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Volumn 39, Issue 4, 2014, Pages 199-218

The Nrf2 regulatory network provides an interface between redox and intermediary metabolism

Author keywords

Fatty acid oxidation; Glutathione; GSK 3; Keap1; NADPH; Nrf2; Oxidative stress; Pentose phosphate pathway; Purine synthesis; Thioredoxin; TrCP

Indexed keywords

CR6 INTERACTING FACTOR 1; GLYCOGEN SYNTHASE KINASE 3BETA; KELCH LIKE ECH ASSOCIATED PROTEIN 1; MICRORNA; PENTOSE PHOSPHATE; PROTEASOME; PURINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REGULATOR PROTEIN; RING FINGER PROTEIN; RING FINGER PROTEIN 4; SEVEN IN ABSENTIA HOMOLOG 2 PROTEIN; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; BRCA1 PROTEIN; GLUTAMINE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; GLYCOGEN SYNTHASE KINASE 3; LIPID;

EID: 84897421970     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2014.02.002     Document Type: Review
Times cited : (1594)

References (176)
  • 1
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
    • Hayes J.D., McMahon M. NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends Biochem. Sci. 2009, 34:176-188.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 2
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • Moi P., et al. Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:9926-9930.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9926-9930
    • Moi, P.1
  • 3
    • 77953012548 scopus 로고    scopus 로고
    • Stress-activated cap'n'collar transcription factors in aging and human disease
    • Sykiotis G.P., Bohmann D. Stress-activated cap'n'collar transcription factors in aging and human disease. Sci. Signal. 2010, 3:re3.
    • (2010) Sci. Signal. , vol.3
    • Sykiotis, G.P.1    Bohmann, D.2
  • 4
    • 80054762424 scopus 로고    scopus 로고
    • NFE2L3 (NRF3): the Cinderella of the Cap'n'Collar transcription factors
    • Chevillard G., Blank V. NFE2L3 (NRF3): the Cinderella of the Cap'n'Collar transcription factors. Cell. Mol. Life Sci. 2011, 68:3337-3348.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 3337-3348
    • Chevillard, G.1    Blank, V.2
  • 5
    • 2342511435 scopus 로고    scopus 로고
    • Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway
    • Motohashi H., et al. Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:6379-6384.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6379-6384
    • Motohashi, H.1
  • 6
    • 0030451213 scopus 로고    scopus 로고
    • NRF2, a member of the NFE2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development
    • Chan K., et al. NRF2, a member of the NFE2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:13943-13948.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13943-13948
    • Chan, K.1
  • 7
    • 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., et al. 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
  • 8
    • 0026571238 scopus 로고
    • Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene
    • Friling R.S., et al. Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:668-672.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 668-672
    • Friling, R.S.1
  • 9
    • 0019142866 scopus 로고
    • Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity
    • Benson A.M., et al. Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity. Proc. Natl. Acad. Sci. U.S.A. 1980, 77:5216-5220.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 5216-5220
    • Benson, A.M.1
  • 11
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • Itoh K., et al. An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem. Biophys. Res. Commun. 1997, 236:313-322.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 313-322
    • Itoh, K.1
  • 12
    • 0037101768 scopus 로고    scopus 로고
    • Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice
    • Chanas S.A., et al. Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice. Biochem. J. 2002, 365:405-416.
    • (2002) Biochem. J. , vol.365 , pp. 405-416
    • Chanas, S.A.1
  • 13
    • 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., et al. 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
  • 14
    • 77957237159 scopus 로고    scopus 로고
    • Global mapping of binding sites for Nrf2 identifies novel targets in cell survival response through ChIP-Seq profiling and network analysis
    • Malhotra D., et al. Global mapping of binding sites for Nrf2 identifies novel targets in cell survival response through ChIP-Seq profiling and network analysis. Nucleic Acids Res. 2010, 38:5718-5734.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 5718-5734
    • Malhotra, D.1
  • 15
    • 84857918033 scopus 로고    scopus 로고
    • Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles
    • Agyeman A.S., et al. Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles. Breast Cancer Res. Treat. 2012, 132:175-187.
    • (2012) Breast Cancer Res. Treat. , vol.132 , pp. 175-187
    • Agyeman, A.S.1
  • 16
    • 84867317004 scopus 로고    scopus 로고
    • Identification of novel NRF2-regulated genes by ChIP-Seq: influence on retinoid X receptor alpha
    • Chorley B.N., et al. Identification of novel NRF2-regulated genes by ChIP-Seq: influence on retinoid X receptor alpha. Nucleic Acids Res. 2012, 40:7416-7429.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 7416-7429
    • Chorley, B.N.1
  • 17
    • 84869076474 scopus 로고    scopus 로고
    • Nrf2-MafG heterodimers contribute globally to antioxidant and metabolic networks
    • Hirotsu Y., et al. Nrf2-MafG heterodimers contribute globally to antioxidant and metabolic networks. Nucleic Acids Res. 2012, 40:10228-10239.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10228-10239
    • Hirotsu, Y.1
  • 18
    • 84867040616 scopus 로고    scopus 로고
    • Mitochondrial SKN-1/Nrf mediates a conserved starvation response
    • Paek J., et al. Mitochondrial SKN-1/Nrf mediates a conserved starvation response. Cell Metab. 2012, 16:526-537.
