메뉴 건너뛰기




Volumn 15, Issue 10, 2010, Pages 7266-7291

The Nrf2 system as a potential target for the development of indirect antioxidants

Author keywords

Indirect antioxidants; Keap1; Nrf2; Oxidative stress

Indexed keywords

ANTIOXIDANT; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR NRF2;

EID: 78149434112     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules15107266     Document Type: Review
Times cited : (389)

References (165)
  • 1
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 1995, 64, 97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 2
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P.; Beckman, J.S.; Liaudet, L. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 2007, 87, 315-424.
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 4
    • 72649102374 scopus 로고    scopus 로고
    • Protection against reactive oxygen species by selenoproteins
    • Steinbrenner, H.; Sies, H. Protection against reactive oxygen species by selenoproteins. Biochim. Biophys. Acta 2009, 1790, 1478-1485.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1478-1485
    • Steinbrenner, H.1    Sies, H.2
  • 6
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski, T.P.; Nathan, C.F. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 1991, 51, 794-798.
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 7
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita, I.; Rossmann, M.G. The active center of catalase. J. Mol. Biol. 1985, 185, 21-37.
    • (1985) J. Mol. Biol. , vol.185 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 8
    • 0034730942 scopus 로고    scopus 로고
    • Anti-proliferative effect of resveratrol, a natural component of grapes and wine, on human colonic cancer cells
    • Schneider, Y.; Vincent, F.; Duranton, B.; Badolo, L.; Gosse, F.; Bergmann, C.; Seiler, N.; Raul, F. Anti-proliferative effect of resveratrol, a natural component of grapes and wine, on human colonic cancer cells. Cancer Lett. 2000, 158, 85-91.
    • (2000) Cancer Lett. , vol.158 , pp. 85-91
    • Schneider, Y.1    Vincent, F.2    Duranton, B.3    Badolo, L.4    Gosse, F.5    Bergmann, C.6    Seiler, N.7    Raul, F.8
  • 9
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohe, R. Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 1999, 27, 951-965.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 13
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase
    • Huang, C.S.; Chang, L.S.; Anderson, M.E.; Meister, A. Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase. J. Biol. Chem. 1993, 268, 19675-19680.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19675-19680
    • Huang, C.S.1    Chang, L.S.2    Anderson, M.E.3    Meister, A.4
  • 15
    • 0042352219 scopus 로고    scopus 로고
    • Induction of drug-metabolizing enzymes: A path to the discovery of multiple cytochromes P450
    • Conney, A.H. Induction of drug-metabolizing enzymes: a path to the discovery of multiple cytochromes P450. Annu. Rev. Pharmacol. Toxicol. 2003, 43, 1-30.
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 1-30
    • Conney, A.H.1
  • 16
    • 52449089630 scopus 로고    scopus 로고
    • Direct and indirect antioxidant properties of inducers of cytoprotective proteins
    • Dinkova-Kostova, A.T.; Talalay, P. Direct and indirect antioxidant properties of inducers of cytoprotective proteins. Mol. Nutr. Food Res. 2008, 52 (Suppl. 1), S128-S138.
    • (2008) Mol. Nutr. Food Res. , vol.52 , Issue.SUPPL. 1
    • Dinkova-Kostova, A.T.1    Talalay, P.2
  • 18
    • 0021324828 scopus 로고
    • Metabolic activation of benzoa.pyrene-7,8-dihydrodiol and benzoa.pyrene-7,8-dihydrodiol-9,10-epoxide to protein-binding products and the inhibitory effect of glutathione and cysteine
    • Jernstrom, B.; Dock, L.; Martinez, M. Metabolic activation of benzoa.pyrene-7,8-dihydrodiol and benzoa.pyrene-7,8-dihydrodiol-9,10-epoxide to protein-binding products and the inhibitory effect of glutathione and cysteine. Carcinogenesis 1984, 5, 199-204.
    • (1984) Carcinogenesis , vol.5 , pp. 199-204
    • Jernstrom, B.1    Dock, L.2    Martinez, M.3
  • 21
    • 35148858830 scopus 로고    scopus 로고
    • Glutathione transferase pi plays a critical role in the development of lung carcinogenesis following exposure to tobacco-related carcinogens and urethane
    • Ritchie, K.J.; Henderson, C.J.; Wang, X.J.; Vassieva, O.; Carrie, D.; Farmer, P.B.; Gaskell, M.; Park, K.; Wolf, C.R. Glutathione transferase pi plays a critical role in the development of lung carcinogenesis following exposure to tobacco-related carcinogens and urethane. Cancer Res.. 2007, 67, 9248-9257.
    • (2007) Cancer Res. , vol.67 , pp. 9248-9257
    • Ritchie, K.J.1    Henderson, C.J.2    Wang, X.J.3    Vassieva, O.4    Carrie, D.5    Farmer, P.B.6    Gaskell, M.7    Park, K.8    Wolf, C.R.9
  • 23
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression, and disease
    • Tukey, R.H.; Strassburg, C.P. Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu. Rev. Pharmacol. Toxicol. 2000, 40, 581-616.
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 24
    • 0028956177 scopus 로고
    • Potential genoprotective role for UDP-glucuronosyltransferases in chemical carcinogenesis: Initiation of micronuclei by benzo(a)pyrene and benzo(e)pyrene in UDP-glucuronosyltransferase-deficient cultured rat skin fibroblasts
    • Vienneau, D.S.; DeBoni, U.; Wells, P.G. Potential genoprotective role for UDP-glucuronosyltransferases in chemical carcinogenesis: initiation of micronuclei by benzo(a)pyrene and benzo(e)pyrene in UDP-glucuronosyltransferase- deficient cultured rat skin fibroblasts. Cancer Res. 1995, 55, 1045-1051.
    • (1995) Cancer Res. , vol.55 , pp. 1045-1051
    • Vienneau, D.S.1    DeBoni, U.2    Wells, P.G.3
  • 25
    • 36048977522 scopus 로고    scopus 로고
    • Differential effect of over-expressing UGT1A1 and CYP1A1 on xenobiotic assault in MCF-7 cells
    • Leung, H.Y.; Wang, Y.; Leung, L.K. Differential effect of over-expressing UGT1A1 and CYP1A1 on xenobiotic assault in MCF-7 cells. Toxicology 2007, 242, 153-159.
    • (2007) Toxicology , vol.242 , pp. 153-159
    • Leung, H.Y.1    Wang, Y.2    Leung, L.K.3
  • 26
    • 5444240961 scopus 로고    scopus 로고
    • Contribution of NAD(P)H: Quinone oxidoreductase 1 to protection against carcinogenesis, and regulation of its gene by the Nrf2 basic-region leucine zipper and the arylhydrocarbon receptor basic helix-loop-helix transcription factors
    • Nioi, P.; Hayes, J.D. Contribution of NAD(P)H:quinone oxidoreductase 1 to protection against carcinogenesis, and regulation of its gene by the Nrf2 basic-region leucine zipper and the arylhydrocarbon receptor basic helix-loop-helix transcription factors. Mutat. Res. 2004, 555, 149-171.
