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Volumn 85, Issue 6, 2013, Pages 705-717

The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation

Author keywords

Cell defence; Keap1; Nrf2; Oxidative stress; Regulation

Indexed keywords

CASEIN KINASE II; CAVEOLIN 1; CYSTEINE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; MICRORNA; PROTEASOME; TRANSCRIPTION FACTOR NRF2;

EID: 84874111758     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2012.11.016     Document Type: Note
Times cited : (892)

References (126)
  • 1
    • 47849083585 scopus 로고    scopus 로고
    • Nrf2 signaling: An adaptive response pathway for protection against environmental toxic insults
    • W.O. Osburn, and T.W. Kensler Nrf2 signaling: an adaptive response pathway for protection against environmental toxic insults Mutat Res 659 2008 31 39
    • (2008) Mutat Res , vol.659 , pp. 31-39
    • Osburn, W.O.1    Kensler, T.W.2
  • 2
    • 20144385916 scopus 로고    scopus 로고
    • Transcriptional regulation of NF-E2 p45-related factor (NRF2) expression by the aryl hydrocarbon receptor-xenobiotic response element signaling pathway: Direct cross-talk between phase I and II drug-metabolizing enzymes
    • DOI 10.1074/jbc.M412081200
    • W. Miao, L. Hu, P.J. Scrivens, and G. Batist Transcriptional regulation of NF-E2 p45-related factor (NRF2) expression by the aryl hydrocarbon receptor-xenobiotic response element signaling pathway: direct cross-talk between phase I and II drug-metabolizing enzymes J Biol Chem 280 2005 20340 20348 (Pubitemid 40776732)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20340-20348
    • Miao, W.1    Hu, L.2    Scrivens, P.J.3    Batist, G.4
  • 3
    • 65549131476 scopus 로고    scopus 로고
    • Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational level
    • X.J. Wang, and D.D. Zhang Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational level PLoS One 4 2009 e5492
    • (2009) PLoS One , vol.4 , pp. 5492
    • Wang, X.J.1    Zhang, D.D.2
  • 4
    • 84864359086 scopus 로고    scopus 로고
    • Mechanism of chemical activation of Nrf2
    • Y. Li, J.D. Paonessa, and Y. Zhang Mechanism of chemical activation of Nrf2 PLoS One 7 2012 e35122
    • (2012) PLoS One , vol.7 , pp. 35122
    • Li, Y.1    Paonessa, J.D.2    Zhang, Y.3
  • 6
    • 0029043995 scopus 로고
    • Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins
    • K. Itoh, K. Igarashi, N. Hayashi, M. Nishizawa, and M. Yamamoto Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins Mol Cell Biol 15 1995 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
  • 7
    • 77649271223 scopus 로고    scopus 로고
    • The rise of antioxidant signaling - The evolution and hormetic actions of Nrf2
    • J. Maher, and M. Yamamoto The rise of antioxidant signaling - the evolution and hormetic actions of Nrf2 Toxicol Appl Pharmacol 244 2010 4 15
    • (2010) Toxicol Appl Pharmacol , vol.244 , pp. 4-15
    • Maher, J.1    Yamamoto, M.2
  • 8
    • 77953290236 scopus 로고    scopus 로고
    • Proteomic analysis of Nrf2 deficient transgenic mice reveals cellular defence and lipid metabolism as primary Nrf2-dependent pathways in the liver
    • N.R. Kitteringham, A. Abdullah, J. Walsh, L. Randle, R.E. Jenkins, and R. Sison Proteomic analysis of Nrf2 deficient transgenic mice reveals cellular defence and lipid metabolism as primary Nrf2-dependent pathways in the liver J Proteomics 73 2010 1612 1631
    • (2010) J Proteomics , vol.73 , pp. 1612-1631
    • Kitteringham, N.R.1    Abdullah, A.2    Walsh, J.3    Randle, L.4    Jenkins, R.E.5    Sison, R.6
  • 9
    • 70349140473 scopus 로고    scopus 로고
    • Role of Nrf2 in prevention of high-fat diet-induced obesity by synthetic triterpenoid CDDO-imidazolide
    • S. Shin, J. Wakabayashi, M.S. Yates, N. Wakabayashi, P.M. Dolan, and S. Aja Role of Nrf2 in prevention of high-fat diet-induced obesity by synthetic triterpenoid CDDO-imidazolide Eur J Pharmacol 620 2009 138 144
    • (2009) Eur J Pharmacol , vol.620 , pp. 138-144
    • Shin, S.1    Wakabayashi, J.2    Yates, M.S.3    Wakabayashi, N.4    Dolan, P.M.5    Aja, S.6
  • 10
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
    • DOI 10.1515/BC.2006.164, PII BCHM38710111311
    • K.I. Tong, A. Kobayashi, F. Katsuoka, and M. Yamamoto Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism Biol Chem 387 2006 1311 1320 (Pubitemid 44691409)
    • (2006) Biological Chemistry , vol.387 , Issue.10-11 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 11
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory Mechanisms Controlling Gene Expression Mediated by the Antioxidant Response Element
    • DOI 10.1146/annurev.pharmtox.43.100901.140229
    • T. Nguyen, P.J. Sherratt, and C.B. Pickett Regulatory mechanisms controlling gene expression mediated by the antioxidant response element Annu Rev Pharmacol Toxicol 43 2003 233 260 (Pubitemid 37372641)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherratt, P.J.2    Pickett, C.B.3
  • 13
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • DOI 10.1080/10715769900300851
    • J.D. Hayes, and L.I. McLellan Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress Free Radic Res 31 1999 273 300 (Pubitemid 29452854)
    • (1999) Free Radical Research , vol.31 , Issue.4 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 16
    • 0037569694 scopus 로고    scopus 로고
    • Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element
