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Volumn 43, Issue 36, 2004, Pages 11417-11426

Crystal structure of quinone reductase 2 in complex with resveratrol

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION CONSTANTS; ENZYME EXPRESSION; NATURAL POLYPHENOLS; OXIDATIVE STRESSES;

EID: 4444267291     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049162o     Document Type: Article
Times cited : (218)

References (69)
  • 1
    • 0030760030 scopus 로고    scopus 로고
    • Wine as a biological fluid: History, production, and role in disease prevention
    • Soleas, G. J., Diamandis, E. P., and Goldberg, D. M. (1997) Wine as a biological fluid: History, production, and role in disease prevention, J. Clin. Lab. Anal. 11, 287-313.
    • (1997) J. Clin. Lab. Anal. , vol.11 , pp. 287-313
    • Soleas, G.J.1    Diamandis, E.P.2    Goldberg, D.M.3
  • 3
    • 0036297527 scopus 로고    scopus 로고
    • Cancer chemopreventive activity of resveratrol
    • Bhat, K. P., and Pezzuto, J. M. (2002) Cancer chemopreventive activity of resveratrol, Ann. N.Y. Acad. Sci. 957, 210-229.
    • (2002) Ann. N.Y. Acad. Sci. , vol.957 , pp. 210-229
    • Bhat, K.P.1    Pezzuto, J.M.2
  • 4
    • 0034827121 scopus 로고    scopus 로고
    • Resveratrol inhibits intestinal tumorigenesis and modulates host-defense-related gene expression in an animal model of human familial adenomatous polyposis
    • Schneider, Y., Duranton, B., Gosse, F., Schleiffer, R., Seiler, N., and Raul, F. (2001) Resveratrol inhibits intestinal tumorigenesis and modulates host-defense-related gene expression in an animal model of human familial adenomatous polyposis, Nutr. Cancer 39, 102-107.
    • (2001) Nutr. Cancer , vol.39 , pp. 102-107
    • Schneider, Y.1    Duranton, B.2    Gosse, F.3    Schleiffer, R.4    Seiler, N.5    Raul, F.6
  • 5
    • 0038075469 scopus 로고    scopus 로고
    • Point: From animal models to prevention of colon cancer. Systematic review of chemoprevention in min mice and choice of the model system
    • Corpet, D. E., and Pierre, F. (2003) Point: From animal models to prevention of colon cancer. Systematic review of chemoprevention in min mice and choice of the model system, Cancer Epidemiol., Biomarkers Prev. 12, 391-400.
    • (2003) Cancer Epidemiol., Biomarkers Prev. , vol.12 , pp. 391-400
    • Corpet, D.E.1    Pierre, F.2
  • 7
    • 0037454754 scopus 로고    scopus 로고
    • Inhibition of free radical-induced peroxidation of rat liver microsomes by resveratrol and its analogues
    • Cai, Y. J., Fang, J. G., Ma, L. P., Yang, L., and Liu, Z. L. (2003) Inhibition of free radical-induced peroxidation of rat liver microsomes by resveratrol and its analogues, Biochim. Biophys. Acta 1637, 31-38.
    • (2003) Biochim. Biophys. Acta , vol.1637 , pp. 31-38
    • Cai, Y.J.1    Fang, J.G.2    Ma, L.P.3    Yang, L.4    Liu, Z.L.5
  • 8
    • 0035015930 scopus 로고    scopus 로고
    • Inhibition of oxidative and antioxidative enzymes by trans-resveratrol
    • Fan, X., and Matthis, J. P. (2001) Inhibition of oxidative and antioxidative enzymes by trans-resveratrol, J. Food Sci. 66, 200-203.