    • (2004) Mutat. Res. , vol.555 , pp. 149-171
    • Nioi, P.1    Hayes, J.D.2
  • 28
    • 0029859863 scopus 로고    scopus 로고
    • DT-Diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function
    • Landi, L.; Fiorentini, D.; Galli, M.C.; Segura-Aguilar, J.; Beyer, R.E. DT-Diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function. Free Radic. Biol. Med. 1997, 22, 329-335.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 329-335
    • Landi, L.1    Fiorentini, D.2    Galli, M.C.3    Segura-Aguilar, J.4    Beyer, R.E.5
  • 29
    • 0030739681 scopus 로고    scopus 로고
    • The reduction of alphatocopherolquinone by human NAD(P)H: Quinone oxidoreductase: The role of alpha-tocopherolhydroquinone as a cellular antioxidant
    • Siegel, D.; Bolton, E.M.; Burr, J.A.; Liebler, D.C.; Ross, D. The reduction of alpha-tocopherolquinone by human NAD(P)H: quinone oxidoreductase: the role of alphatocopherolhydroquinone as a cellular antioxidant. Mol. Pharmacol. 1997, 52, 300-305.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 300-305
    • Siegel, D.1    Bolton, E.M.2    Burr, J.A.3    Liebler, D.C.4    Ross, D.5
  • 30
    • 0034326245 scopus 로고    scopus 로고
    • NAD(P)H: Quinone oxidoreductase 1 deficiency increases susceptibility to benzo(a)pyrene-induced mouse skin carcinogenesis
    • Long, D.J., 2nd; Waikel, R.L.; Wang, X.J.; Perlaky, L.; Roop, D.R.; Jaiswal, A.K. NAD(P)H:quinone oxidoreductase 1 deficiency increases susceptibility to benzo(a)pyrene-induced mouse skin carcinogenesis. Cancer Res. 2000, 60, 5913-5915.
    • (2000) Cancer Res. , vol.60 , pp. 5913-5915
    • Long II, D.J.1    Waikel, R.L.2    Wang, X.J.3    Perlaky, L.4    Roop, D.R.5    Jaiswal, A.K.6
  • 32
    • 0033566767 scopus 로고    scopus 로고
    • A lack of a functional NAD(P)H: Quinone oxidoreductase allele is selectively associated with pediatric leukemias that have MLL fusions. United Kingdom childhood cancer study investigators
    • Wiemels, J.L.; Pagnamenta, A.; Taylor, G.M.; Eden, O.B.; Alexander, F.E.; Greaves, M.F. A lack of a functional NAD(P)H:quinone oxidoreductase allele is selectively associated with pediatric leukemias that have MLL fusions. United Kingdom Childhood Cancer Study Investigators. Cancer Res. 1999, 59, 4095-4099.
    • (1999) Cancer Res. , vol.59 , pp. 4095-4099
    • Wiemels, J.L.1    Pagnamenta, A.2    Taylor, G.M.3    Eden, O.B.4    Alexander, F.E.5    Greaves, M.F.6
  • 33
    • 0033782995 scopus 로고    scopus 로고
    • NAD(P)H: Quinone oxidoreductase-dependent risk for colorectal cancer and its association with the presence of K-ras mutations in tumors
    • Lafuente, M.J.; Casterad, X.; Trias, M.; Ascaso, C.; Molina, R.; Ballesta, A.; Zheng, S.; Wiencke, J.K.; Lafuente, A. NAD(P)H:quinone oxidoreductase-dependent risk for colorectal cancer and its association with the presence of K-ras mutations in tumors. Carcinogenesis 2000, 21, 1813-1819.
    • (2000) Carcinogenesis , vol.21 , pp. 1813-1819
    • Lafuente, M.J.1    Casterad, X.2    Trias, M.3    Ascaso, C.4    Molina, R.5    Ballesta, A.6    Zheng, S.7    Wiencke, J.K.8    Lafuente, A.9
  • 36
    • 0029411321 scopus 로고
    • Parallel induction of heme oxygenase-1 and chemoprotective phase 2 enzymes by electrophiles and antioxidants: Regulation by upstream antioxidant-responsive elements (ARE)
    • Prestera, T.; Talalay, P.; Alam, J.; Ahn, Y.I.; Lee, P.J.; Choi, A.M. Parallel induction of heme oxygenase-1 and chemoprotective phase 2 enzymes by electrophiles and antioxidants: regulation by upstream antioxidant-responsive elements (ARE). Mol. Med. 1995, 1, 827-837.
    • (1995) Mol. Med. , vol.1 , pp. 827-837
    • Prestera, T.1    Talalay, P.2    Alam, J.3    Ahn, Y.I.4    Lee, P.J.5    Choi, A.M.6
  • 37
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M.; Arosio, P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1996, 1275, 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 38
    • 0033853838 scopus 로고    scopus 로고
    • Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress
    • Tsuji, Y.; Ayaki, H.; Whitman, S.P.; Morrow, C.S.; Torti, S.V.; Torti, F.M. Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress. Mol. Cell Biol. 2000, 20, 5818-5827.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5818-5827
    • Tsuji, Y.1    Ayaki, H.2    Whitman, S.P.3    Morrow, C.S.4    Torti, S.V.5    Torti, F.M.6
  • 39
    • 0024997241 scopus 로고
    • Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants
    • Rushmore, T.H.; Pickett, C.B. Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. J. Biol. Chem. 1990, 265, 14648-14653.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14648-14653
    • Rushmore, T.H.1    Pickett, C.B.2
  • 40
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore, T.H.; Morton, M.R.; Pickett, C.B. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J. Biol. Chem. 1991, 266, 11632-11639.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 41
    • 0025806510 scopus 로고
    • Transcriptional regulation of the rat NAD(P)H: Quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants
    • Favreau, L.V.; Pickett, C.B. Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants. J. Biol. Chem. 1991, 266, 4556-4561.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4556-4561
    • Favreau, L.V.1    Pickett, C.B.2
  • 42
    • 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
    • Nioi, P.; McMahon, M.; Itoh, K.; Yamamoto, M.; Hayes, J.D. 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. 2003, 374, 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
  • 43
    • 0026319263 scopus 로고
    • Human NAD(P)H: Quinone oxidoreductase (NQO1) gene structure and induction by dioxin
    • Jaiswal, A.K. Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin. Biochemistry 1991, 30, 10647-10653.