    • DOI 10.1042/BJ20021619
    • E. Balogun, M. Hoque, P. Gong, E. Killeen, C.J. Green, and R. Foresti Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element Biochem J 371 2003 887 895 (Pubitemid 36578887)
    • (2003) Biochemical Journal , vol.371 , Issue.3 , 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
  • 17
    • 46949104416 scopus 로고    scopus 로고
    • Dietary curcumin modulates transcriptional regulators of phase I and phase II enzymes in benzo[a]pyrene-treated mice: Mechanism of its anti-initiating action
    • DOI 10.1093/carcin/bgn064
    • R. Garg, S. Gupta, and G.B. Maru Dietary curcumin modulates transcriptional regulators of phase I and phase II enzymes in benzo[a]pyrene-treated mice: mechanism of its anti-initiating action Carcinogenesis 29 2008 1022 1032 (Pubitemid 351982248)
    • (2008) Carcinogenesis , vol.29 , Issue.5 , pp. 1022-1032
    • Garg, R.1    Gupta, S.2    Maru, G.B.3
  • 18
    • 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
    • A. Kode, S. Rajendrasozhan, S. Caito, S.R. Yang, I.L. Megson, and I. Rahman 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 294 2008 L478 L488
    • (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
  • 19
    • 18844402874 scopus 로고    scopus 로고
    • Resveratrol upregulates heme oxygenase-1 expression via activation of NF-E2-related factor 2 in PC12 cells
    • C.Y. Chen, J.H. Jang, M.H. Li, and Y.J. Surh Resveratrol upregulates heme oxygenase-1 expression via activation of NF-E2-related factor 2 in PC12 cells Biochem Biophys Res Commun 331 2005 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
  • 22
    • 79953889329 scopus 로고    scopus 로고
    • Nrf2 is overexpressed in pancreatic cancer: Implications for cell proliferation and therapy
    • A. Lister, T. Nedjadi, N.R. Kitteringham, F. Campbell, E. Costello, and B. Lloyd Nrf2 is overexpressed in pancreatic cancer: implications for cell proliferation and therapy Mol Cancer 10 2011 37
    • (2011) Mol Cancer , vol.10 , pp. 37
    • Lister, A.1    Nedjadi, T.2    Kitteringham, N.R.3    Campbell, F.4    Costello, E.5    Lloyd, B.6
  • 23
    • 79960060305 scopus 로고    scopus 로고
    • Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
    • G.M. DeNicola, F.A. Karreth, T.J. Humpton, A. Gopinathan, C. Wei, and K. Frese Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis Nature 475 2011 106 109
    • (2011) Nature , vol.475 , pp. 106-109
    • Denicola, G.M.1    Karreth, F.A.2    Humpton, T.J.3    Gopinathan, A.4    Wei, C.5    Frese, K.6
  • 24
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • T.W. Kensler, N. Wakabayashi, and S. Biswal Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway Annu Rev Pharmacol Toxicol 47 2007 89 116
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 25
    • 84863769005 scopus 로고    scopus 로고
    • The Keap1-Nrf2 cell defense pathway - A promising therapeutic target
    • I.M. Copple The Keap1-Nrf2 cell defense pathway - a promising therapeutic target Adv Pharmacol 63 2012 43 79
    • (2012) Adv Pharmacol , vol.63 , pp. 43-79
    • Copple, I.M.1
  • 27
    • 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 (Pubitemid 29045117)
    • (1999) Genes and Development , vol.13 , Issue.1 , 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
  • 28
    • 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 oxidoreductase1 gene
    • DOI 10.1038/sj.onc.1204506
    • S. Dhakshinamoorthy, and A.K. Jaiswal Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase1 gene Oncogene 20 2001 3906 3917 (Pubitemid 32646201)
    • (2001) Oncogene , vol.20 , Issue.29 , pp. 3906-3917
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 29
    • 0037183998 scopus 로고    scopus 로고
    • The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • L.M. Zipper, and R.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, R.T.2
  • 30
    • 77958125017 scopus 로고    scopus 로고
    • Discovery of the negative regulator of Nrf2, Keap1: A historical overview
    • K. Itoh, J. Mimura, and M. Yamamoto Discovery of the negative regulator of Nrf2, Keap1: a historical overview Antioxid Redox Signal 13 2010 1665 1678
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1665-1678
    • Itoh, K.1    Mimura, J.2    Yamamoto, M.3
  • 32
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • DOI 10.1046/j.1365-2443.2003.00640.x
    • 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 (Pubitemid 36504013)
    • (2003) Genes to Cells , vol.8 , Issue.4 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 34
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • DOI 10.1128/MCB.24.16.7130-7139.2004
    • A. Kobayashi, M.I. Kang, H. Okawa, M. Ohtsuji, Y. Zenke, and T. Chiba Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2 Mol Cell Biol 24 2004 7130 7139 (Pubitemid 39014439)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.16 , 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
  • 35
    • 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
    • DOI 10.1074/jbc.M300931200
    • 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 (Pubitemid 36792558)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 36
    • 0035260034 scopus 로고    scopus 로고
    • Role of Transcription Factor Nrf2 in the Induction of Hepatic Phase 2 and Antioxidative Enzymes in vivo by the Cancer Chemoprotective Agent, 3H-1, 2-Dithiole-3-thione
