    • K.-S. Chun, K.K. Park, J. Lee, M. Kang, and Y.-J. Surh Inhibition of mouse skin tumor promotion by anti-inflammatory diarylheptanoids derived from Alpinia oxyphylla Miquel (Zingiberaceae) Oncol. Res. 13 2002 37 45
    • (2002) Oncol. Res. , vol.13 , pp. 37-45
    • Chun, K.-S.1    Park, K.K.2    Lee, J.3    Kang, M.4    Surh, Y.-J.5
  • 104
    • 0141814600 scopus 로고    scopus 로고
    • Curcumin inhibits phorbol ester-induced expression of cyclooxygenase-2 in mouse skin through suppression of extracellular signal-regulated kinase activity and NF-κB activation
    • K.-S. Chun, Y.-S. Keum, S.S. Han, Y.S. Song, S.H. Kim, and Y.-J. Surh Curcumin inhibits phorbol ester-induced expression of cyclooxygenase-2 in mouse skin through suppression of extracellular signal-regulated kinase activity and NF-κB activation Carcinogenesis 24 2003 1515 1524
    • (2003) Carcinogenesis , vol.24 , pp. 1515-1524
    • Chun, K.-S.1    Keum, Y.-S.2    Han, S.S.3    Song, Y.S.4    Kim, S.H.5    Surh, Y.-J.6
  • 105
    • 0026553336 scopus 로고
    • Chemopreventive effect of turmeric against stomach and skin tumors induced by chemical carcinogens in Swiss mice
    • M.A. Azuine, and V. Bhide Chemopreventive effect of turmeric against stomach and skin tumors induced by chemical carcinogens in Swiss mice Nutr. Cancer 17 1992 77 83
    • (1992) Nutr. Cancer , vol.17 , pp. 77-83
    • Azuine, M.A.1    Bhide, V.2
  • 106
    • 0028073507 scopus 로고
    • Inhibitory effects of dietary curcumin on forestomach, duodenal, and colon carcinogenesis in mice
    • M.T. Huang, Y.R. Lou, W. Ma, H.L. Newmark, K.R. Reuhl, and A.H. Conney Inhibitory effects of dietary curcumin on forestomach, duodenal, and colon carcinogenesis in mice Cancer Res. 54 1994 5841 5847
    • (1994) Cancer Res. , vol.54 , pp. 5841-5847
    • Huang, M.T.1    Lou, Y.R.2    Ma, W.3    Newmark, H.L.4    Reuhl, K.R.5    Conney, A.H.6
  • 107
    • 0027333082 scopus 로고
    • Inhibition by dietary curcumin of azoxymethane-induced ornithine decarboxylase, tyrosine protein kinase, arachidonic acid metabolism and aberrant crypt foci formation in the rat colon
    • C.V. Rao, B. Simi, and B.S. Reddy Inhibition by dietary curcumin of azoxymethane-induced ornithine decarboxylase, tyrosine protein kinase, arachidonic acid metabolism and aberrant crypt foci formation in the rat colon Carcinogenesis 14 1993 2219 2225
    • (1993) Carcinogenesis , vol.14 , pp. 2219-2225
    • Rao, C.V.1    Simi, B.2    Reddy, B.S.3
  • 108
    • 0033562995 scopus 로고    scopus 로고
    • Inhibitory effects of caffeic acid phenethyl ester on the activity and expression of cyclooxygenase-2 in human oral epithelial cells and in a rat model of inflammation
    • P. Michaluart, J.L. Masferrer, A.M. Carothers, K. Subbaramaiah, B.S. Zweifel, and C. Koboldt Inhibitory effects of caffeic acid phenethyl ester on the activity and expression of cyclooxygenase-2 in human oral epithelial cells and in a rat model of inflammation Cancer Res. 59 1999 2347 2352
    • (1999) Cancer Res. , vol.59 , pp. 2347-2352
    • Michaluart, P.1    Masferrer, J.L.2    Carothers, A.M.3    Subbaramaiah, K.4    Zweifel, B.S.5    Koboldt, C.6
  • 109
    • 0027880285 scopus 로고
    • Inhibitory effect of caffeic acid esters on azoxymethane-induced biochemical changes and aberrant crypt foci formation in rat colon
    • C.V. Rao, D. Desai, B. Simi, N. Kulkarni, S. Amin, and B.S. Reddy Inhibitory effect of caffeic acid esters on azoxymethane-induced biochemical changes and aberrant crypt foci formation in rat colon Cancer Res. 53 1993 4182 4188
    • (1993) Cancer Res. , vol.53 , pp. 4182-4188
    • Rao, C.V.1    Desai, D.2    Simi, B.3    Kulkarni, N.4    Amin, S.5    Reddy, B.S.6
  • 110
    • 0029874984 scopus 로고    scopus 로고
    • Inhibitory effects of caffeic acid phenethyl ester (CAPE) on 12-O-tetradecanoylphorbol-13-acetate-induced tumor promotion in mouse skin and the synthesis of DNA, RNA and protein in HeLa cells
    • M.T. Huang, W. Ma, P. Yen, J.G. Xie, J. Han, and K. Frenkel Inhibitory effects of caffeic acid phenethyl ester (CAPE) on 12-O-tetradecanoylphorbol-13- acetate-induced tumor promotion in mouse skin and the synthesis of DNA, RNA and protein in HeLa cells Carcinogenesis 17 1996 761 765