    • (1991) Biochemistry , vol.30 , pp. 10647-10653
    • Jaiswal, A.K.1
  • 44
    • 0037163092 scopus 로고    scopus 로고
    • Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene. Revision of the ARE consensus sequence
    • Erickson, A.M.; Nevarea, Z.; Gipp, J.J.; Mulcahy, R.T. Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene. Revision of the ARE consensus sequence. J. Biol. Chem. 2002, 277, 30730-30737.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30730-30737
    • Erickson, A.M.1    Nevarea, Z.2    Gipp, J.J.3    Mulcahy, R.T.4
  • 45
    • 0028914295 scopus 로고
    • Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene
    • Mulcahy, R.T.; Gipp, J.J. Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem. Biophys. Res. Commun. 1995, 209, 227-233.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 227-233
    • Mulcahy, R.T.1    Gipp, J.J.2
  • 46
    • 0030956247 scopus 로고    scopus 로고
    • Constitutive and beta-naphthoflavone-induced expression of the human gamma-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/TRE sequence
    • Mulcahy, R.T.; Wartman, M.A.; Bailey, H.H.; Gipp, J.J. Constitutive and beta-naphthoflavone-induced expression of the human gamma-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/TRE sequence. J. Biol. Chem. 1997, 272, 7445-7454.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7445-7454
    • Mulcahy, R.T.1    Wartman, M.A.2    Bailey, H.H.3    Gipp, J.J.4
  • 47
  • 49
    • 14044254798 scopus 로고    scopus 로고
    • Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation
    • Kobayashi, M.; Yamamoto, M. Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation. Antioxid. Redox Signal 2005, 7, 385-394.
    • (2005) Antioxid. Redox Signal , vol.7 , pp. 385-394
    • Kobayashi, M.1    Yamamoto, M.2
  • 51
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H: Quinone oxidoreductase1 gene
    • Venugopal, R.; Jaiswal, A.K. Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene. Proc. Natl. Acad. Sci. USA 1996, 93, 14960-14965.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 52
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
    • Ramos-Gomez, M.; Kwak, M.K.; Dolan, P.M.; Itoh, K.; Yamamoto, M.; Talalay, P.; Kensler, T.W. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc. Natl. Acad. Sci. USA 2001, 98, 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    Kensler, T.W.7
  • 53
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam, J.; Stewart, D.; Touchard, C.; Boinapally, S.; Choi, A.M.; Cook, J.L. Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J. Biol. Chem. 1999, 274, 26071-26078.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 54
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation
    • He, C.H.; Gong, P.; Hu, B.; Stewart, D.; Choi, M.E.; Choi, A.M.; Alam, J. Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation. J. Biol. Chem. 2001, 276, 20858-20865.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 55
    • 0028118492 scopus 로고
    • Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins
    • Igarashi, K.; Kataoka, K.; Itoh, K.; Hayashi, N.; Nishizawa, M.; Yamamoto, M. Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins. Nature 1994, 367, 568-572.
    • (1994) Nature , vol.367 , pp. 568-572
    • Igarashi, K.1    Kataoka, K.2    Itoh, K.3    Hayashi, N.4    Nishizawa, M.5    Yamamoto, M.6
  • 56
    • 24344479164 scopus 로고    scopus 로고
    • Genetic evidence that small maf proteins are essential for the activation of antioxidant response element-dependent genes
    • Katsuoka, F.; Motohashi, H.; Ishii, T.; Aburatani, H.; Engel, J.D.; Yamamoto, M. Genetic evidence that small maf proteins are essential for the activation of antioxidant response element-dependent genes. Mol. Cell Biol. 2005, 25, 8044-8051.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 8044-8051
    • Katsuoka, F.1    Motohashi, H.2    Ishii, T.3    Aburatani, H.4    Engel, J.D.5    Yamamoto, M.6
  • 57
    • 0037055265 scopus 로고    scopus 로고
    • Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors
    • Motohashi, H.; O'Connor, T.; Katsuoka, F.; Engel, J.D.; Yamamoto, M. Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors. Gene 2002, 294, 1-12.
    • (2002) Gene , vol.294 , pp. 1-12
    • Motohashi, H.1    O'Connor, T.2    Katsuoka, F.3    Engel, J.D.4    Yamamoto, M.5
  • 58
    • 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
    • Kwak, M.K.; Wakabayashi, N.; Itoh, K.; Motohashi, H.; Yamamoto, M.; Kensler, T.W. Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival. J. Biol. Chem. 2003, 278, 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
  • 59
    • 33746889956 scopus 로고    scopus 로고
    • Gene expression profiles induced by cancer chemopreventive isothiocyanate sulforaphane in the liver of C57BL/6J mice and C57BL/6J/Nrf2 (-/-) mice
    • Hu, R.; Xu, C.; Shen, G.; Jain, M.R.; Khor, T.O.; Gopalkrishnan, A.; Lin, W.; Reddy, B.; Chan, J.Y.; Kong, A.N. Gene expression profiles induced by cancer chemopreventive isothiocyanate sulforaphane in the liver of C57BL/6J mice and C57BL/6J/Nrf2 (-/-) mice. Cancer Lett. 2006, 243, 170-192.
    • (2006) Cancer Lett. , vol.243 , pp. 170-192
    • Hu, R.1    Xu, C.2    Shen, G.3    Jain, M.R.4    Khor, T.O.5    Gopalkrishnan, A.6    Lin, W.7    Reddy, B.8    Chan, J.Y.9    Kong, A.N.10
  • 60
    • 33749263503 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by chemopreventive isothiocyanate PEITC by oligonucleotide microarray
    • Hu, R.; Xu, C.; Shen, G.; Jain, M.R.; Khor, T.O.; Gopalkrishnan, A.; Lin, W.; Reddy, B.; Chan, J.Y.; Kong, A.N. Identification of Nrf2-regulated genes induced by chemopreventive isothiocyanate PEITC by oligonucleotide microarray. Life Sci. 2006, 79, 1944-1955.
    • (2006) Life Sci. , vol.79 , pp. 1944-1955
    • Hu, R.1    Xu, C.2    Shen, G.3    Jain, M.R.4    Khor, T.O.5    Gopalkrishnan, A.6    Lin, W.7    Reddy, B.8    Chan, J.Y.9    Kong, A.N.10
  • 61
    • 77649270763 scopus 로고    scopus 로고
    • Targeting NRF2 signaling for cancer chemoprevention
    • Kwak, M.K.; Kensler, T.W. Targeting NRF2 signaling for cancer chemoprevention. Toxicol. Appl. Pharmacol. 2010, 244, 66-76.
    • (2010) Toxicol. Appl. Pharmacol. , vol.244 , pp. 66-76
    • Kwak, M.K.1    Kensler, T.W.2
  • 62
    • 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, J.M.; Calkins, M.J.; Chan, K.; Kan, Y.W.; Johnson, J.A. 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. 2003, 278, 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
  • 63
    • 33750605111 scopus 로고    scopus 로고
    • Pharmacogenomics of phenolic antioxidant butylated hydroxyanisole (BHA) in the small intestine and liver of Nrf2 knockout and C57BL/6J mice
    • Nair, S.; Xu, C.; Shen, G.; Hebbar, V.; Gopalakrishnan, A.; Hu, R.; Jain, M.R.; Lin, W.; Keum, Y.S.; Liew, C.; Chan, J.Y.; Kong, A.N. Pharmacogenomics of phenolic antioxidant butylated hydroxyanisole (BHA) in the small intestine and liver of Nrf2 knockout and C57BL/6J mice. Pharm. Res. 2006, 23, 2621-2637.