    • (2012) Cell Metab. , vol.16 , pp. 526-537
    • Paek, J.1
  • 19
    • 84873443918 scopus 로고    scopus 로고
    • Identification of aldo-keto reductases as NRF2-target marker genes in human cells
    • Jung K.A., et al. Identification of aldo-keto reductases as NRF2-target marker genes in human cells. Toxicol. Lett. 2013, 218:39-49.
    • (2013) Toxicol. Lett. , vol.218 , pp. 39-49
    • Jung, K.A.1
  • 20
    • 36349015332 scopus 로고    scopus 로고
    • Oxidative and electrophilic stress induces multidrug resistance-associated protein transporters via the nuclear factor-E2-related factor-2 transcriptional pathway
    • Maher J.M., et al. Oxidative and electrophilic stress induces multidrug resistance-associated protein transporters via the nuclear factor-E2-related factor-2 transcriptional pathway. Hepatology 2007, 46:1597-1610.
    • (2007) Hepatology , vol.46 , pp. 1597-1610
    • Maher, J.M.1
  • 21
    • 66749112860 scopus 로고    scopus 로고
    • Genetic versus chemoprotective activation of Nrf2 signaling: overlapping yet distinct gene expression profiles between Keap1 knockout and triterpenoid-treated mice
    • Yates M.S., et al. Genetic versus chemoprotective activation of Nrf2 signaling: overlapping yet distinct gene expression profiles between Keap1 knockout and triterpenoid-treated mice. Carcinogenesis 2009, 30:1024-1031.
    • (2009) Carcinogenesis , vol.30 , pp. 1024-1031
    • Yates, M.S.1
  • 22
    • 84872191631 scopus 로고    scopus 로고
    • - in health and disease: from molecular mechanisms to novel therapeutic opportunities
    • - in health and disease: from molecular mechanisms to novel therapeutic opportunities. Antioxid. Redox Signal. 2013, 18:522-555.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 522-555
    • Lewerenz, J.1
  • 23
    • 67349247003 scopus 로고    scopus 로고
    • Transcription factor Nrf2 mediates an adaptive response to sulforaphane that protects fibroblasts in vitro against the cytotoxic effects of electrophiles, peroxides and redox-cycling agents
    • Higgins L.G., et al. Transcription factor Nrf2 mediates an adaptive response to sulforaphane that protects fibroblasts in vitro against the cytotoxic effects of electrophiles, peroxides and redox-cycling agents. Toxicol. Appl. Pharmacol. 2009, 237:267-280.
    • (2009) Toxicol. Appl. Pharmacol. , vol.237 , pp. 267-280
    • Higgins, L.G.1
  • 24
    • 84885364275 scopus 로고    scopus 로고
    • Regulation of the human thioredoxin gene promoter and its key substrates: A study of functional and putative regulatory elements
    • Hawkes H.J., et al. Regulation of the human thioredoxin gene promoter and its key substrates: A study of functional and putative regulatory elements. Biochim. Biophys. Acta 2013, 1840:303-314.
    • (2013) Biochim. Biophys. Acta , vol.1840 , pp. 303-314
    • Hawkes, H.J.1
  • 25
    • 79957963156 scopus 로고    scopus 로고
    • Nitric oxide activates an Nrf2/sulfiredoxin antioxidant pathway in macrophages
    • Abbas K., et al. Nitric oxide activates an Nrf2/sulfiredoxin antioxidant pathway in macrophages. Free Radic. Biol. Med. 2011, 51:107-114.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 107-114
    • Abbas, K.1
  • 26
    • 84863463209 scopus 로고    scopus 로고
    • Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression
    • Jeong W., et al. Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression. Free Radic. Biol. Med. 2012, 53:447-456.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 447-456
    • Jeong, W.1
  • 27
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • Lu J., Holmgren A. The thioredoxin antioxidant system. Free Radic. Biol. Med. 2014, 66:75-87.
    • (2014) Free Radic. Biol. Med. , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2
  • 28
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • Thimmulappa R.K., et al. 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
  • 29
    • 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., et al. 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
  • 30
    • 80053452983 scopus 로고    scopus 로고
    • Beneficial role of Nrf2 in regulating NADPH generation and consumption
    • Wu K.C., et al. Beneficial role of Nrf2 in regulating NADPH generation and consumption. Toxicol. Sci. 2011, 123:590-600.
    • (2011) Toxicol. Sci. , vol.123 , pp. 590-600
    • Wu, K.C.1
  • 31
    • 84863764614 scopus 로고    scopus 로고
    • Nrf2 redirects glucose and glutamine into anabolic pathways in metabolic reprogramming
    • Mitsuishi Y., et al. Nrf2 redirects glucose and glutamine into anabolic pathways in metabolic reprogramming. Cancer Cell 2012, 22:66-79.