    • M.K. Kwak, K. Itoh, M. Yamamoto, T.R. Sutter, and T.W. Kensler Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione Mol Med 7 2001 135 145 (Pubitemid 33702029)
    • (2001) Molecular Medicine , vol.7 , Issue.2 , pp. 135-145
    • Kwak, M.-K.1    Itoh, K.2    Yamamoto, M.3    Sutter, T.R.4    Kensler, T.W.5
  • 37
    • 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
    • DOI 10.1074/jbc.M207293200
    • T. Nguyen, P.J. Sherratt, H.C. Huang, C.S. Yang, and C.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 (Pubitemid 36800950)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.-C.3    Yang, C.S.4    Pickett, C.B.5
  • 38
    • 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
    • DOI 10.1128/MCB.22.9.2883-2892.2002
    • 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 (Pubitemid 34437448)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.9 , pp. 2883-2892
    • Kwak, M.-K.1    Itoh, K.2    Yamamoto, M.3    Kensler, T.W.4
  • 39
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • DOI 10.1042/BJ20031049
    • A.L. Levonen, A. Landar, A. Ramachandran, E.K. Ceaser, D.A. Dickinson, and G. Zanoni Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products Biochem J 378 2004 373 382 (Pubitemid 38367228)
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 373-382
    • Levonen, A.-L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 40
    • 71449099635 scopus 로고    scopus 로고
    • Antioxidant-induced modification of INrf2 cysteine 151 and PKC-delta-mediated phosphorylation of Nrf2 serine 40 are both required for stabilization and nuclear translocation of Nrf2 and increased drug resistance
    • S.K. Niture, A.K. Jain, and A.K. Jaiswal Antioxidant-induced modification of INrf2 cysteine 151 and PKC-delta-mediated phosphorylation of Nrf2 serine 40 are both required for stabilization and nuclear translocation of Nrf2 and increased drug resistance J Cell Sci 122 2009 4452 4464
    • (2009) J Cell Sci , vol.122 , pp. 4452-4464
    • Niture, S.K.1    Jain, A.K.2    Jaiswal, A.K.3
  • 41
    • 68749091158 scopus 로고    scopus 로고
    • Cul3-mediated Nrf2 ubiquitination and antioxidant response element (ARE) activation are dependent on the partial molar volume at position 151 of Keap1
    • A.L. Eggler, E. Small, M. Hannink, and A.D. Mesecar Cul3-mediated Nrf2 ubiquitination and antioxidant response element (ARE) activation are dependent on the partial molar volume at position 151 of Keap1 Biochem J 422 2009 171 180
    • (2009) Biochem J , vol.422 , pp. 171-180
    • Eggler, A.L.1    Small, E.2    Hannink, M.3    Mesecar, A.D.4
  • 43
    • 41849146057 scopus 로고    scopus 로고
    • Covalent modification at Cys151 dissociates the electrophile sensor Keap1 from the ubiquitin ligase CUL3
    • DOI 10.1021/tx700302s
    • G. Rachakonda, Y. Xiong, K.R. Sekhar, S.L. Stamer, D.C. Liebler, and M.L. Freeman Covalent modification at Cys151 dissociates the electrophile sensor Keap1 from the ubiquitin ligase CUL3 Chem Res Toxicol 21 2008 705 710 (Pubitemid 351498046)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.3 , pp. 705-710
    • Rachakonda, G.1    Xiong, Y.2    Sekhar, K.R.3    Stamer, S.L.4    Liebler, D.C.5    Freeman, M.L.6
  • 44
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • DOI 10.1074/jbc.M501279200
    • D.D. Zhang, S.C. Lo, Z. Sun, G.M. Habib, M.W. Lieberman, and M. Hannink Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway J Biol Chem 280 2005 30091 30099 (Pubitemid 41216185)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30091-30099
    • Zhang, D.D.1    Lo, S.-C.2    Sun, Z.3    Habib, G.M.4    Lieberman, M.W.5    Hannink, M.6
  • 45
    • 25444449520 scopus 로고    scopus 로고
    • Nrf2 controls constitutive and inducible expression of ARE-driven genes through a dynamic pathway involving nucleocytoplasmic shuttling by Keap1
    • DOI 10.1074/jbc.M503074200
    • T. Nguyen, P.J. Sherratt, P. Nioi, C.S. Yang, and C.B. Pickett Nrf2 controls constitutive and inducible expression of ARE-driven genes through a dynamic pathway involving nucleocytoplasmic shuttling by Keap1 J Biol Chem 280 2005 32485 32492 (Pubitemid 41361861)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32485-32492
    • Nguyen, T.1    Sherratt, P.J.2    Nioi, P.3    Yang, C.S.4    Pickett, C.B.5
  • 46
    • 34548772935 scopus 로고    scopus 로고
    • Keap1 controls postinduction repression of the Nrf2-mediated antioxidant response by escorting nuclear export of Nrf2
    • DOI 10.1128/MCB.00630-07
    • Z. Sun, S. Zhang, J.Y. Chan, and D.D. Zhang Keap1 controls postinduction repression of the Nrf2-mediated antioxidant response by escorting nuclear export of Nrf2 Mol Cell Biol 27 2007 6334 6349 (Pubitemid 47435741)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.18 , pp. 6334-6349
    • Sun, Z.1    Zhang, S.2    Chan, J.Y.3    Zhang, D.D.4
  • 48
    • 34249934085 scopus 로고    scopus 로고
    • Selective degradation of mitochondria by mitophagy
    • DOI 10.1016/j.abb.2007.03.034, PII S0003986107001622, Highlight Issue: Pro- and antiapoptotic Signalling
    • I. Kim, S. Rodriguez-Enriquez, and J.J. Lemasters Selective degradation of mitochondria by mitophagy Arch Biochem Biophys 462 2007 245 253 (Pubitemid 46876640)
    • (2007) Archives of Biochemistry and Biophysics , vol.462 , Issue.2 , pp. 245-253
    • Kim, I.1    Rodriguez-Enriquez, S.2    Lemasters, J.J.3
  • 50
    • 33745357459 scopus 로고    scopus 로고