    • (2001) J. Food Sci. , vol.66 , pp. 200-203
    • Fan, X.1    Matthis, J.P.2
  • 9
    • 0033952265 scopus 로고    scopus 로고
    • Effect of resveratrol, a natural polyphenolic compound, on reactive oxygen species and prostaglandin production
    • Martinez, J., and Moreno, J. J. (2000) Effect of resveratrol, a natural polyphenolic compound, on reactive oxygen species and prostaglandin production, Biochem. Pharmacol. 59, 865-870.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 865-870
    • Martinez, J.1    Moreno, J.J.2
  • 10
    • 0037414403 scopus 로고    scopus 로고
    • Oral administration of trans-resveratrol to guinea pigs increases cardiac DT-diaphorase and catalase activities, and protects isolated atria from menadione toxicity
    • Floreani, M., Napoli, E., Quintieri, L., and Palatini, P. (2003) Oral administration of trans-resveratrol to guinea pigs increases cardiac DT-diaphorase and catalase activities, and protects isolated atria from menadione toxicity, Life Sci. 72, 2741-2750.
    • (2003) Life Sci. , vol.72 , pp. 2741-2750
    • Floreani, M.1    Napoli, E.2    Quintieri, L.3    Palatini, P.4
  • 11
    • 1942484416 scopus 로고    scopus 로고
    • Potent induction of cellular antioxidants and phase 2 enzymes by resveratrol in cardiomyocytes: Protection against oxidative and electrophilic injury
    • Cao, Z., and Li, Y. (2004) Potent induction of cellular antioxidants and phase 2 enzymes by resveratrol in cardiomyocytes: Protection against oxidative and electrophilic injury, Eur. J. Pharmacol. 489, 39-48.
    • (2004) Eur. J. Pharmacol. , vol.489 , pp. 39-48
    • Cao, Z.1    Li, Y.2
  • 12
    • 0033805326 scopus 로고    scopus 로고
    • Persuasive evidence that quinone reductase type 1 (DT diaphorase) protects cells against the toxicity of electrophiles and reactive forms of oxygen
    • Dinkova-Kostova, A. T., and Talalay, P. (2000) Persuasive evidence that quinone reductase type 1 (DT diaphorase) protects cells against the toxicity of electrophiles and reactive forms of oxygen, Free Radical Biol. Med. 29, 231-240.
    • (2000) Free Radical Biol. Med. , vol.29 , pp. 231-240
    • Dinkova-Kostova, A.T.1    Talalay, P.2
  • 13
    • 0027938689 scopus 로고
    • Oxy-radicals and cancer
    • Cerutti, P. A. (1994) Oxy-radicals and cancer, Lancet 344, 862-863.
    • (1994) Lancet , vol.344 , pp. 862-863
    • Cerutti, P.A.1
  • 15
    • 0034011261 scopus 로고    scopus 로고
    • Oxyradicals and DNA damage
    • Marnett, L. J. (2000) Oxyradicals and DNA damage, Carcinogenesis 21, 361-370.
    • (2000) Carcinogenesis , vol.21 , pp. 361-370
    • Marnett, L.J.1
  • 16
    • 0036716819 scopus 로고    scopus 로고
    • Identification of potential prostate cancer preventive agents through induction of quinone reductase in vitro
    • Brooks, J. D., Goldberg, M. F., Nelson, L. A., Wu, D., and Nelson, W. G. (2002) Identification of potential prostate cancer preventive agents through induction of quinone reductase in vitro, Cancer Epidemiol., Biomarkers Prev. 11, 868-875.
    • (2002) Cancer Epidemiol., Biomarkers Prev. , vol.11 , pp. 868-875
    • Brooks, J.D.1    Goldberg, M.F.2    Nelson, L.A.3    Wu, D.4    Nelson, W.G.5
  • 17
    • 0035798831 scopus 로고    scopus 로고
    • Induction of human NAD(P)H:quinone oxidoreductase (NQO1) gene expression by the flavonol quercetin
    • Valerio, L. G., Jr., Kepa, J. K., Pickwell, G. V., and Quattrochi, L. C. (2001) Induction of human NAD(P)H:quinone oxidoreductase (NQO1) gene expression by the flavonol quercetin, Toxicol. Lett. 119, 49-57.