    • (2012) Cancer Cell , vol.22 , pp. 66-79
    • Mitsuishi, Y.1
  • 32
    • 84879661552 scopus 로고    scopus 로고
    • Transcription factor NRF2 regulates miR-1 and miR-206 to drive tumorigenesis
    • Singh A., et al. Transcription factor NRF2 regulates miR-1 and miR-206 to drive tumorigenesis. J. Clin. Invest. 2013, 123:2921-2934.
    • (2013) J. Clin. Invest. , vol.123 , pp. 2921-2934
    • Singh, A.1
  • 33
    • 35148823513 scopus 로고    scopus 로고
    • NRF2 modulates aryl hydrocarbon receptor signaling: influence on adipogenesis
    • Shin S., et al. NRF2 modulates aryl hydrocarbon receptor signaling: influence on adipogenesis. Mol. Cell. Biol. 2007, 27:7188-7197.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7188-7197
    • Shin, S.1
  • 34
    • 84855453637 scopus 로고    scopus 로고
    • Nuclear factor erythroid-derived factor 2-related factor 2 regulates transcription of CCAAT/enhancer-binding protein β during adipogenesis
    • Hou Y., et al. Nuclear factor erythroid-derived factor 2-related factor 2 regulates transcription of CCAAT/enhancer-binding protein β during adipogenesis. Free Radic. Biol. Med. 2012, 52:462-472.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 462-472
    • Hou, Y.1
  • 35
    • 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
    • Kwak M.K., et al. 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. 2002, 22:2883-2892.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2883-2892
    • Kwak, M.K.1
  • 36
    • 77958130983 scopus 로고    scopus 로고
    • Cancer chemoprevention mechanisms mediated through the Keap1-Nrf2 pathway
    • Hayes J.D., et al. Cancer chemoprevention mechanisms mediated through the Keap1-Nrf2 pathway. Antioxid. Redox Signal. 2010, 13:1713-1748.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1713-1748
    • Hayes, J.D.1
  • 37
    • 84877846556 scopus 로고    scopus 로고
    • RXRα inhibits the NRF2-ARE signaling pathway through a direct interaction with the Neh7 domain of NRF2
    • Wang H., et al. RXRα inhibits the NRF2-ARE signaling pathway through a direct interaction with the Neh7 domain of NRF2. Cancer Res. 2013, 73:3097-3108.
    • (2013) Cancer Res. , vol.73 , pp. 3097-3108
    • Wang, H.1
  • 38
    • 79954416526 scopus 로고    scopus 로고
    • The cytoprotective role of the Keap1-Nrf2 pathway
    • Baird L., Dinkova-Kostova A.T. The cytoprotective role of the Keap1-Nrf2 pathway. Arch. Toxicol. 2011, 85:241-272.
    • (2011) Arch. Toxicol. , vol.85 , pp. 241-272
    • Baird, L.1    Dinkova-Kostova, A.T.2
  • 39
    • 33344463325 scopus 로고    scopus 로고
    • Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model
    • Tong K.I., et al. Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. Mol. Cell. Biol. 2006, 26:2887-2900.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2887-2900
    • Tong, K.I.1
  • 40
    • 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., et al. 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
  • 41
    • 84893840509 scopus 로고    scopus 로고
    • Kinetic, thermodynamic and structural characterizations of association between Nrf2-DLGex degron and Keap1
    • Fukutomi T., et al. Kinetic, thermodynamic and structural characterizations of association between Nrf2-DLGex degron and Keap1. Mol. Cell. Biol. 2014, 34:832-846.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 832-846
    • Fukutomi, T.1
  • 42
    • 77649261371 scopus 로고    scopus 로고
    • Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains
    • Ogura T., et al. Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:2842-2847.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2842-2847
    • Ogura, T.1
  • 43
    • 84873056802 scopus 로고    scopus 로고
    • The nuclear cofactor RAC3/AIB1/SRC-3 enhances Nrf2 signaling by interacting with transactivation domains
    • Kim J.H., et al. The nuclear cofactor RAC3/AIB1/SRC-3 enhances Nrf2 signaling by interacting with transactivation domains. Oncogene 2013, 32:514-527.
    • (2013) Oncogene , vol.32 , pp. 514-527
    • Kim, J.H.1
  • 44
    • 79952256187 scopus 로고    scopus 로고
    • SCF/β-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner
    • Rada P., et al. SCF/β-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner. Mol. Cell. Biol. 2011, 31:1121-1133.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1121-1133
    • Rada, P.1
  • 45
    • 84866283856 scopus 로고    scopus 로고
    • Structural and functional characterization of Nrf2 degradation by the glycogen synthase kinase 3/β-TrCP axis
    • Rada P., et al. Structural and functional characterization of Nrf2 degradation by the glycogen synthase kinase 3/β-TrCP axis. Mol. Cell. Biol. 2012, 32:3486-3499.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 3486-3499
    • Rada, P.1
  • 46
    • 84881476323 scopus 로고    scopus 로고
    • Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity
    • Chowdhry S., et al. Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity. Oncogene 2013, 32:3765-3781.