    • Autophagy as an immune defense mechanism
    • DOI 10.1016/j.coi.2006.05.019, PII S095279150600094X
    • V. Deretic Autophagy as an immune defense mechanism Curr Opin Immunol 18 2006 375 382 (Pubitemid 43947574)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.4 , pp. 375-382
    • Deretic, V.1
  • 51
    • 34047179973 scopus 로고    scopus 로고
    • Ubiquitinated-protein aggregates form in pancreatic β-cells during diabetes-induced oxidative stress and are regulated by autophagy
    • DOI 10.2337/db06-1160
    • N.A. Kaniuk, M. Kiraly, H. Bates, M. Vranic, A. Volchuk, and J.H. Brumell Ubiquitinated-protein aggregates form in pancreatic beta-cells during diabetes-induced oxidative stress and are regulated by autophagy Diabetes 56 2007 930 939 (Pubitemid 46525060)
    • (2007) Diabetes , vol.56 , Issue.4 , pp. 930-939
    • Kaniuk, N.A.1    Kiraly, M.2    Bates, H.3    Vranic, M.4    Volchuk, A.5    Brumell, J.H.6
  • 52
    • 58549084167 scopus 로고    scopus 로고
    • Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
    • P.K. Kim, D.W. Hailey, R.T. Mullen, and J. Lippincott-Schwartz Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes Proc Natl Acad Sci USA 105 2008 20567 20574
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20567-20574
    • Kim, P.K.1    Hailey, D.W.2    Mullen, R.T.3    Lippincott-Schwartz, J.4
  • 54
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • M. Komatsu, H. Kurokawa, S. Waguri, K. Taguchi, A. Kobayashi, and Y. Ichimura The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1 Nat Cell Biol 12 2010 213 223
    • (2010) Nat Cell Biol , vol.12 , pp. 213-223
    • Komatsu, M.1    Kurokawa, H.2    Waguri, S.3    Taguchi, K.4    Kobayashi, A.5    Ichimura, Y.6
  • 55
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between keap1 and p62
    • A. Lau, X.J. Wang, F. Zhao, N.F. Villeneuve, T. Wu, and T. Jiang A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between keap1 and p62 Mol Cell Biol 30 2010 3275 3285
    • (2010) Mol Cell Biol , vol.30 , pp. 3275-3285
    • Lau, A.1    Wang, X.J.2    Zhao, F.3    Villeneuve, N.F.4    Wu, T.5    Jiang, T.6
  • 56
    • 77954599053 scopus 로고    scopus 로고
    • P62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • A. Jain, T. Lamark, E. Sjøttem, K.B. Larsen, J.A. Awuh, and A. Øvervatn p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription J Biol Chem 285 2010 22576 22591
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjøttem, E.3    Larsen, K.B.4    Awuh, J.A.5    Øvervatn, A.6
  • 57
    • 77955352128 scopus 로고    scopus 로고
    • Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy
    • W. Fan, Z. Tang, D. Chen, D. Moughon, X. Ding, and S. Chen Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy Autophagy 6 2010 614 621
    • (2010) Autophagy , vol.6 , pp. 614-621
    • Fan, W.1    Tang, Z.2    Chen, D.3    Moughon, D.4    Ding, X.5    Chen, S.6
  • 58
    • 77952781968 scopus 로고    scopus 로고
    • Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway
    • I.M. Copple, A. Lister, A.D. Obeng, N.R. Kitteringham, R.E. Jenkins, and R. Layfield Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway J Biol Chem 285 2010 16782 16788
    • (2010) J Biol Chem , vol.285 , pp. 16782-16788
    • Copple, I.M.1    Lister, A.2    Obeng, A.D.3    Kitteringham, N.R.4    Jenkins, R.E.5    Layfield, R.6
  • 59
    • 79955492012 scopus 로고    scopus 로고
    • Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells
    • Y. Inami, S. Waguri, A. Sakamoto, T. Kouno, K. Nakada, and O. Hino Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells J Cell Biol 193 2011 275 284
    • (2011) J Cell Biol , vol.193 , pp. 275-284
    • Inami, Y.1    Waguri, S.2    Sakamoto, A.3    Kouno, T.4    Nakada, K.5    Hino, O.6
  • 60
    • 0033861403 scopus 로고    scopus 로고
    • Relationship between the occurrence of cysteine in proteins and the complexity of organisms
    • A. Miseta, and P. Csutora Relationship between the occurrence of cysteine in proteins and the complexity of organisms Mol Biol Evol 17 2000 1232 1239 (Pubitemid 30617150)
    • (2000) Molecular Biology and Evolution , vol.17 , Issue.8 , pp. 1232-1239
    • Miseta, A.1    Csutora, P.2
  • 61
    • 84856834259 scopus 로고    scopus 로고
    • Analysis and functional prediction of reactive cysteine residues
    • S.M. Marino, and V.N. Gladyshev Analysis and functional prediction of reactive cysteine residues J Biol Chem 287 2012 4419 4425
    • (2012) J Biol Chem , vol.287 , pp. 4419-4425
    • Marino, S.M.1    Gladyshev, V.N.2
  • 62
    • 77958122499 scopus 로고    scopus 로고
    • Chemistry of the cysteine sensors in Kelch-like ECH-associated protein 1
    • R. Holland, and J.C. Fishbein Chemistry of the cysteine sensors in Kelch-like ECH-associated protein 1 Antioxid Redox Signal 13 2010 1749 1761
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1749-1761
    • Holland, R.1    Fishbein, J.C.2
  • 63
    • 0019877708 scopus 로고
    • Electrostatic influence of local cysteine environments on disulfide exchange kinetics
    • G.H. Snyder, M.J. Cennerazzo, A.J. Karalis, and D. Field Electrostatic influence of local cysteine environments on disulfide exchange kinetics Biochemistry 20 1981 6509 6519
    • (1981) Biochemistry , vol.20 , pp. 6509-6519
    • Snyder, G.H.1    Cennerazzo, M.J.2    Karalis, A.J.3    Field, D.4
  • 67
    • 58249117780 scopus 로고    scopus 로고