    • (2001) Toxicol. Lett. , vol.119 , pp. 49-57
    • Valerio Jr., L.G.1    Kepa, J.K.2    Pickwell, G.V.3    Quattrochi, L.C.4
  • 19
    • 12644302182 scopus 로고    scopus 로고
    • Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)
    • Zhao, Q., Yang, X. L., Holtzclaw, W. D., and Talalay, P. (1997) Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase), Proc. Natl. Acad. Sci. U.S.A. 94, 1669-1674.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1669-1674
    • Zhao, Q.1    Yang, X.L.2    Holtzclaw, W.D.3    Talalay, P.4
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • (Carter, J. R. M. S. C. W., Ed.), Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) in Methods in Enzymology (Carter, J. R. M. S. C. W., Ed.) pp 307-326, Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0033520090 scopus 로고    scopus 로고
    • Crystal structure of human quinone reductase type 2, a metalloflavoprotein
    • Foster, C. E., Bianchet, M. A., Talalay, P., Zhao, Q., and Amzel, L. M. (1999) Crystal structure of human quinone reductase type 2, a metalloflavoprotein, Biochemistry 38, 9881-9886.
    • (1999) Biochemistry , vol.38 , pp. 9881-9886
    • Foster, C.E.1    Bianchet, M.A.2    Talalay, P.3    Zhao, Q.4    Amzel, L.M.5
  • 23
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 24
    • 0034903751 scopus 로고    scopus 로고
    • Molray - A web interface between O and the POV-Ray ray tracer
    • Harris, M., and Jones, T. A. (2001) Molray - A web interface between O and the POV-Ray ray tracer, Acta Crystallogr., Sect. D 57, 1201-1203.
    • (2001) Acta Crystallogr., Sect. D , vol.57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 25
    • 0242582359 scopus 로고    scopus 로고
    • Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action
    • Lam, A. M., Keeney, D., and Frick, D. N. (2003) Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action, J. Biol. Chem. 278, 44514-44524.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44514-44524
    • Lam, A.M.1    Keeney, D.2    Frick, D.N.3
  • 27
    • 0345074085 scopus 로고    scopus 로고
    • Dietary supplementation of curcumin enhances anti-oxidant and phase II metabolizing enzymes in ddY male mice: Possible role in protection against chemical carcinogenesis and toxicity
    • Iqbal, M., Sharma, S. D., Okazaki, Y., Fujisawa, M., and Okada, S. (2003) Dietary supplementation of curcumin enhances anti-oxidant and phase II metabolizing enzymes in ddY male mice: Possible role in protection against chemical carcinogenesis and toxicity, Pharmacol. Toxicol. 92, 33-38.
    • (2003) Pharmacol. Toxicol. , vol.92 , pp. 33-38
    • Iqbal, M.1    Sharma, S.D.2    Okazaki, Y.3    Fujisawa, M.4    Okada, S.5
  • 28
    • 0032793633 scopus 로고    scopus 로고
    • Molecular characterization of binding of substrates and inhibitors to DT-diaphorase: Combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling
    • Chen, S., Wu, K., Zhang, D., Sherman, M., Knox, R., and Yang, C. S. (1999) Molecular characterization of binding of substrates and inhibitors to DT-diaphorase: Combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling, Mol. Pharmacol. 56, 272-278.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 272-278
    • Chen, S.1    Wu, K.2    Zhang, D.3    Sherman, M.4    Knox, R.5    Yang, C.S.6
  • 29
    • 0000665443 scopus 로고
    • Enzymatic oxidation of some nonphosphorylated derivatives of dihydronicotinamide
    • Liao, S. W.-A., H. G. (1961) Enzymatic oxidation of some nonphosphorylated derivatives of dihydronicotinamide, Biochem. Biophys. Res. Commun. 4, 208-213.