    • (2013) Oncogene , vol.32 , pp. 3765-3781
    • Chowdhry, S.1
  • 47
    • 0034723296 scopus 로고    scopus 로고
    • Homodimer of two F-box proteins βTrCP1 or βTrCP2 binds to IκBα for signal-dependent ubiquitination
    • Suzuki H., et al. Homodimer of two F-box proteins βTrCP1 or βTrCP2 binds to IκBα for signal-dependent ubiquitination. J. Biol. Chem. 2000, 275:2877-2884.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2877-2884
    • Suzuki, H.1
  • 48
    • 0037756787 scopus 로고    scopus 로고
    • β-TrCP1 ubiquitin ligase
    • β-TrCP1 ubiquitin ligase. Mol. Cell 2003, 11:1445-1456.
    • (2003) Mol. Cell , vol.11 , pp. 1445-1456
    • Wu, G.1
  • 49
    • 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., et al. 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. 2001, 61:3299-3307.
    • (2001) Cancer Res. , vol.61 , pp. 3299-3307
    • McMahon, M.1
  • 50
    • 77649163840 scopus 로고    scopus 로고
    • Nrf2 expression is regulated by epigenetic mechanisms in prostate cancer of TRAMP mice
    • Yu S., et al. Nrf2 expression is regulated by epigenetic mechanisms in prostate cancer of TRAMP mice. PLoS ONE 2010, 5:e8579.
    • (2010) PLoS ONE , vol.5
    • Yu, S.1
  • 51
    • 0036006792 scopus 로고    scopus 로고
    • Linkage analysis of susceptibility to hyperoxia. Nrf2 is a candidate gene
    • Cho H.Y., et al. Linkage analysis of susceptibility to hyperoxia. Nrf2 is a candidate gene. Am. J. Respir. Cell Mol. Biol. 2002, 26:42-51.
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , pp. 42-51
    • Cho, H.Y.1
  • 52
    • 84878620505 scopus 로고    scopus 로고
    • Regulatory nexus of synthesis and degradation deciphers cellular Nrf2 expression levels
    • Suzuki T., et al. Regulatory nexus of synthesis and degradation deciphers cellular Nrf2 expression levels. Mol. Cell. Biol. 2013, 33:2402-2412.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2402-2412
    • Suzuki, T.1
  • 53
    • 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
    • Miao W., et al. 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. 2005, 280:20340-20348.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20340-20348
    • Miao, W.1
  • 54
    • 70349269512 scopus 로고    scopus 로고
    • Introducing the "TCDD-inducible AhR-Nrf2 gene battery"
    • Yeager R.L., et al. Introducing the "TCDD-inducible AhR-Nrf2 gene battery". Toxicol. Sci. 2009, 111:238-246.
    • (2009) Toxicol. Sci. , vol.111 , pp. 238-246
    • Yeager, R.L.1
  • 55
    • 80053130888 scopus 로고    scopus 로고
    • Nrf2 protects against 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)-induced oxidative injury and steatohepatitis
    • Lu H., et al. Nrf2 protects against 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)-induced oxidative injury and steatohepatitis. Toxicol. Appl. Pharmacol. 2011, 256:122-135.
    • (2011) Toxicol. Appl. Pharmacol. , vol.256 , pp. 122-135
    • Lu, H.1
  • 56
    • 58149181985 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced expression of NAD(P)H:quinone oxidoreductase 1 and heme oxygenase-1 protects against excessive inflammatory responses in human monocytes
    • Rushworth S.A., et al. Lipopolysaccharide-induced expression of NAD(P)H:quinone oxidoreductase 1 and heme oxygenase-1 protects against excessive inflammatory responses in human monocytes. J. Immunol. 2008, 181:6730-6737.
    • (2008) J. Immunol. , vol.181 , pp. 6730-6737
    • Rushworth, S.A.1
  • 57
    • 84871519753 scopus 로고    scopus 로고
    • The high Nrf2 expression in human acute myeloid leukemia is driven by NF-κB and underlies its chemo-resistance
    • Rushworth S.A., et al. The high Nrf2 expression in human acute myeloid leukemia is driven by NF-κB and underlies its chemo-resistance. Blood 2012, 120:5188-5198.
    • (2012) Blood , vol.120 , pp. 5188-5198
    • Rushworth, S.A.1
  • 58
    • 79960972350 scopus 로고    scopus 로고
    • Detoxification: a novel function of BRCA1 in tumor suppression?
    • Kang H.J., et al. Detoxification: a novel function of BRCA1 in tumor suppression?. Toxicol. Sci. 2011, 122:26-37.
    • (2011) Toxicol. Sci. , vol.122 , pp. 26-37
    • Kang, H.J.1
  • 59
    • 33744962596 scopus 로고    scopus 로고
    • BRCA1 modulates xenobiotic stress-inducible gene expression by interacting with ARNT in human breast cancer cells
    • Kang H.J., et al. BRCA1 modulates xenobiotic stress-inducible gene expression by interacting with ARNT in human breast cancer cells. J. Biol. Chem. 2006, 281:14654-14662.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14654-14662
    • Kang, H.J.1
  • 60
    • 77949676576 scopus 로고    scopus 로고
    • Transcriptional profiling reveals divergent roles of PPARα and PPARβ/δ in regulation of gene expression in mouse liver
    • Sanderson L.M., et al. Transcriptional profiling reveals divergent roles of PPARα and PPARβ/δ in regulation of gene expression in mouse liver. Physiol. Genomics 2010, 41:42-52.