    • (1996) Carcinogenesis , vol.17 , pp. 761-765
    • Huang, M.T.1    Ma, W.2    Yen, P.3    Xie, J.G.4    Han, J.5    Frenkel, K.6
  • 111
    • 0037366092 scopus 로고    scopus 로고
    • Curcumin alters EpRE and AP-1 binding complexes and elevates glutamate-cysteine ligase gene expression
    • D.A. Dickinson, K.E. Iles, H. Zhang, V. Blank, and J. Forman Curcumin alters EpRE and AP-1 binding complexes and elevates glutamate-cysteine ligase gene expression FASEBJ. 17 2003 473 475
    • (2003) FASEBJ. , vol.17 , pp. 473-475
    • Dickinson, D.A.1    Iles, K.E.2    Zhang, H.3    Blank, V.4    Forman, J.5
  • 112
    • 0033083919 scopus 로고    scopus 로고
    • Cancer chemopreventive activity mediated by 4′-bromoflavone, a potent inducer of phase II detoxification enzymes
    • L.L. Song, J.W. Kosmeder II, S.K. Lee, C. Gerhauser, D. Lantvit, and R.C. Moon Cancer chemopreventive activity mediated by 4′-bromoflavone, a potent inducer of phase II detoxification enzymes Cancer Res. 59 1999 578 585
    • (1999) Cancer Res. , vol.59 , pp. 578-585
    • Song, L.L.1    Kosmeder II, J.W.2    Lee, S.K.3    Gerhauser, C.4    Lantvit, D.5    Moon, R.C.6
  • 113
    • 0037462675 scopus 로고    scopus 로고
    • Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones
    • E.C. Pietsch, J.Y. Chan, F.M. Torti, and V. Torti Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones J. Biol. Chem. 278 2003 2361 2369
    • (2003) J. Biol. Chem. , vol.278 , pp. 2361-2369
    • Pietsch, E.C.1    Chan, J.Y.2    Torti, F.M.3    Torti, V.4
  • 114
    • 0036240610 scopus 로고    scopus 로고
    • Enhanced expression of the transcription factor Nrf2 by cancer chemopreventive agents: Role of antioxidant response element-like sequences in the nrf2 promoter
    • M.K. Kwak, K. Itoh, M. Yamamoto, and T.W. Kensler Enhanced expression of the transcription factor Nrf2 by cancer chemopreventive agents: role of antioxidant response element-like sequences in the nrf2 promoter Mol. Cell Biol. 22 2002 2883 2892
    • (2002) Mol. Cell Biol. , vol.22 , pp. 2883-2892
    • Kwak, M.K.1    Itoh, K.2    Yamamoto, M.3    Kensler, T.W.4
  • 115
    • 0842304134 scopus 로고    scopus 로고
    • Nuclear factor E2-related factor 2-dependent antioxidant response element activation by tert-butylhydroquinone and sulforaphane occurring preferentially in astrocytes conditions neurons against oxidative insult
    • A.D. Kraft, D.A. Johnson, and J.A. Johnson Nuclear factor E2-related factor 2-dependent antioxidant response element activation by tert-butylhydroquinone and sulforaphane occurring preferentially in astrocytes conditions neurons against oxidative insult J. Neurosci. 24 2004 1101 1112
    • (2004) J. Neurosci. , vol.24 , pp. 1101-1112
    • Kraft, A.D.1    Johnson, D.A.2    Johnson, J.A.3
  • 116
    • 2442658079 scopus 로고    scopus 로고
    • Transactivation of the PPAR-responsive enhancer module in chemopreventive glutathione S-transferase gene by the peroxisome proliferator-activated receptor-gamma and retinoid X receptor heterodimer
    • E.Y. Park, I.J. Cho, and S.G. Kim Transactivation of the PPAR-responsive enhancer module in chemopreventive glutathione S-transferase gene by the peroxisome proliferator-activated receptor-gamma and retinoid X receptor heterodimer Cancer Res. 64 2004 3701 3713
    • (2004) Cancer Res. , vol.64 , pp. 3701-3713
    • Park, E.Y.1    Cho, I.J.2    Kim, S.G.3
  • 117
    • 4143081630 scopus 로고    scopus 로고
    • Zerumbone, a tropical ginger sesquiterpene, activates phase II drug metabolizing enzymes
    • Y. Nakamura, C. Yoshida, A. Murakami, H. Ohigashi, T. Osawa, and K. Uchida Zerumbone, a tropical ginger sesquiterpene, activates phase II drug metabolizing enzymes FEBS Lett. 572 2004 245 250
    • (2004) FEBS Lett. , vol.572 , pp. 245-250
    • Nakamura, Y.1    Yoshida, C.2    Murakami, A.3    Ohigashi, H.4    Osawa, T.5    Uchida, K.6
  • 118
    • 0034573074 scopus 로고    scopus 로고
    • Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death
    • C. Chen, R. Yu, E.D. Owuor, and A.N. Kong Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death Arch. Pharm. Res. 23 2000 605 612
    • (2000) Arch. Pharm. Res. , vol.23 , pp. 605-612
    • Chen, C.1    Yu, R.2    Owuor, E.D.3    Kong, A.N.4


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