    • (1961) Biochem. Biophys. Res. Commun. , vol.4 , pp. 208-213
    • Liao, S.W.-A.1
  • 30
    • 0031573462 scopus 로고    scopus 로고
    • Catalytic properties of NAD-(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase
    • Wu, K., Knox, R., Sun, X. Z., Joseph, P., Jaiswal, A. K., Zhang, D., Deng, P. S., and Chen, S. (1997) Catalytic properties of NAD-(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase, Arch. Biochem. Biophys. 347, 221-228.
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 221-228
    • Wu, K.1    Knox, R.2    Sun, X.Z.3    Joseph, P.4    Jaiswal, A.K.5    Zhang, D.6    Deng, P.S.7    Chen, S.8
  • 32
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li, R., Bianchet, M. A., Talalay, P., and Amzel, L. M. (1995) The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction, Proc. Natl. Acad. Sci. U.S.A. 92, 8846-8850.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 34
    • 0037195924 scopus 로고    scopus 로고
    • Disruption of dihydronicotinamide riboside:quinone oxidoreductase 2 (NQO2) leads to myeloid hyperplasia of bone marrow and decreased sensitivity to menadione toxicity
    • Long, D. J., II, Iskander, K., Gaikwad, A., Arin, M., Roop, D. R., Knox, R., Barrios, R., and Jaiswal, A. K. (2002) Disruption of dihydronicotinamide riboside:quinone oxidoreductase 2 (NQO2) leads to myeloid hyperplasia of bone marrow and decreased sensitivity to menadione toxicity, J. Biol. Chem. 277, 46131-46139.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46131-46139
    • Long II, D.J.1    Iskander, K.2    Gaikwad, A.3    Arin, M.4    Roop, D.R.5    Knox, R.6    Barrios, R.7    Jaiswal, A.K.8
  • 35
    • 0036605993 scopus 로고    scopus 로고
    • Disruption of the NAD(P)H:quinone oxidoreductase 1 (NQO1) gene in mice causes myelogenous hyperplasia
    • Long, D. J., II, Gaikwad, A., Multani, A., Pathak, S., Montgomery, C. A., Gonzalez, F. J., and Jaiswal, A. K. (2002) Disruption of the NAD(P)H:quinone oxidoreductase 1 (NQO1) gene in mice causes myelogenous hyperplasia, Cancer Res. 62, 3030-3036.
    • (2002) Cancer Res. , vol.62 , pp. 3030-3036
    • Long II, D.J.1    Gaikwad, A.2    Multani, A.3    Pathak, S.4    Montgomery, C.A.5    Gonzalez, F.J.6    Jaiswal, A.K.7
  • 36
    • 0033233393 scopus 로고    scopus 로고
    • Cancer chemoprevention: Progress and promise
    • Kelloff, G. J., Sigman, C. C., and Greenwald, P. (1999) Cancer chemoprevention: Progress and promise, Eur. J. Cancer 35, 2031-2038.
    • (1999) Eur. J. Cancer , vol.35 , pp. 2031-2038
    • Kelloff, G.J.1    Sigman, C.C.2    Greenwald, P.3
  • 39
    • 0032536187 scopus 로고    scopus 로고
    • Resveratrol, a remarkable inhibitor of ribonucleotide reductase
    • Fontecave, M., Lepoivre, M., Elleingand, E., Gerez, C., and Guittet, O. (1998) Resveratrol, a remarkable inhibitor of ribonucleotide reductase, FEBS Lett. 421, 277-279.
    • (1998) FEBS Lett. , vol.421 , pp. 277-279
    • Fontecave, M.1    Lepoivre, M.2    Elleingand, E.3    Gerez, C.4    Guittet, O.5
  • 40
    • 0032830226 scopus 로고    scopus 로고
    • Capillary electrophoretic determination of resveratrol in wines
    • Gu, X., Creasy, L., Kester, A., and Zeece, M. (1999) Capillary electrophoretic determination of resveratrol in wines, J. Agric. Food Chem. 47, 3223-3227.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3223-3227
    • Gu, X.1    Creasy, L.2    Kester, A.3    Zeece, M.4
  • 43
    • 2442455834 scopus 로고    scopus 로고
    • Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors
    • Brehmer, D., Godl, K., Zech, B., Wissing, J., and Daub, H. (2004) Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors, Mol. Cell Proteomics 3, 490-500.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 490-500
    • Brehmer, D.1    Godl, K.2    Zech, B.3    Wissing, J.4    Daub, H.5
  • 45
    • 4444265496 scopus 로고    scopus 로고
    • Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines
    • Kwiek, J. J., Haystead, T. A., and Rudolph, J. (2004) Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines, Biochemistry 43, 4538-4547.