    • (2010) Physiol. Genomics , vol.41 , pp. 42-52
    • Sanderson, L.M.1
  • 61
    • 84875061355 scopus 로고    scopus 로고
    • Genetic activation of Nrf2 protects against fasting-induced oxidative stress in livers of mice
    • Zhang Y.K., et al. Genetic activation of Nrf2 protects against fasting-induced oxidative stress in livers of mice. PLoS ONE 2013, 8:e59122.
    • (2013) PLoS ONE , vol.8
    • Zhang, Y.K.1
  • 62
    • 84892181024 scopus 로고    scopus 로고
    • Fasting induces nuclear factor E2-related factor 2 and ATP-binding cassette transporters via protein kinase A and sirtuin-1 in mouse and human
    • Kulkarni S.R., et al. Fasting induces nuclear factor E2-related factor 2 and ATP-binding cassette transporters via protein kinase A and sirtuin-1 in mouse and human. Antioxid. Redox Signal. 2014, 20:15-30.
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 15-30
    • Kulkarni, S.R.1
  • 63
    • 3843070757 scopus 로고    scopus 로고
    • Starvation response in mouse liver shows strong correlation with life-span-prolonging processes
    • Bauer M., et al. Starvation response in mouse liver shows strong correlation with life-span-prolonging processes. Physiol. Genomics 2004, 17:230-244.
    • (2004) Physiol. Genomics , vol.17 , pp. 230-244
    • Bauer, M.1
  • 64
    • 79960060305 scopus 로고    scopus 로고
    • Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
    • DeNicola G.M., et al. Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis. Nature 2011, 475:106-109.
    • (2011) Nature , vol.475 , pp. 106-109
    • DeNicola, G.M.1
  • 65
    • 80052570740 scopus 로고    scopus 로고
    • MiR-28 regulates Nrf2 expression through a Keap1-independent mechanism
    • Yang M., et al. MiR-28 regulates Nrf2 expression through a Keap1-independent mechanism. Breast Cancer Res. Treat. 2011, 129:983-991.
    • (2011) Breast Cancer Res. Treat. , vol.129 , pp. 983-991
    • Yang, M.1
  • 66
    • 84870859466 scopus 로고    scopus 로고
    • Identification of novel microRNAs in post-transcriptional control of Nrf2 expression and redox homeostasis in neuronal, SH-SY5Y cells
    • Narasimhan M., et al. Identification of novel microRNAs in post-transcriptional control of Nrf2 expression and redox homeostasis in neuronal, SH-SY5Y cells. PLoS ONE 2012, 7:e51111.
    • (2012) PLoS ONE , vol.7
    • Narasimhan, M.1
  • 67
    • 84877113289 scopus 로고    scopus 로고
    • MicroRNA-93 regulates NRF2 expression and is associated with breast carcinogenesis
    • Singh B., et al. MicroRNA-93 regulates NRF2 expression and is associated with breast carcinogenesis. Carcinogenesis 2013, 34:1165-1172.
    • (2013) Carcinogenesis , vol.34 , pp. 1165-1172
    • Singh, B.1
  • 68
    • 0242329881 scopus 로고    scopus 로고
    • Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation
    • Wakabayashi N., et al. Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation. Nat. Genet. 2003, 35:238-245.
    • (2003) Nat. Genet. , vol.35 , pp. 238-245
    • Wakabayashi, N.1
  • 69
    • 18844454763 scopus 로고    scopus 로고
    • Utility of siRNA against Keap1 as a strategy to stimulate a cancer chemopreventive phenotype
    • Devling T.W., et al. Utility of siRNA against Keap1 as a strategy to stimulate a cancer chemopreventive phenotype. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:7280-7285A.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102
    • Devling, T.W.1
  • 70
    • 84878681301 scopus 로고    scopus 로고
    • The Keap1-Nrf2 system in cancers: stress response and anabolic metabolism
    • Mitsuishi Y., et al. The Keap1-Nrf2 system in cancers: stress response and anabolic metabolism. Front. Oncol. 2012, 2:200.
    • (2012) Front. Oncol. , vol.2 , pp. 200
    • Mitsuishi, Y.1
  • 71
    • 84885944468 scopus 로고    scopus 로고
    • The emerging role of the Nrf2-Keap1 signaling pathway in cancer
    • Jaramillo M.C., Zhang D.D. The emerging role of the Nrf2-Keap1 signaling pathway in cancer. Genes Dev. 2013, 27:2179-2191.
    • (2013) Genes Dev. , vol.27 , pp. 2179-2191
    • Jaramillo, M.C.1    Zhang, D.D.2
  • 72
    • 79958702879 scopus 로고    scopus 로고
    • Frequent epigenetics inactivation of KEAP1 gene in non-small cell lung cancer
    • Muscarella L.A., et al. Frequent epigenetics inactivation of KEAP1 gene in non-small cell lung cancer. Epigenetics 2011, 6:710-719.