    • The antioxidant defense system Keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds
    • M. Kobayashi, L. Li, N. Iwamoto, Y. Nakajima-Takagi, H. Kaneko, and Y. Nakayama The antioxidant defense system Keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds Mol Cell Biol 29 2009 493 502
    • (2009) Mol Cell Biol , vol.29 , pp. 493-502
    • Kobayashi, M.1    Li, L.2    Iwamoto, N.3    Nakajima-Takagi, Y.4    Kaneko, H.5    Nakayama, Y.6
  • 70
    • 78650509515 scopus 로고    scopus 로고
    • Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals
    • M. McMahon, D.J. Lamont, K.A. Beattie, and J.D. Hayes Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals Proc Natl Acad Sci USA 107 2010 18838 18843
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18838-18843
    • McMahon, M.1    Lamont, D.J.2    Beattie, K.A.3    Hayes, J.D.4
  • 71
    • 77954947797 scopus 로고    scopus 로고
    • The critical role of nitric oxide signaling, via protein S-guanylation and nitrated cyclic GMP, in the antioxidant adaptive response
    • S. Fujii, T. Sawa, H. Ihara, K.I. Tong, T. Ida, and T. Okamoto The critical role of nitric oxide signaling, via protein S-guanylation and nitrated cyclic GMP, in the antioxidant adaptive response J Biol Chem 285 2010 23970 23984
    • (2010) J Biol Chem , vol.285 , pp. 23970-23984
    • Fujii, S.1    Sawa, T.2    Ihara, H.3    Tong, K.I.4    Ida, T.5    Okamoto, T.6
  • 72
    • 80051548161 scopus 로고    scopus 로고
    • Nitric oxide activates Nrf2 through S-nitrosylation of Keap1 in PC12 cells
    • H.C. Um, J.H. Jang, D.H. Kim, C. Lee, and Y.J. Surh Nitric oxide activates Nrf2 through S-nitrosylation of Keap1 in PC12 cells Nitric Oxide 25 2011 161 168
    • (2011) Nitric Oxide , vol.25 , pp. 161-168
    • Um, H.C.1    Jang, J.H.2    Kim, D.H.3    Lee, C.4    Surh, Y.J.5
  • 73
    • 77953357236 scopus 로고    scopus 로고
    • Differential effect of covalent protein modification and glutathione depletion on the transcriptional response of Nrf2 and NF-kappaB
    • A.J. Chia, C.E. Goldring, N.R. Kitteringham, S.Q. Wong, P. Morgan, and B.K. Park Differential effect of covalent protein modification and glutathione depletion on the transcriptional response of Nrf2 and NF-kappaB Biochem Pharmacol 80 2010 410 421
    • (2010) Biochem Pharmacol , vol.80 , pp. 410-421
    • Chia, A.J.1    Goldring, C.E.2    Kitteringham, N.R.3    Wong, S.Q.4    Morgan, P.5    Park, B.K.6
  • 74
    • 54449093352 scopus 로고    scopus 로고
    • The hepatotoxic metabolite of acetaminophen directly activates the Keap1-Nrf2 cell defense system
    • I.M. Copple, C.E. Goldring, R.E. Jenkins, A.J. Chia, L.E. Randle, and J.D. Hayes The hepatotoxic metabolite of acetaminophen directly activates the Keap1-Nrf2 cell defense system Hepatology 48 2008 1292 1301
    • (2008) Hepatology , vol.48 , pp. 1292-1301
    • Copple, I.M.1    Goldring, C.E.2    Jenkins, R.E.3    Chia, A.J.4    Randle, L.E.5    Hayes, J.D.6
  • 75
    • 0036783335 scopus 로고    scopus 로고
    • Pharmacogenomics, regulation and signaling pathways of phase I and II drug metabolizing enzymes
    • DOI 10.2174/1389200023337171
    • T.H. Rushmore, and A.N. Kong Pharmacogenomics, regulation and signaling pathways of phase I and II drug metabolizing enzymes Curr Drug Metab 3 2002 481 490 (Pubitemid 34987481)
    • (2002) Current Drug Metabolism , vol.3 , Issue.5 , pp. 481-490
    • Rushmore, T.H.1    Kong, A.-N.T.2
  • 76
    • 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 C.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, C.B.4
  • 79
    • 56349163056 scopus 로고    scopus 로고
    • The susceptibility to vitiligo is associated with NF-E2-related factor2 (Nrf2) gene polymorphisms: A study on Chinese Han population
    • C.P. Guan, M.N. Zhou, A.E. Xu, K.F. Kang, J.F. Liu, and X.D. Wei The susceptibility to vitiligo is associated with NF-E2-related factor2 (Nrf2) gene polymorphisms: a study on Chinese Han population Exp Dermatol 17 2008 1059 1062
    • (2008) Exp Dermatol , vol.17 , pp. 1059-1062
    • Guan, C.P.1    Zhou, M.N.2    Xu, A.E.3    Kang, K.F.4    Liu, J.F.5    Wei, X.D.6
  • 80
    • 57449111441 scopus 로고    scopus 로고
    • Regulatory potential for concerted modulation of Nrf2- and Nfkb1-mediated gene expression in inflammation and carcinogenesis
    • S. Nair, S.T. Doh, J.Y. Chan, A.N. Kong, and L. Cai Regulatory potential for concerted modulation of Nrf2- and Nfkb1-mediated gene expression in inflammation and carcinogenesis Br J Cancer 99 2008 2070 2082
    • (2008) Br J Cancer , vol.99 , pp. 2070-2082
    • Nair, S.1    Doh, S.T.2    Chan, J.Y.3    Kong, A.N.4    Cai, L.5
  • 81
    • 77955653742 scopus 로고    scopus 로고
    • Suppression of NF-kappaB signaling by KEAP1 regulation of IKKbeta activity through autophagic degradation and inhibition of phosphorylation
    • J.E. Kim, D.J. You, C. Lee, C. Ahn, J.Y. Seong, and J.I. Hwang Suppression of NF-kappaB signaling by KEAP1 regulation of IKKbeta activity through autophagic degradation and inhibition of phosphorylation Cell Signal 22 2010 1645 1654
    • (2010) Cell Signal , vol.22 , pp. 1645-1654
    • Kim, J.E.1    You, D.J.2    Lee, C.3    Ahn, C.4    Seong, J.Y.5    Hwang, J.I.6
  • 82
    • 70349970493 scopus 로고    scopus 로고
    • KEAP1 E3 ligase-mediated downregulation of NF-kappaB signaling by targeting IKKbeta