    • (2004) Biochemistry , vol.43 , pp. 4538-4547
    • Kwiek, J.J.1    Haystead, T.A.2    Rudolph, J.3
  • 46
    • 0346074656 scopus 로고    scopus 로고
    • Cancer chemoprevention by resveratrol: In vitro and in vivo studies and the underlying mechanisms
    • Aziz, M. H., Kumar, R., and Ahmad, N. (2003) Cancer chemoprevention by resveratrol: In vitro and in vivo studies and the underlying mechanisms (review), Int. J. Oncol. 23, 17-28.
    • (2003) Int. J. Oncol. , vol.23 , pp. 17-28
    • Aziz, M.H.1    Kumar, R.2    Ahmad, N.3
  • 49
    • 0027219704 scopus 로고
    • Inhibition of NAD(P)H:quinone acceptor oxidoreductase by flavones: A structure-activity study
    • Chen, S., Hwang, J., and Deng, P. S. (1993) Inhibition of NAD(P)H:quinone acceptor oxidoreductase by flavones: A structure-activity study, Arch. Biochem. Biophys. 302, 72-77.
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 72-77
    • Chen, S.1    Hwang, J.2    Deng, P.S.3
  • 50
    • 0024781837 scopus 로고
    • Mechanisms of induction of enzymes that protect against chemical carcinogenesis
    • Talalay, P. (1989) Mechanisms of induction of enzymes that protect against chemical carcinogenesis, Adv. Enzyme Regul. 28, 237-250.
    • (1989) Adv. Enzyme Regul. , vol.28 , pp. 237-250
    • Talalay, P.1
  • 51
    • 0035963293 scopus 로고    scopus 로고
    • Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase 1 gene
    • Dhakshinamoorthy, S., and Jaiswal, A. K. (2001) Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase 1 gene, Oncogene 20, 3906-3917.
    • (2001) Oncogene , vol.20 , pp. 3906-3917
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 52
    • 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
    • McMahon, M., Itoh, K., Yamamoto, M., Ghanas, S. A., Henderson, C. J., McLellan, L. I., Wolf, C. R., Cavin, C., and Hayes, J. D. (2001) 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, 3299-3307.
    • (2001) Cancer Res. , vol.61 , pp. 3299-3307
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Ghanas, S.A.4    Henderson, C.J.5    McLellan, L.I.6    Wolf, C.R.7    Cavin, C.8    Hayes, J.D.9
  • 53
    • 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., and Kensler, T. W. (2003) 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, 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
  • 54
    • 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., II, Waikel, R. L., Wang, X. J., Perlaky, L., Roop, D. R., and Jaiswal, A. K. (2000) NAD(P)H:quinone oxidoreductase 1 deficiency increases susceptibility to benzo[a]pyrene-induced mouse skin carcinogenesis, Cancer Res. 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
  • 55
    • 0035422794 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase 1 deficiency and increased susceptibility to 7,12-dimethylbenz[a]-anthracene-induced carcinogenesis in mouse skin
    • Long, D. J., II, Waikel, R. L., Wang, X. J., Roop, D. R., and Jaiswal, A. K. (2001) NAD(P)H:quinone oxidoreductase 1 deficiency and increased susceptibility to 7,12-dimethylbenz[a]-anthracene-induced carcinogenesis in mouse skin, J. Natl. Cancer Inst. 93, 1166-1170.