    • (2011) Epigenetics , vol.6 , pp. 710-719
    • Muscarella, L.A.1
  • 73
    • 84872038941 scopus 로고    scopus 로고
    • Aberrant Keap1 methylation in breast cancer and association with clinicopathological features
    • Barbano R., et al. Aberrant Keap1 methylation in breast cancer and association with clinicopathological features. Epigenetics 2013, 8:105-112.
    • (2013) Epigenetics , vol.8 , pp. 105-112
    • Barbano, R.1
  • 74
    • 84857997256 scopus 로고    scopus 로고
    • Methylation of the KEAP1 gene promoter region in human colorectal cancer
    • Hanada N., et al. Methylation of the KEAP1 gene promoter region in human colorectal cancer. BMC Cancer 2012, 12:66.
    • (2012) BMC Cancer , vol.12 , pp. 66
    • Hanada, N.1
  • 75
    • 81755171451 scopus 로고    scopus 로고
    • MiR-200a regulates Nrf2 activation by targeting Keap1 mRNA in breast cancer cells
    • Eades G., et al. miR-200a regulates Nrf2 activation by targeting Keap1 mRNA in breast cancer cells. J. Biol. Chem. 2011, 286:40725-40733.
    • (2011) J. Biol. Chem. , vol.286 , pp. 40725-40733
    • Eades, G.1
  • 76
    • 84883743438 scopus 로고    scopus 로고
    • MiR-141 regulates KEAP1 and modulates cisplatin sensitivity in ovarian cancer cells
    • van Jaarsveld M.T., et al. miR-141 regulates KEAP1 and modulates cisplatin sensitivity in ovarian cancer cells. Oncogene 2013, 32:4284-4293.
    • (2013) Oncogene , vol.32 , pp. 4284-4293
    • van Jaarsveld, M.T.1
  • 77
    • 84884338770 scopus 로고    scopus 로고
    • Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex
    • Baird L., et al. Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:15259-15264.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 15259-15264
    • Baird, L.1
  • 78
    • 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., et al. 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. U.S.A. 2002, 99:11908-11913.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1
  • 79
    • 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
  • 80
    • 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
    • Kobayashi M., et al. The antioxidant defense system Keap1-Nrf2 comprises a multiple sensing mechanism for responding to a wide range of chemical compounds. Mol. Cell. Biol. 2009, 29:493-502.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 493-502
    • Kobayashi, M.1
  • 81
    • 77950887186 scopus 로고    scopus 로고
    • 2 involves KEAP1 disulfide formation
    • 2 involves KEAP1 disulfide formation. J. Biol. Chem. 2010, 285:8463-8471.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8463-8471
    • Fourquet, S.1
  • 82
    • 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
    • Fujii S., et al. The critical role of nitric oxide signaling, via protein S-guanylation and nitrated cyclic GMP, in the antioxidant adaptive response. J. Biol. Chem. 2010, 285:23970-23984.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23970-23984
    • Fujii, S.1
  • 83
    • 78650509515 scopus 로고    scopus 로고
    • Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals
    • McMahon M., et al. Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:18838-18843.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 18838-18843
    • McMahon, M.1
  • 84
    • 84864461148 scopus 로고    scopus 로고
    • Validation of the multiple sensor mechanism of the Keap1-Nrf2 system
    • Takaya K., et al. Validation of the multiple sensor mechanism of the Keap1-Nrf2 system. Free Radic. Biol. Med. 2012, 53:817-827.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 817-827
    • Takaya, K.1
  • 85
    • 84879893851 scopus 로고    scopus 로고
    • The gasotransmitter hydrogen sulfide induces nrf2-target genes by inactivating the keap1 ubiquitin ligase substrate adaptor through formation of a disulfide bond between cys-226 and cys-613
    • Hourihan J.M., et al. The gasotransmitter hydrogen sulfide induces nrf2-target genes by inactivating the keap1 ubiquitin ligase substrate adaptor through formation of a disulfide bond between cys-226 and cys-613. Antioxid. Redox Signal. 2013, 19:465-481.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 465-481
    • Hourihan, J.M.1
  • 86
    • 79954616432 scopus 로고    scopus 로고
    • Electrophilic nitro-fatty acids activate NRF2 by a KEAP1 cysteine 151-independent mechanism
    • Kansanen E., et al. Electrophilic nitro-fatty acids activate NRF2 by a KEAP1 cysteine 151-independent mechanism. J. Biol. Chem. 2011, 286:14019-14027.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14019-14027
    • Kansanen, E.1
  • 87
    • 80054767730 scopus 로고    scopus 로고
    • Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling
    • Adam J., et al. Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling. Cancer Cell 2011, 20:524-537.
    • (2011) Cancer Cell , vol.20 , pp. 524-537
    • Adam, J.1
  • 88
    • 84865287281 scopus 로고    scopus 로고
    • Keap1 degradation by autophagy for the maintenance of redox homeostasis
    • Taguchi K., et al. Keap1 degradation by autophagy for the maintenance of redox homeostasis. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:13561-13566.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 13561-13566
    • Taguchi, K.1
  • 89
    • 84891686345 scopus 로고    scopus 로고
    • USP15 negatively regulates Nrf2 through deubiquitination of Keap1
    • Villeneuve N.F., et al. USP15 negatively regulates Nrf2 through deubiquitination of Keap1. Mol. Cell 2013, 51:68-79.