    • D.F. Lee, H.P. Kuo, M. Liu, C.K. Chou, W. Xia, and Y. Du KEAP1 E3 ligase-mediated downregulation of NF-kappaB signaling by targeting IKKbeta Mol Cell 36 2009 131 140
    • (2009) Mol Cell , vol.36 , pp. 131-140
    • Lee, D.F.1    Kuo, H.P.2    Liu, M.3    Chou, C.K.4    Xia, W.5    Du, Y.6
  • 83
    • 80052570740 scopus 로고    scopus 로고
    • MiR-28 regulates Nrf2 expression through a Keap1-independent mechanism
    • M. Yang, Y. Yao, G. Eades, Y. Zhang, and Q. Zhou MiR-28 regulates Nrf2 expression through a Keap1-independent mechanism Breast Cancer Res Treat 129 2011 983 991
    • (2011) Breast Cancer Res Treat , vol.129 , pp. 983-991
    • Yang, M.1    Yao, Y.2    Eades, G.3    Zhang, Y.4    Zhou, Q.5
  • 84
    • 78549277802 scopus 로고    scopus 로고
    • Chi JT. microRNA miR-144 modulates oxidative stress tolerance and associates with anemia severity in sickle cell disease
    • C. Sangokoya, and M.J. Telen Chi JT. microRNA miR-144 modulates oxidative stress tolerance and associates with anemia severity in sickle cell disease Blood 116 2010 4338 4348
    • (2010) Blood , vol.116 , pp. 4338-4348
    • Sangokoya, C.1    Telen, M.J.2
  • 85
    • 81755171451 scopus 로고    scopus 로고
    • MiR-200a regulates Nrf2 activation by targeting Keap1 mRNA in breast cancer cells
    • G. Eades, M. Yang, Y. Yao, Y. Zhang, and Q. Zhou miR-200a regulates Nrf2 activation by targeting Keap1 mRNA in breast cancer cells J Biol Chem 286 2011 40725 40733
    • (2011) J Biol Chem , vol.286 , pp. 40725-40733
    • Eades, G.1    Yang, M.2    Yao, Y.3    Zhang, Y.4    Zhou, Q.5
  • 86
    • 79952742806 scopus 로고    scopus 로고
    • Increased expression of miR-34a and miR-93 in rat liver during aging, and their impact on the expression of Mgst1 and Sirt1
    • N. Li, S. Muthusamy, R. Liang, H. Sarojini, and E. Wang Increased expression of miR-34a and miR-93 in rat liver during aging, and their impact on the expression of Mgst1 and Sirt1 Mech Ageing Dev 132 2011 75 85
    • (2011) Mech Ageing Dev , vol.132 , pp. 75-85
    • Li, N.1    Muthusamy, S.2    Liang, R.3    Sarojini, H.4    Wang, E.5
  • 87
    • 38349169664 scopus 로고    scopus 로고
    • Mechanisms of post-transcriptional regulation by microRNAs: Are the answers in sight
    • W. Filipowicz, S.N. Bhattacharyya, and N. Sonenberg Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight Nat Rev Genet 9 2008 102 114
    • (2008) Nat Rev Genet , vol.9 , pp. 102-114
    • Filipowicz, W.1    Bhattacharyya, S.N.2    Sonenberg, N.3
  • 88
    • 84855458875 scopus 로고    scopus 로고
    • Signaling pathways activated by the phytochemical nordihydroguaiaretic acid contribute to a Keap1-independent regulation of Nrf2 stability: Role of glycogen synthase kinase-3
    • A.I. Rojo, O.N. Medina-Campos, P. Rada, A. Zuniga-Toala, A. Lopez-Gazcon, and S. Espada Signaling pathways activated by the phytochemical nordihydroguaiaretic acid contribute to a Keap1-independent regulation of Nrf2 stability: role of glycogen synthase kinase-3 Free Radic Biol Med 52 2012 473 487
    • (2012) Free Radic Biol Med , vol.52 , pp. 473-487
    • Rojo, A.I.1    Medina-Campos, O.N.2    Rada, P.3    Zuniga-Toala, A.4    Lopez-Gazcon, A.5    Espada, S.6
  • 89
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • DOI 10.1074/jbc.M206911200
    • H.C. Huang, T. Nguyen, and C.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 (Pubitemid 35285650)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42769-42774
    • Huang, H.-C.1    Nguyen, T.2    Pickett, C.B.3
  • 90
    • 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
  • 91
    • 0242666198 scopus 로고    scopus 로고
    • 40 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
    • DOI 10.1074/jbc.M307633200
    • D.A. Bloom, and A.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 (Pubitemid 37377224)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44675-44682
    • Bloom, D.A.1    Jaiswal, A.K.2
  • 92
    • 44049093741 scopus 로고    scopus 로고
    • Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2
    • M. Theodore, Y. Kawai, J. Yang, Y. Kleshchenko, S.P. Reddy, and F. Villalta Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2 J Biol Chem 283 2008 8984 8994
    • (2008) J Biol Chem , vol.283 , pp. 8984-8994
    • Theodore, M.1    Kawai, Y.2    Yang, J.3    Kleshchenko, Y.4    Reddy, S.P.5    Villalta, F.6
  • 94
    • 40549121572 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 in the transcription activation domain by casein kinase 2 (CK2) is critical for the nuclear translocation and transcription activation function of Nrf2 in IMR-32 neuroblastoma cells
    • DOI 10.1002/jbt.20212
    • P.L. Apopa, X. He, and Q. Ma Phosphorylation of Nrf2 in the transcription activation domain by casein kinase 2 (CK2) is critical for the nuclear translocation and transcription activation function of Nrf2 in IMR-32 neuroblastoma cells J Biochem Mol Toxicol 22 2008 63 76 (Pubitemid 351360163)
    • (2008) Journal of Biochemical and Molecular Toxicology , vol.22 , Issue.1 , pp. 63-76
    • Apopa, P.L.1    He, X.2    Ma, Q.3
  • 95
    • 33744953050 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 568 controls nuclear export of Nrf2
    • DOI 10.1074/jbc.M511198200
    • A.K. Jain, and A.K. Jaiswal Phosphorylation of tyrosine 568 controls nuclear export of Nrf2 J Biol Chem 281 2006 12132 12142 (Pubitemid 43855477)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 12132-12142
    • Jain, A.K.1    Jaiswal, A.K.2
  • 96