    • (2006) Pharm. Res. , vol.23 , pp. 2621-2637
    • Nair, S.1    Xu, C.2    Shen, G.3    Hebbar, V.4    Gopalakrishnan, A.5    Hu, R.6    Jain, M.R.7    Lin, W.8    Keum, Y.S.9    Liew, C.10    Chan, J.Y.11    Kong, A.N.12
  • 64
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • Thimmulappa, R.K.; Mai, K.H.; Srisuma, S.; Kensler, T.W.; Yamamoto, M.; Biswal, S. Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray. Cancer Res. 2002, 62, 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
  • 68
    • 70249138697 scopus 로고    scopus 로고
    • Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: Demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds
    • MacLeod, A.K.; McMahon, M.; Plummer, S.M.; Higgins, L.G.; Penning, T.M.; Igarashi, K.; Hayes, J.D. Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds. Carcinogenesis 2009, 30, 1571-1580.
    • (2009) Carcinogenesis , vol.30 , pp. 1571-1580
    • MacLeod, A.K.1    McMahon, M.2    Plummer, S.M.3    Higgins, L.G.4    Penning, T.M.5    Igarashi, K.6    Hayes, J.D.7
  • 69
    • 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
    • Li, J.; Lee, J.M.; Johnson, J.A. 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. 2002, 277, 388-394.
    • (2002) J. Biol. Chem. , vol.277 , pp. 388-394
    • Li, J.1    Lee, J.M.2    Johnson, J.A.3
  • 71
    • 61349117533 scopus 로고    scopus 로고
    • Increased Nrf2 activation in livers from Keap1-knockdown mice increases expression of cytoprotective genes that detoxify electrophiles more than those that detoxify reactive oxygen species
    • Reisman, S.A.; Yeager, R.L.; Yamamoto, M.; Klaassen, C.D. Increased Nrf2 activation in livers from Keap1-knockdown mice increases expression of cytoprotective genes that detoxify electrophiles more than those that detoxify reactive oxygen species. Toxicol. Sci. 2009, 108, 35-47.
    • (2009) Toxicol. Sci. , vol.108 , pp. 35-47
    • Reisman, S.A.1    Yeager, R.L.2    Yamamoto, M.3    Klaassen, C.D.4
  • 74
    • 28144445947 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity
    • Okawa, H.; Motohashi, H.; Kobayashi, A.; Aburatani, H.; Kensler, T.W.; Yamamoto, M. Hepatocyte-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity. Biochem. Biophys. Res. Commun. 2006, 339, 79-88.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 79-88
    • Okawa, H.1    Motohashi, H.2    Kobayashi, A.3    Aburatani, H.4    Kensler, T.W.5    Yamamoto, M.6
  • 77
    • 58049088157 scopus 로고    scopus 로고
    • Oxidant stress stimulates expression of the human peroxiredoxin 6 gene by a transcriptional mechanism involving an antioxidant response element
    • Chowdhury, I.; Mo, Y.; Gao, L.; Kazi, A.; Fisher, A.B.; Feinstein, S.I. Oxidant stress stimulates expression of the human peroxiredoxin 6 gene by a transcriptional mechanism involving an antioxidant response element. Free Radic. Biol. Med. 2009, 46, 146-153.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 146-153
    • Chowdhury, I.1    Mo, Y.2    Gao, L.3    Kazi, A.4    Fisher, A.B.5    Feinstein, S.I.6
  • 78
    • 27944494853 scopus 로고    scopus 로고
    • Effect of sulforaphane on metallothionein expression and induction of apoptosis in human hepatoma HepG2 cells
    • Yeh, C.T.; Yen, G.C. Effect of sulforaphane on metallothionein expression and induction of apoptosis in human hepatoma HepG2 cells. Carcinogenesis 2005, 26, 2138-2148.
    • (2005) Carcinogenesis , vol.26 , pp. 2138-2148
    • Yeh, C.T.1    Yen, G.C.2
  • 79
    • 67349089075 scopus 로고    scopus 로고
    • Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma
    • Mahaffey, C.M.; Zhang, H.; Rinna, A.; Holland, W.; Mack, P.C.; Forman, H.J. Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma. Free Radic. Biol. Med. 2009, 46, 1650-1657.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1650-1657
    • Mahaffey, C.M.1    Zhang, H.2    Rinna, A.3    Holland, W.4    Mack, P.C.5    Forman, H.J.6
  • 80
    • 0029043995 scopus 로고
    • Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins
    • Itoh, K.; Igarashi, K.; Hayashi, N.; Nishizawa, M.; Yamamoto, M. Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins. Mol. Cell Biol. 1995, 15, 4184-4193.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4184-4193
    • Itoh, K.1    Igarashi, K.2    Hayashi, N.3    Nishizawa, M.4    Yamamoto, M.5
  • 81
    • 0034752461 scopus 로고    scopus 로고
    • Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription
    • Katoh, Y.; Itoh, K.; Yoshida, E.; Miyagishi, M.; Fukamizu, A.; Yamamoto, M. Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription. Genes Cells 2001, 6, 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
  • 82
    • 28544450507 scopus 로고    scopus 로고
    • The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation
    • Nioi, P.; Nguyen, T.; Sherratt, P.J.; Pickett, C.B. The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation. Mol. Cell Biol. 2005, 25, 10895-10906.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 10895-10906
    • Nioi, P.1    Nguyen, T.2    Sherratt, P.J.3    Pickett, C.B.4
  • 83
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K.; Wakabayashi, N.; Katoh, Y.; Ishii, T.; Igarashi, K.; Engel, J.D.; Yamamoto, M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 1999, 13, 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    Yamamoto, M.7
  • 84
    • 0027403024 scopus 로고
    • Kelch encodes a component of intercellular bridges in Drosophila egg chambers
    • Xue, F.; Cooley, L. kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 1993, 72, 681-693.
    • (1993) Cell , vol.72 , pp. 681-693
    • Xue, F.1    Cooley, L.2
  • 85
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi, A.; Kang, M.I.; Okawa, H.; Ohtsuji, M.; Zenke, Y.; Chiba, T.; Igarashi, K.; Yamamoto, M. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell Biol. 2004, 24, 7130-7139.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 86
    • 33747728194 scopus 로고    scopus 로고
    • Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: A two-site interaction model for the Nrf2-Keap1 complex
    • McMahon, M.; Thomas, N.; Itoh, K.; Yamamoto, M.; Hayes, J.D. Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: a two-site interaction model for the Nrf2-Keap1 complex. J. Biol. Chem. 2006, 281, 24756-24768.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24756-24768
    • McMahon, M.1    Thomas, N.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 87
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang, D.D.; Lo, S.C.; Cross, J.V.; Templeton, D.J.; Hannink, M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol. Cell Biol. 2004, 24, 10941-10953.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 88
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
    • Tong, K.I.; Kobayashi, A.; Katsuoka, F.; Yamamoto, M. Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism. Biol Chem 2006, 387, 1311-1320.