    • (2013) Mol. Cell , vol.51 , pp. 68-79
    • Villeneuve, N.F.1
  • 90
    • 37549032763 scopus 로고    scopus 로고
    • An auto-regulatory loop between stress sensors INrf2 and Nrf2 controls their cellular abundance
    • Lee O.H., et al. An auto-regulatory loop between stress sensors INrf2 and Nrf2 controls their cellular abundance. J. Biol. Chem. 2007, 282:36412-36420.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36412-36420
    • Lee, O.H.1
  • 91
    • 84876011848 scopus 로고    scopus 로고
    • Proteomic analysis of ubiquitin ligase KEAP1 reveals associated proteins that inhibit NRF2 ubiquitination
    • Hast B.E., et al. Proteomic analysis of ubiquitin ligase KEAP1 reveals associated proteins that inhibit NRF2 ubiquitination. Cancer Res. 2013, 73:2199-2210.
    • (2013) Cancer Res. , vol.73 , pp. 2199-2210
    • Hast, B.E.1
  • 92
    • 70349970493 scopus 로고    scopus 로고
    • KEAP1 E3 ligase-mediated downregulation of NF-κB signaling by targeting IKKβ
    • Lee D.F., et al. KEAP1 E3 ligase-mediated downregulation of NF-κB signaling by targeting IKKβ. Mol. Cell 2009, 36:131-140.
    • (2009) Mol. Cell , vol.36 , pp. 131-140
    • Lee, D.F.1
  • 93
    • 77955653742 scopus 로고    scopus 로고
    • Suppression of NF-κB signaling by KEAP1 regulation of IKKβ activity through autophagic degradation and inhibition of phosphorylation
    • Kim J.E., et al. Suppression of NF-κB signaling by KEAP1 regulation of IKKβ activity through autophagic degradation and inhibition of phosphorylation. Cell. Signal. 2010, 22:1645-1654.
    • (2010) Cell. Signal. , vol.22 , pp. 1645-1654
    • Kim, J.E.1
  • 94
    • 84884172226 scopus 로고    scopus 로고
    • Insight into the intermolecular recognition mechanism between Keap1 and IKKβ combining homology modelling, protein-protein docking, molecular dynamics simulations and virtual alanine mutation
    • Jiang Z.Y., et al. Insight into the intermolecular recognition mechanism between Keap1 and IKKβ combining homology modelling, protein-protein docking, molecular dynamics simulations and virtual alanine mutation. PLoS ONE 2013, 8:e75076.
    • (2013) PLoS ONE , vol.8
    • Jiang, Z.Y.1
  • 95
    • 84861312722 scopus 로고    scopus 로고
    • PALB2 interacts with KEAP1 to promote NRF2 nuclear accumulation and function
    • Ma J., et al. PALB2 interacts with KEAP1 to promote NRF2 nuclear accumulation and function. Mol. Cell. Biol. 2012, 32:1506-1517.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1506-1517
    • Ma, J.1
  • 96
    • 42649130014 scopus 로고    scopus 로고
    • PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria
    • Lo S.C., Hannink M. PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria. Exp. Cell Res. 2008, 314:1789-1803.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1789-1803
    • Lo, S.C.1    Hannink, M.2
  • 97
    • 84857493148 scopus 로고    scopus 로고
    • Wilms tumor gene on X chromosome (WTX) inhibits degradation of NRF2 protein through competitive binding to KEAP1 protein
    • Camp N.D., et al. Wilms tumor gene on X chromosome (WTX) inhibits degradation of NRF2 protein through competitive binding to KEAP1 protein. J. Biol. Chem. 2012, 287:6539-6550.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6539-6550
    • Camp, N.D.1
  • 98
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M., et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat. Cell Biol. 2010, 12:213-223.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 213-223
    • Komatsu, M.1
  • 99
    • 77952781968 scopus 로고    scopus 로고
    • Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway
    • Copple I.M., et al. Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway. J. Biol. Chem. 2010, 285:16782-16788.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16782-16788
    • Copple, I.M.1
  • 100
    • 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
    • Jain A., et al. 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. 2010, 285:22576-22591.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22576-22591
    • Jain, A.1
  • 101
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62
    • Lau A., et al. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol. Cell. Biol. 2010, 30:3275-3285.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3275-3285
    • Lau, A.1
  • 102
    • 84883830467 scopus 로고    scopus 로고
    • Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy
    • Ichimura Y., et al. Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy. Mol. Cell 2013, 51:618-631.
    • (2013) Mol. Cell , vol.51 , pp. 618-631
    • Ichimura, Y.1
  • 103
    • 84885187437 scopus 로고    scopus 로고
    • A Central role for mTOR in lipid homeostasis
    • Lamming D.W., Sabatini D.M. A Central role for mTOR in lipid homeostasis. Cell Metab. 2013, 18:465-469.