    • 34447526197 scopus 로고    scopus 로고
    • GSK-3β acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2
    • DOI 10.1074/jbc.M611336200
    • A.K. Jain, and A.K. Jaiswal GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2 J Biol Chem 282 2007 16502 16510 (Pubitemid 47100395)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.22 , pp. 16502-16510
    • Jain, A.K.1    Jaiswal, A.K.2
  • 97
    • 33749019130 scopus 로고    scopus 로고
    • Mechanism of action of sulforaphane: Inhibition of p38 mitogen-activated protein kinase isoforms contributing to the induction of antioxidant response element-mediated heme oxygenase-1 in human hepatoma HepG2 cells
    • DOI 10.1158/0008-5472.CAN-05-3513
    • Y.S. Keum, S. Yu, P.P. Chang, X. Yuan, J.H. Kim, and C. Xu Mechanism of action of sulforaphane: inhibition of p38 mitogen-activated protein kinase isoforms contributing to the induction of antioxidant response element-mediated heme oxygenase-1 in human hepatoma HepG2 cells Cancer Res 66 2006 8804 8813 (Pubitemid 44449198)
    • (2006) Cancer Research , vol.66 , Issue.17 , pp. 8804-8813
    • Keum, Y.-S.1    Yu, S.2    Chang, P.P.-J.3    Yuan, X.4    Kim, J.-H.5    Xu, C.6    Han, J.7    Agarwal, A.8    Kong, A.-N.T.9
  • 98
    • 33750430654 scopus 로고    scopus 로고
    • Butylated hydroxyanisole regulates ARE-mediated gene expression via Nrf2 coupled with ERK and JNK signaling pathway in HepG2 cells
    • DOI 10.1002/mc.20234
    • X. Yuan, C. Xu, Z. Pan, Y.S. Keum, J.H. Kim, and G. Shen Butylated hydroxyanisole regulates ARE-mediated gene expression via Nrf2 coupled with ERK and JNK signaling pathway in HepG2 cells Mol Carcinog 45 2006 841 850 (Pubitemid 44646336)
    • (2006) Molecular Carcinogenesis , vol.45 , Issue.11 , pp. 841-850
    • Yuan, X.1    Xu, C.2    Pan, Z.3    Keum, Y.-S.4    Kim, J.-H.5    Shen, G.6    Yu, S.7    Oo, K.T.8    Ma, J.9    Kong, A.-N.T.10
  • 100
    • 33744950387 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2
    • DOI 10.1074/jbc.M513737200
    • M. Salazar, A.I. Rojo, D. Velasco, R.M. de Sagarra, and A. Cuadrado Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2 J Biol Chem 281 2006 14841 14851 (Pubitemid 43855189)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14841-14851
    • Salazar, M.1    Rojo, A.I.2    Velasco, D.3    De Sagarra, R.M.4    Cuadrado, A.5
  • 101
    • 79952256187 scopus 로고    scopus 로고
    • SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner
    • P. Rada, A.I. Rojo, S. Chowdhry, M. McMahon, J.D. Hayes, and A. Cuadrado SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner Mol Cell Biol 31 2011 1121 1133
    • (2011) Mol Cell Biol , vol.31 , pp. 1121-1133
    • Rada, P.1    Rojo, A.I.2    Chowdhry, S.3    McMahon, M.4    Hayes, J.D.5    Cuadrado, A.6
  • 102
  • 103
    • 0034671768 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation
    • DOI 10.1101/gad.854900
    • J.R. Alt, J.L. Cleveland, M. Hannink, and J.A. Diehl Phosphorylation- dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation Genes Dev 14 2000 3102 3114 (Pubitemid 32015129)
    • (2000) Genes and Development , vol.14 , Issue.24 , pp. 3102-3114
    • Alt, J.R.1    Cleveland, J.L.2    Hannink, M.3    Diehl, J.A.4
  • 104
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • DOI 10.1016/S0092-8674(00)82001-2
    • V.V. Ogryzko, R.L. Schiltz, V. Russanova, B.H. Howard, and Y. Nakatani The transcriptional coactivators p300 and CBP are histone acetyltransferases Cell 87 1996 953 959 (Pubitemid 26404293)
    • (1996) Cell , vol.87 , Issue.5 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 106
    • 66349129338 scopus 로고    scopus 로고
    • Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response
    • Z. Sun, Y.E. Chin, and D.D. Zhang Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response Mol Cell Biol 29 2009 2658 2672
    • (2009) Mol Cell Biol , vol.29 , pp. 2658-2672
    • Sun, Z.1    Chin, Y.E.2    Zhang, D.D.3
  • 107
    • 0034752461 scopus 로고    scopus 로고
    • Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription
    • DOI 10.1046/j.1365-2443.2001.00469.x
    • 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 (Pubitemid 33019739)
    • (2001) Genes to Cells , vol.6 , Issue.10 , pp. 857-868
    • Katoh, Y.1    Itoh, K.2    Yoshida, E.3    Miyagishi, M.4    Fukamizu, A.5    Yamamoto, M.6
  • 108
    • 84861911235 scopus 로고    scopus 로고
    • Interaction with CREB binding protein modulates the activities of Nrf2 and NF-kappaB in cystic fibrosis airway epithelial cells
    • A.G. Ziady, A. Sokolow, S. Shank, D. Corey, R. Myers, and S. Plafker Interaction with CREB binding protein modulates the activities of Nrf2 and NF-kappaB in cystic fibrosis airway epithelial cells Am J Physiol Lung Cell Mol Physiol 302 2012 L1221 L1231
    • (2012) Am J Physiol Lung Cell Mol Physiol , vol.302
    • Ziady, A.G.1    Sokolow, A.2    Shank, S.3    Corey, D.4    Myers, R.5    Plafker, S.6
  • 109
    • 45549091466 scopus 로고    scopus 로고
    • BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase
    • P. Rondou, G. Haegeman, P. Vanhoenacker, and K. Van Craenenbroeck BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase J Biol Chem 283 2008 11083 11096
    • (2008) J Biol Chem , vol.283 , pp. 11083-11096
    • Rondou, P.1    Haegeman, G.2    Vanhoenacker, P.3    Van Craenenbroeck, K.4
  • 111
    • 77949550917 scopus 로고    scopus 로고