    • (2006) Biol Chem , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 89
    • 35648970026 scopus 로고    scopus 로고
    • Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response
    • Tong, K.I.; Padmanabhan, B.; Kobayashi, A.; Shang, C.; Hirotsu, Y.; Yokoyama, S.; Yamamoto, M. Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response. Mol. Cell Biol. 2007, 27, 7511-7521.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 7511-7521
    • Tong, K.I.1    Padmanabhan, B.2    Kobayashi, A.3    Shang, C.4    Hirotsu, Y.5    Yokoyama, S.6    Yamamoto, M.7
  • 92
    • 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
    • Dinkova-Kostova, A.T.; Holtzclaw, W.D.; Cole, R.N.; Itoh, K.; Wakabayashi, N.; Katoh, Y.; Yamamoto, M.; Talalay, P. 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 2002, 99, 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    Yamamoto, M.7    Talalay, P.8
  • 93
    • 22544464124 scopus 로고    scopus 로고
    • Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2
    • Eggler, A.L.; Liu, G.; Pezzuto, J.M.; van Breemen, R.B.; Mesecar, A.D. Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc. Natl. Acad. Sci. USA 2005, 102, 10070-10075.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10070-10075
    • Eggler, A.L.1    Liu, G.2    Pezzuto, J.M.3    Van Breemen, R.B.4    Mesecar, A.D.5
  • 94
    • 36349019109 scopus 로고    scopus 로고
    • Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent
    • Eggler, A.L.; Luo, Y.; van Breemen, R.B.; Mesecar, A.D. Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent. Chem. Res. Toxicol.2007, 20, 1878-1884.
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1878-1884
    • Eggler, A.L.1    Luo, Y.2    Van Breemen, R.B.3    Mesecar, A.D.4
  • 95
    • 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
    • Zhang, D.D.; Hannink, M. 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. 2003, 23, 8137-8151.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 96
    • 13044304201 scopus 로고    scopus 로고
    • Nrf2 is essential for protection against acute pulmonary injury in mice
    • Chan, K.; Kan, Y.W. Nrf2 is essential for protection against acute pulmonary injury in mice. Proc. Natl. Acad. Sci. USA 1999, 96, 12731-12736.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12731-12736
    • Chan, K.1    Kan, Y.W.2
  • 99
    • 38149003106 scopus 로고    scopus 로고
    • Role of the Nrf2-antioxidant system in cytotoxicity mediated by anticancer cisplatin: Implication to cancer cell resistance
    • Cho, J.M.; Manandhar, S.; Lee, H.R.; Park, H.M.; Kwak, M.K. Role of the Nrf2-antioxidant system in cytotoxicity mediated by anticancer cisplatin: implication to cancer cell resistance. Cancer Lett. 2008, 260, 96-108.
    • (2008) Cancer Lett. , vol.260 , pp. 96-108
    • Cho, J.M.1    Manandhar, S.2    Lee, H.R.3    Park, H.M.4    Kwak, M.K.5
  • 100
    • 1242319539 scopus 로고    scopus 로고
    • Chemoprevention by 1,2-dithiole-3-thiones through induction of NQO1 and other phase 2 enzymes
    • Kwak, M.K.; Ramos-Gomez, M.; Wakabayashi, N.; Kensler, T.W. Chemoprevention by 1,2-dithiole-3-thiones through induction of NQO1 and other phase 2 enzymes. Methods Enzymol. 2004, 382, 414-423.
    • (2004) Methods Enzymol. , vol.382 , pp. 414-423
    • Kwak, M.K.1    Ramos-Gomez, M.2    Wakabayashi, N.3    Kensler, T.W.4
  • 101
    • 33748893228 scopus 로고    scopus 로고
    • Nrf2 regulates an adaptive response protecting against oxidative damage following diquat-mediated formation of superoxide anion
    • Osburn, W.O.; Wakabayashi, N.; Misra, V.; Nilles, T.; Biswal, S.; Trush, M.A.; Kensler, T.W. Nrf2 regulates an adaptive response protecting against oxidative damage following diquat-mediated formation of superoxide anion. Arch. Biochem. Biophys. 2006, 454, 7-15.
    • (2006) Arch. Biochem. Biophys. , vol.454 , pp. 7-15
    • Osburn, W.O.1    Wakabayashi, N.2    Misra, V.3    Nilles, T.4    Biswal, S.5    Trush, M.A.6    Kensler, T.W.7
  • 102
    • 0037356451 scopus 로고    scopus 로고
    • Interactive effects of nrf2 genotype and oltipraz on benzoa.pyrene-DNA adducts and tumor yield in mice
    • Ramos-Gomez, M.; Dolan, P.M.; Itoh, K.; Yamamoto, M.; Kensler, T.W. Interactive effects of nrf2 genotype and oltipraz on benzoa.pyrene-DNA adducts and tumor yield in mice. Carcinogenesis 2003, 24, 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
  • 103
    • 0035875447 scopus 로고    scopus 로고
    • Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust
    • Aoki, Y.; Sato, H.; Nishimura, N.; Takahashi, S.; Itoh, K.; Yamamoto, M. Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust. Toxicol. Appl. Pharmacol. 2001, 173, 154-160.
    • (2001) Toxicol. Appl. Pharmacol. , vol.173 , pp. 154-160
    • Aoki, Y.1    Sato, H.2    Nishimura, N.3    Takahashi, S.4    Itoh, K.5    Yamamoto, M.6
  • 104
  • 105
    • 69749108385 scopus 로고    scopus 로고
    • Nrf2 protects against As(III)-induced damage in mouse liver and bladder
    • Jiang, T.; Huang, Z.; Chan, J.Y.; Zhang, D.D. Nrf2 protects against As(III)-induced damage in mouse liver and bladder. Toxicol. Appl. Pharmacol. 2009, 240, 8-14.
    • (2009) Toxicol. Appl. Pharmacol. , vol.240 , pp. 8-14
    • Jiang, T.1    Huang, Z.2    Chan, J.Y.3    Zhang, D.D.4
  • 107
    • 41549129055 scopus 로고    scopus 로고
    • Antioxidants and phase 2 enzymes in macrophages: Regulation by Nrf2 signaling and protection against oxidative and electrophilic stress
    • Zhu, H.; Jia, Z.; Zhang, L.; Yamamoto, M.; Misra, H.P.; Trush, M.A.; Li, Y. Antioxidants and phase 2 enzymes in macrophages: regulation by Nrf2 signaling and protection against oxidative and electrophilic stress. Exp. Biol. Med. (Maywood) 2008, 233, 463-474.