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 1166-1170
    • Long II, D.J.1    Waikel, R.L.2    Wang, X.J.3    Roop, D.R.4    Jaiswal, A.K.5
  • 58
    • 0032804227 scopus 로고    scopus 로고
    • Association of NAD(P)H:quinone oxidoreductase (NQO1) null with numbers of basal cell carcinomas: Use of a multivariate model to rank the relative importance of this polymorphism and those at other relevant loci
    • Clairmont, A., Sies, H., Ramachandran, S., Lear, J. T., Smith, A. G., Bowers, B., Jones, P. W., Fryer, A. A., and Strange, R. C. (1999) Association of NAD(P)H:quinone oxidoreductase (NQO1) null with numbers of basal cell carcinomas: Use of a multivariate model to rank the relative importance of this polymorphism and those at other relevant loci, Carcinogenesis 20, 1235-1240.
    • (1999) Carcinogenesis , vol.20 , pp. 1235-1240
    • Clairmont, A.1    Sies, H.2    Ramachandran, S.3    Lear, J.T.4    Smith, A.G.5    Bowers, B.6    Jones, P.W.7    Fryer, A.A.8    Strange, R.C.9
  • 59
    • 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., and Lafuente, A. (2000) NAD(P)H:quinone oxidoreductase-dependent risk for colorectal cancer and its association with the presence of K-ras mutations in tumors, Carcinogenesis 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
  • 60
    • 0037114637 scopus 로고    scopus 로고
    • Low NAD(P)H:quinone oxidoreductase activity is associated with increased risk of leukemia with MLL translocations in infants and children
    • Smith, M. T., Wang, Y., Skibola, C. F., Slater, D. J., Lo Nigro, L., Nowell, P. C., Lange, B. J., and Felix, C. A. (2002) Low NAD(P)H:quinone oxidoreductase activity is associated with increased risk of leukemia with MLL translocations in infants and children, Blood 100, 4590-4593.
    • (2002) Blood , vol.100 , pp. 4590-4593
    • Smith, M.T.1    Wang, Y.2    Skibola, C.F.3    Slater, D.J.4    Lo Nigro, L.5    Nowell, P.C.6    Lange, B.J.7    Felix, C.A.8
  • 62
    • 12444342653 scopus 로고    scopus 로고
    • Association of NAD(P)H:quinone oxidoreductase 1 (NQO1) C609T polymorphism with esophageal squamous cell carcinoma in a German Caucasian and a northern Chinese population
    • Zhang, J., Schulz, W. A., Li, Y., Wang, R., Zotz, R., Wen, D., Siegel, D., Ross, D., Gabbert, H. E., and Sarbia, M. (2003) Association of NAD(P)H:quinone oxidoreductase 1 (NQO1) C609T polymorphism with esophageal squamous cell carcinoma in a German Caucasian and a northern Chinese population, Carcinogenesis 24, 905-909.
    • (2003) Carcinogenesis , vol.24 , pp. 905-909
    • Zhang, J.1    Schulz, W.A.2    Li, Y.3    Wang, R.4    Zotz, R.5    Wen, D.6    Siegel, D.7    Ross, D.8    Gabbert, H.E.9    Sarbia, M.10
  • 65
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., O'Connor, T., and Yamamoto, M. (2003) Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles, Genes Cells 8, 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
  • 66
    • 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., and Yamamoto, M. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain, Genes Dev. 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
  • 68
    • 0037015682 scopus 로고    scopus 로고
    • Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2
    • Sekhar, K. R., Yan, X. X., and Freeman, M. L. (2002) Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2, Oncogene 21, 6829-6834.
    • (2002) Oncogene , vol.21 , pp. 6829-6834
    • Sekhar, K.R.1    Yan, X.X.2    Freeman, M.L.3
  • 69
    • 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
    • McMahon, M., Itoh, K., Yamamoto, M., and Hayes, J. D. (2003) Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression, J. Biol. Chem. 278, 21592-21600.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4


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