    • Keap1-Nrf2 activation in the presence and absence of DJ-1
    • L. Gan, D.A. Johnson, and J.A. Johnson Keap1-Nrf2 activation in the presence and absence of DJ-1 Eur J Neurosci 31 2010 967 977
    • (2010) Eur J Neurosci , vol.31 , pp. 967-977
    • Gan, L.1    Johnson, D.A.2    Johnson, J.A.3
  • 112
    • 67449128222 scopus 로고    scopus 로고
    • Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response
    • W. Chen, Z. Sun, X.J. Wang, T. Jiang, Z. Huang, and D. Fang Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response Mol Cell 34 2009 663 673
    • (2009) Mol Cell , vol.34 , pp. 663-673
    • Chen, W.1    Sun, Z.2    Wang, X.J.3    Jiang, T.4    Huang, Z.5    Fang, D.6
  • 113
    • 84862280943 scopus 로고    scopus 로고
    • Caveolin-1 inhibits expression of antioxidant enzymes through direct interaction with nuclear erythroid 2 p45-related factor-2 (Nrf2)
    • W. Li, H. Liu, J.S. Zhou, J.F. Cao, X.B. Zhou, and A.M. Choi Caveolin-1 inhibits expression of antioxidant enzymes through direct interaction with nuclear erythroid 2 p45-related factor-2 (Nrf2) J Biol Chem 287 2012 20922 20930
    • (2012) J Biol Chem , vol.287 , pp. 20922-20930
    • Li, W.1    Liu, H.2    Zhou, J.S.3    Cao, J.F.4    Zhou, X.B.5    Choi, A.M.6
  • 114
    • 84855478994 scopus 로고    scopus 로고
    • Epigallocatechin-gallate stimulates NF-E2-related factor and heme oxygenase-1 via caveolin-1 displacement
    • Y. Zheng, A. Morris, M. Sunkara, J. Layne, M. Toborek, and B. Hennig Epigallocatechin-gallate stimulates NF-E2-related factor and heme oxygenase-1 via caveolin-1 displacement J Nutr Biochem 23 2012 163 168
    • (2012) J Nutr Biochem , vol.23 , pp. 163-168
    • Zheng, Y.1    Morris, A.2    Sunkara, M.3    Layne, J.4    Toborek, M.5    Hennig, B.6
  • 115
    • 33748752586 scopus 로고    scopus 로고
    • Nrf2 possesses a redox-sensitive nuclear exporting signal in the Neh5 transactivation domain
    • DOI 10.1074/jbc.M602746200
    • W. Li, S.W. Yu, and A.N. Kong Nrf2 possesses a redox-sensitive nuclear exporting signal in the Neh5 transactivation domain J Biol Chem 281 2006 27251 27263 (Pubitemid 44401754)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 27251-27263
    • Li, W.1    Yu, S.-W.2    Kong, A.-N.T.3
  • 117
    • 84862494503 scopus 로고    scopus 로고
    • The NRF2-related interactome and regulome contain multifunctional proteins and fine-tuned autoregulatory loops
    • D. Papp, K. Lenti, D. Modos, D. Fazekas, Z. Dul, and D. Turei The NRF2-related interactome and regulome contain multifunctional proteins and fine-tuned autoregulatory loops FEBS Lett 586 2012 1795 1802
    • (2012) FEBS Lett , vol.586 , pp. 1795-1802
    • Papp, D.1    Lenti, K.2    Modos, D.3    Fazekas, D.4    Dul, Z.5    Turei, D.6
  • 118
    • 66449114033 scopus 로고    scopus 로고
    • P62 at the crossroads of autophagy, apoptosis, and cancer
    • J. Moscat, and M.T. Diaz-Meco p62 at the crossroads of autophagy, apoptosis, and cancer Cell 137 2009 1001 1004
    • (2009) Cell , vol.137 , pp. 1001-1004
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 121
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation
    • DOI 10.1074/jbc.M503346200
    • F. Hong, K.R. Sekhar, M.L. Freeman, and D.C. Liebler Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation J Biol Chem 280 2005 31768 31775 (Pubitemid 41291926)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.E.2    Freeman, M.L.3    Liebler, D.C.4
  • 123
    • 36349019109 scopus 로고    scopus 로고
    • Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent
    • A.L. Eggler, Y. Luo, R.B. van Breemen, and A.D. Mesecar Identification of the highly reactive cysteine 151 in the chemopreventive agent-sensor Keap1 protein is method-dependent Chem Res Toxicol 20 2007 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
  • 124
    • 29644443964 scopus 로고    scopus 로고
    • Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane
    • DOI 10.1021/tx0502138
    • F. Hong, M.L. Freeman, and D.C. Liebler Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane Chem Res Toxicol 18 2005 1917 1926 (Pubitemid 43023050)
    • (2005) Chemical Research in Toxicology , vol.18 , Issue.12 , pp. 1917-1926
    • Hong, F.1    Freeman, M.L.2    Liebler, D.C.3
  • 125
    • 76449118748 scopus 로고    scopus 로고
    • Chapter 3: Site-specific modification of the electrophile sensor protein Keap1 and activation of Nrf2-dependent gene expression
    • D.C. Liebler, F. Hong, K.R. Sekhar, M.L. Freeman, and C.F. James Chapter 3: Site-specific modification of the electrophile sensor protein Keap1 and activation of Nrf2-dependent gene expression Adv Mol Toxicol 1 2006 65 83
    • (2006) Adv Mol Toxicol , vol.1 , pp. 65-83
    • Liebler, D.C.1    Hong, F.2    Sekhar, K.R.3    Freeman, M.L.4    James, C.F.5
  • 126
    • 55949128500 scopus 로고    scopus 로고
    • Angelica sinensis and its alkylphthalides induce the detoxification enzyme NAD(P)H: Quinone oxidoreductase 1 by alkylating Keap1
    • B.M. Dietz, D. Liu, G.K. Hagos, P. Yao, A. Schinkovitz, and S.M. Pro Angelica sinensis and its alkylphthalides induce the detoxification enzyme NAD(P)H: quinone oxidoreductase 1 by alkylating Keap1 Chem Res Toxicol 21 2008 1939 1948
    • (2008) Chem Res Toxicol , vol.21 , pp. 1939-1948
    • Dietz, B.M.1    Liu, D.2    Hagos, G.K.3    Yao, P.4    Schinkovitz, A.5    Pro, S.M.6


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