    • (2008) Exp. Biol. Med. (Maywood) , vol.233 , pp. 463-474
    • Zhu, H.1    Jia, Z.2    Zhang, L.3    Yamamoto, M.4    Misra, H.P.5    Trush, M.A.6    Li, Y.7
  • 108
    • 9444249870 scopus 로고    scopus 로고
    • The transcription factor NRF2 protects against pulmonary fibrosis
    • Cho, H.Y.; Reddy, S.P.; Yamamoto, M.; Kleeberger, S.R. The transcription factor NRF2 protects against pulmonary fibrosis. FASEB J. 2004, 18, 1258-1260.
    • (2004) FASEB J. , vol.18 , pp. 1258-1260
    • Cho, H.Y.1    Reddy, S.P.2    Yamamoto, M.3    Kleeberger, S.R.4
  • 110
    • 56249106571 scopus 로고    scopus 로고
    • Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals
    • Surh, Y.J.; Kundu, J.K.; Na, H.K. Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals. Planta Med. 2008, 74, 1526-1539.
    • (2008) Planta Med. , vol.74 , pp. 1526-1539
    • Surh, Y.J.1    Kundu, J.K.2    Na, H.K.3
  • 111
    • 0034525122 scopus 로고    scopus 로고
    • Chemoprevention of colonic aberrant crypt foci in Fischer rats by sulforaphane and phenethyl isothiocyanate
    • Chung, F.L.; Conaway, C.C.; Rao, C.V.; Reddy, B.S. Chemoprevention of colonic aberrant crypt foci in Fischer rats by sulforaphane and phenethyl isothiocyanate. Carcinogenesis 2000, 21, 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
  • 112
    • 51349088974 scopus 로고    scopus 로고
    • Multi-targeted prevention of cancer by sulforaphane
    • Clarke, J.D.; Dashwood, R.H.; Ho, E. Multi-targeted prevention of cancer by sulforaphane. Cancer Lett. 2008, 269, 291-304.
    • (2008) Cancer Lett. , vol.269 , pp. 291-304
    • Clarke, J.D.1    Dashwood, R.H.2    Ho, E.3
  • 113
    • 0037188518 scopus 로고    scopus 로고
    • Sulforaphane inhibits extracellular, intracellular, and antibiotic-resistant strains of Helicobacter pylori and prevents benzoa.pyrene-induced stomach tumors
    • Fahey, J.W.; Haristoy, X.; Dolan, P.M.; Kensler, T.W.; Scholtus, I.; Stephenson, K.K.; Talalay, P.; Lozniewski, A. Sulforaphane inhibits extracellular, intracellular, and antibiotic-resistant strains of Helicobacter pylori and prevents benzoa.pyrene-induced stomach tumors. Proc. Natl. Acad. Sci. USA 2002, 99, 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    Talalay, P.7    Lozniewski, A.8
  • 114
    • 34247606510 scopus 로고    scopus 로고
    • Molecular basis for chemoprevention by sulforaphane: A comprehensive review
    • Juge, N.; Mithen, R.F.; Traka, M. Molecular basis for chemoprevention by sulforaphane: a comprehensive review. Cell Mol Life Sci. 2007, 64, 1105-1127.
    • (2007) Cell Mol Life Sci. , vol.64 , pp. 1105-1127
    • Juge, N.1    Mithen, R.F.2    Traka, M.3
  • 115
    • 0028203252 scopus 로고
    • Anticarcinogenic activities of sulforaphane and structurally related synthetic norbornyl isothiocyanates
    • Zhang, Y.; Kensler, T.W.; Cho, C.G.; Posner, G.H.; Talalay, P. Anticarcinogenic activities of sulforaphane and structurally related synthetic norbornyl isothiocyanates. Proc. Natl. Acad. Sci. USA 1994, 91, 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
  • 116
    • 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
    • Kensler, T.W.; Egner, P.A.; Dolan, P.M.; Groopman, J.D.; Roebuck, B.D. 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. 1987, 47, 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, B.D.5
  • 117
    • 0026501721 scopus 로고
    • Potent inhibition of aflatoxin-induced hepatic tumorigenesis by the monofunctional enzyme inducer 1,2-dithiole-3-thione
    • Kensler, T.W.; Groopman, J.D.; Eaton, D.L.; Curphey, T.J.; Roebuck, B.D. Potent inhibition of aflatoxin-induced hepatic tumorigenesis by the monofunctional enzyme inducer 1,2-dithiole-3-thione. Carcinogenesis 1992, 13, 95-100.
    • (1992) Carcinogenesis , vol.13 , pp. 95-100
    • Kensler, T.W.1    Groopman, J.D.2    Eaton, D.L.3    Curphey, T.J.4    Roebuck, B.D.5
  • 120
    • 0346074656 scopus 로고    scopus 로고
    • Cancer chemoprevention by resveratrol: in vitro and in vivo studies and the underlying mechanisms (review)
    • Aziz, M.H.; Kumar, R.; Ahmad, N. Cancer chemoprevention by resveratrol: in vitro and in vivo studies and the underlying mechanisms (review). Int. J. Oncol. 2003, 23, 17-28.
    • (2003) Int. J. Oncol. , vol.23 , pp. 17-28
    • Aziz, M.H.1    Kumar, R.2    Ahmad, N.3
  • 121
    • 0036170178 scopus 로고    scopus 로고
    • The daily oral administration of high doses of trans-resveratrol to rats for 28 days is not harmful
    • Juan, M.E.; Vinardell, M.P.; Planas, J.M. The daily oral administration of high doses of trans-resveratrol to rats for 28 days is not harmful. J. Nutr. 2002, 132, 257-260.
    • (2002) J. Nutr. , vol.132 , pp. 257-260
    • Juan, M.E.1    Vinardell, M.P.2    Planas, J.M.3
  • 122
    • 0142166328 scopus 로고    scopus 로고
    • Cancer chemoprevention with dietary phytochemicals
    • Surh, Y.J. Cancer chemoprevention with dietary phytochemicals. Nat. Rev. Cancer 2003, 3, 768-780.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 768-780
    • Surh, Y.J.1
  • 124
    • 33744490370 scopus 로고    scopus 로고
    • Biological effects of curcumin and its role in cancer chemoprevention and therapy
    • Singh, S.; Khar, A. Biological effects of curcumin and its role in cancer chemoprevention and therapy. Anticancer Agents Med. Chem. 2006, 6, 259-270.
    • (2006) Anticancer Agents Med. Chem. , vol.6 , pp. 259-270
    • Singh, S.1    Khar, A.2
  • 127
    • 0036336025 scopus 로고    scopus 로고
    • Selective antiproliferative activity of caffeic acid phenethyl ester analogues on highly liver-metastatic murine colon 26-L5 carcinoma cell line
    • Nagaoka, T.; Banskota, A.H.; Tezuka, Y.; Saiki, I.; Kadota, S. Selective antiproliferative activity of caffeic acid phenethyl ester analogues on highly liver-metastatic murine colon 26-L5 carcinoma cell line. Bioorg. Med. Chem. 2002, 10, 3351-3359.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3351-3359
    • Nagaoka, T.1    Banskota, A.H.2    Tezuka, Y.3    Saiki, I.4    Kadota, S.5
  • 128
    • 0026577605 scopus 로고
    • A major inducer of anticarcinogenic protective enzymes from broccoli: Isolation and elucidation of structure
    • Zhang, Y.; Talalay, P.; Cho, C.G.; Posner, G.H. A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc. Natl. Acad. Sci. USA 1992, 89, 2399-2403.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2399-2403
    • Zhang, Y.1    Talalay, P.2    Cho, C.G.3    Posner, G.H.4
  • 129
    • 24944480252 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate and sulforaphane and their N-acetylcysteine conjugates inhibit malignant progression of lung adenomas induced by tobacco carcinogens in A/J mice
    • Conaway, C.C.; Wang, C.X.; Pittman, B.; Yang, Y.M.; Schwartz, J.E.; Tian, D.; McIntee, E.J.; Hecht, S.S.; Chung, F.L. Phenethyl isothiocyanate and sulforaphane and their N-acetylcysteine conjugates inhibit malignant progression of lung adenomas induced by tobacco carcinogens in A/J mice. Cancer Res. 2005, 65, 8548-8557.
    • (2005) Cancer Res. , vol.65 , pp. 8548-8557
    • Conaway, C.C.1    Wang, C.X.2    Pittman, B.3    Yang, Y.M.4    Schwartz, J.E.5    Tian, D.6    McIntee, E.J.7    Hecht, S.S.8    Chung, F.L.9
  • 130
    • 56249128623 scopus 로고    scopus 로고
    • Dithiolethiones for cancer chemoprevention: Where do we stand?
    • Zhang, Y.; Munday, R. Dithiolethiones for cancer chemoprevention: where do we stand? Mol. Cancer Ther. 2008, 7, 3470-3479.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 3470-3479
    • Zhang, Y.1    Munday, R.2
  • 133
    • 2642559707 scopus 로고    scopus 로고
    • Effects of cis-resveratrol on inflammatory murine macrophages: Antioxidant activity and down-regulation of inflammatory genes
    • Leiro, J.; Alvarez, E.; Arranz, J.A.; Laguna, R.; Uriarte, E.; Orallo, F. Effects of cis-resveratrol on inflammatory murine macrophages: antioxidant activity and down-regulation of inflammatory genes. J. Leukoc. Biol .2004, 75, 1156-1165.
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 1156-1165
    • Leiro, J.1    Alvarez, E.2    Arranz, J.A.3    Laguna, R.4    Uriarte, E.5    Orallo, F.6
  • 135
    • 0028845839 scopus 로고
    • Antioxidant activity of resveratrol in red wine
    • Miller, N.J.; Rice-Evans, C.A. Antioxidant activity of resveratrol in red wine. Clin. Chem. 1995, 41, 1789.
    • (1995) Clin. Chem. , vol.41 , pp. 1789
    • Miller, N.J.1    Rice-Evans, C.A.2
  • 136
    • 18844402874 scopus 로고    scopus 로고
    • Resveratrol upregulates heme oxygenase-1 expression via activation of NF-E2-related factor 2 in PC12 cells
    • Chen, C.Y.; Jang, J.H.; Li, M.H.; Surh, Y.J. Resveratrol upregulates heme oxygenase-1 expression via activation of NF-E2-related factor 2 in PC12 cells. Biochem. Biophys. Res. Commun. 2005, 331, 993-1000.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 993-1000
    • Chen, C.Y.1    Jang, J.H.2    Li, M.H.3    Surh, Y.J.4
  • 137
    • 41549108838 scopus 로고    scopus 로고
    • Resveratrol induces glutathione synthesis by activation of Nrf2 and protects against cigarette smoke-mediated oxidative stress in human lung epithelial cells
    • Kode, A.; Rajendrasozhan, S.; Caito, S.; Yang, S.R.; Megson, I.L.; Rahman, I. Resveratrol induces glutathione synthesis by activation of Nrf2 and protects against cigarette smoke-mediated oxidative stress in human lung epithelial cells. Am. J. Physiol. Lung Cell Mol. Physiol. 2008, 294, L478-488.
    • (2008) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.294
    • Kode, A.1    Rajendrasozhan, S.2    Caito, S.3    Yang, S.R.4    Megson, I.L.5    Rahman, I.6
  • 138
    • 48749085399 scopus 로고    scopus 로고
    • Resveratrol protects primary rat hepatocytes against oxidative stress damage: Activation of the Nrf2 transcription factor and augmented activities of antioxidant enzymes
    • Rubiolo, J.A.; Mithieux, G.; Vega, F.V. Resveratrol protects primary rat hepatocytes against oxidative stress damage: activation of the Nrf2 transcription factor and augmented activities of antioxidant enzymes. Eur. J. Pharmacol. 2008, 591, 66-72.
    • (2008) Eur. J. Pharmacol. , vol.591 , pp. 66-72
    • Rubiolo, J.A.1    Mithieux, G.2    Vega, F.V.3
  • 139
    • 0026093041 scopus 로고
    • Pharmacology of Curcuma longa
    • Ammon, H.P.; Wahl, M.A. Pharmacology of Curcuma longa. Planta Med. 1991, 57, 1-7.
    • (1991) Planta Med. , vol.57 , pp. 1-7
    • Ammon, H.P.1    Wahl, M.A.2
  • 140
    • 0037569694 scopus 로고    scopus 로고
    • Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element
    • Balogun, E.; Hoque, M.; Gong, P.; Killeen, E.; Green, C.J.; Foresti, R.; Alam, J.; Motterlini, R. Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element. Biochem. J. 2003, 371, 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    Alam, J.7    Motterlini, R.8
  • 141
    • 46949104416 scopus 로고    scopus 로고
    • Dietary curcumin modulates transcriptional regulators of phase I and phase II enzymes in benzoa.pyrene-treated mice: Mechanism of its anti-initiating action
    • Garg, R.; Gupta, S.; Maru, G.B. Dietary curcumin modulates transcriptional regulators of phase I and phase II enzymes in benzoa.pyrene-treated mice: mechanism of its anti-initiating action. Carcinogenesis 2008, 29, 1022-1032.
    • (2008) Carcinogenesis , vol.29 , pp. 1022-1032
    • Garg, R.1    Gupta, S.2    Maru, G.B.3
  • 142
    • 27644468991 scopus 로고    scopus 로고
    • The pleiotropic effects of statins
    • Calabro, P.; Yeh, E.T. The pleiotropic effects of statins. Curr Opin Cardiol 2005, 20, 541-546.
    • (2005) Curr Opin Cardiol , vol.20 , pp. 541-546
    • Calabro, P.1    Yeh, E.T.2
  • 143
    • 57149103702 scopus 로고    scopus 로고
    • Pleiotropic effects and cholesterol-lowering therapy
    • Shaw, S.M.; Fildes, J.E.; Yonan, N.; Williams, S.G. Pleiotropic effects and cholesterol-lowering therapy. Cardiology 2009, 112, 4-12.
    • (2009) Cardiology , vol.112 , pp. 4-12
    • Shaw, S.M.1    Fildes, J.E.2    Yonan, N.3    Williams, S.G.4
  • 144
    • 33645471375 scopus 로고    scopus 로고
    • Statins and renal diseases: From primary prevention to renal replacement therapy
    • D'Amico, G. Statins and renal diseases: from primary prevention to renal replacement therapy. J. Am. Soc. Nephrol. 2006, 17, S148-152.
    • (2006) J. Am. Soc. Nephrol. , vol.17
    • D'Amico, G.1
  • 145
    • 29044440878 scopus 로고    scopus 로고
    • Anti-angiogenic and anti-inflammatory effects of statins: Relevance to anti-cancer therapy
    • Dulak, J.; Jozkowicz, A. Anti-angiogenic and anti-inflammatory effects of statins: relevance to anti-cancer therapy. Curr .Cancer Drug Targets 2005, 5, 579-594.
    • (2005) Curr .Cancer Drug Targets , vol.5 , pp. 579-594
    • Dulak, J.1    Jozkowicz, A.2
  • 148
    • 56249107263 scopus 로고    scopus 로고
    • Dietary cancer chemopreventive agents - Targeting inflammation and Nrf2 signaling pathway
    • Khor, T.O.; Yu, S.; Kong, A.N. Dietary cancer chemopreventive agents - targeting inflammation and Nrf2 signaling pathway. Planta Med. 2008, 74, 1540-1547.
    • (2008) Planta Med. , vol.74 , pp. 1540-1547
    • Khor, T.O.1    Yu, S.2    Kong, A.N.3
  • 149
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • Kwak, M.K.; Wakabayashi, N.; Greenlaw, J.L.; Yamamoto, M.; Kensler, T.W. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell Biol. 2003, 23, 8786-8794.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 8786-8794
    • Kwak, M.K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 150
    • 34249727213 scopus 로고    scopus 로고
    • Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: Enhanced activity for degradation of abnormal protein
    • Kwak, M.K.; Huang, B.; Chang, H.; Kim, J.A.; Kensler, T.W. Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein. Life Sci. 2007, 80, 2411-2420.
    • (2007) Life Sci. , vol.80 , pp. 2411-2420
    • Kwak, M.K.1    Huang, B.2    Chang, H.3    Kim, J.A.4    Kensler, T.W.5
  • 151
    • 0036268224 scopus 로고    scopus 로고
    • Hypothesis: Proteasomal dysfunction: A primary event in neurogeneration that leads to nitrative and oxidative stress and subsequent cell death
    • Halliwell, B. Hypothesis: proteasomal dysfunction: a primary event in neurogeneration that leads to nitrative and oxidative stress and subsequent cell death. Ann. N Y Acad. Sci. 2002, 962, 182-194.
    • (2002) Ann. N Y Acad. Sci. , vol.962 , pp. 182-194
    • Halliwell, B.1
  • 152
    • 33644639061 scopus 로고    scopus 로고
    • Proteasomal defense of oxidative protein modifications
    • Poppek, D.; Grune, T. Proteasomal defense of oxidative protein modifications. Antioxid. Redox Signal 2006, 8, 173-184.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 173-184
    • Poppek, D.1    Grune, T.2
  • 153
    • 34249653138 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M.; Dobson, C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003, 27, 27.
    • (2003) J. Mol. Med. , vol.27 , pp. 27
    • Stefani, M.1    Dobson, C.M.2
  • 154
    • 34547092719 scopus 로고    scopus 로고
    • Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells
    • Kwak, M.K.; Cho, J.M.; Huang, B.; Shin, S.; Kensler, T.W. Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells. Free Radic. Biol. Med. 2007, 43, 809-817.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 809-817
    • Kwak, M.K.1    Cho, J.M.2    Huang, B.3    Shin, S.4    Kensler, T.W.5
  • 159
    • 42449110757 scopus 로고    scopus 로고
    • The cytoprotective Nrf2 transcription factor controls insulin receptor signaling in the regenerating liver
    • Beyer, T.A.; Werner, S. The cytoprotective Nrf2 transcription factor controls insulin receptor signaling in the regenerating liver. Cell Cycle 2008, 7, 874-878.
    • (2008) Cell Cycle , vol.7 , pp. 874-878
    • Beyer, T.A.1    Werner, S.2
  • 161
    • 0037154380 scopus 로고    scopus 로고
    • Inhibition of dimethylnitrosamine-induced liver fibrosis by 5-(2-pyrazinyl)-4-methyl-1,2-dithiol-3-thione. (oltipraz) in rats: Suppression of transforming growth factor-beta1 and tumor necrosis factor-alpha expression
    • Kang, K.W.; Choi, S.H.; Ha, J.R.; Kim, C.W.; Kim, S.G. Inhibition of dimethylnitrosamine-induced liver fibrosis by 5-(2-pyrazinyl)-4-methyl-1,2- dithiol-3-thione. (oltipraz) in rats: suppression of transforming growth factor-beta1 and tumor necrosis factor-alpha expression. Chem. Biol. Interact 2002, 139, 61-77.
    • (2002) Chem. Biol. Interact , vol.139 , pp. 61-77
    • Kang, K.W.1    Choi, S.H.2    Ha, J.R.3    Kim, C.W.4    Kim, S.G.5
  • 162
    • 0036884409 scopus 로고    scopus 로고
    • Oltipraz regenerates cirrhotic liver through CCAAT/enhancer binding protein-mediated stellate cell inactivation
    • Kang, K.W.; Kim, Y.G.; Cho, M.K.; Bae, S.K.; Kim, C.W.; Lee, M.G.; Kim, S.G. Oltipraz regenerates cirrhotic liver through CCAAT/enhancer binding protein-mediated stellate cell inactivation. FASEB J. 2002, 16, 1988-1990.
    • (2002) FASEB J. , vol.16 , pp. 1988-1990
    • Kang, K.W.1    Kim, Y.G.2    Cho, M.K.3    Bae, S.K.4    Kim, C.W.5    Lee, M.G.6    Kim, S.G.7
  • 163
    • 0344915418 scopus 로고
    • Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis
    • Talalay, P.; De Long, M.J.; Prochaska, H.J. Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proc. Natl. Acad. Sci. USA 1988, 85, 8261-8265.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8261-8265
    • Talalay, P.1    De Long, M.J.2    Prochaska, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.