    • (2013) Cell Metab. , vol.18 , pp. 465-469
    • Lamming, D.W.1    Sabatini, D.M.2
  • 104
    • 84872137966 scopus 로고    scopus 로고
    • Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage
    • Bae S.H., et al. Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage. Cell Metab. 2013, 17:73-84.
    • (2013) Cell Metab. , vol.17 , pp. 73-84
    • Bae, S.H.1
  • 105
    • 84897394327 scopus 로고    scopus 로고
    • SPBP Is a sulforaphane induced transcriptional coactivator of NRF2 regulating expression of the autophagy receptor p62/SQSTM1
    • Darvekar S.R., et al. SPBP Is a sulforaphane induced transcriptional coactivator of NRF2 regulating expression of the autophagy receptor p62/SQSTM1. PLoS ONE 2014, 9:e85262.
    • (2014) PLoS ONE , vol.9
    • Darvekar, S.R.1
  • 106
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z., et al. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012, 148:228-243.
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1
  • 107
    • 67449128222 scopus 로고    scopus 로고
    • Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response
    • Chen W., et al. Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response. Mol. Cell 2009, 34:663-673.
    • (2009) Mol. Cell , vol.34 , pp. 663-673
    • Chen, W.1
  • 108
    • 84884215156 scopus 로고    scopus 로고
    • BRCA1 interacts with Nrf2 to regulate antioxidant signaling and cell survival
    • Gorrini C., et al. BRCA1 interacts with Nrf2 to regulate antioxidant signaling and cell survival. J. Exp. Med. 2013, 210:1529-1544.
    • (2013) J. Exp. Med. , vol.210 , pp. 1529-1544
    • Gorrini, C.1
  • 109
    • 3843104763 scopus 로고    scopus 로고
    • Redox-regulated turnover of Nrf2 is determined by at least two separate protein domains, the redox-sensitive Neh2 degron and the redox-insensitive Neh6 degron
    • McMahon M., et al. Redox-regulated turnover of Nrf2 is determined by at least two separate protein domains, the redox-sensitive Neh2 degron and the redox-insensitive Neh6 degron. J. Biol. Chem. 2004, 279:31556-31567.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31556-31567
    • McMahon, M.1
  • 110
    • 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
    • Salazar M., et al. Glycogen synthase kinase-3β inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2. J. Biol. Chem. 2006, 281:14841-14851.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14841-14851
    • Salazar, M.1
  • 111
    • 44549085003 scopus 로고    scopus 로고
    • Bromocriptine activates NQO1 via Nrf2-PI3K/Akt signaling: novel cytoprotective mechanism against oxidative damage
    • Lim J.H., et al. Bromocriptine activates NQO1 via Nrf2-PI3K/Akt signaling: novel cytoprotective mechanism against oxidative damage. Pharmacol. Res. 2008, 57:325-331.
    • (2008) Pharmacol. Res. , vol.57 , pp. 325-331
    • Lim, J.H.1
  • 112
    • 45549087514 scopus 로고    scopus 로고
    • Essential roles of the PI3 kinase/Akt pathway in regulating Nrf2-dependent antioxidant functions in the RPE
    • Wang L., et al. Essential roles of the PI3 kinase/Akt pathway in regulating Nrf2-dependent antioxidant functions in the RPE. Invest. Ophthalmol. Vis. Sci. 2008, 49:1671-1678.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 1671-1678
    • Wang, L.1
  • 113
    • 77957221943 scopus 로고    scopus 로고
    • Synthetic triterpenoids attenuate cytotoxic retinal injury: cross-talk between Nrf2 and PI3K/AKT signaling through inhibition of the lipid phosphatase PTEN
    • Pitha-Rowe I., et al. Synthetic triterpenoids attenuate cytotoxic retinal injury: cross-talk between Nrf2 and PI3K/AKT signaling through inhibition of the lipid phosphatase PTEN. Invest. Ophthalmol. Vis. Sci. 2009, 50:5339-5347.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 5339-5347
    • Pitha-Rowe, I.1
  • 114
    • 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., et al. 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
  • 115
    • 84893822502 scopus 로고    scopus 로고
    • Nrf2 enhances cholangiocyte expansion in Pten-deficient livers
    • Taguchi K., et al. Nrf2 enhances cholangiocyte expansion in Pten-deficient livers. Mol. Cell. Biol. 2014, 34:900-913.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 900-913
    • Taguchi, K.1
  • 116
    • 33744953050 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 568 controls nuclear export of Nrf2
    • Jain A.K., Jaiswal A.K. Phosphorylation of tyrosine 568 controls nuclear export of Nrf2. J. Biol. Chem. 2006, 281:12132-12142.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12132-12142
    • Jain, A.K.1    Jaiswal, A.K.2
  • 117
    • 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
    • Jain A.K., Jaiswal A.K. GSK-3β acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2. J. Biol. Chem. 2007, 282:16502-16510.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16502-16510
    • Jain, A.K.1    Jaiswal, A.K.2
  • 118
    • 77954351267 scopus 로고    scopus 로고
    • CR6-interacting factor 1 (CRIF1) regulates NF-E2-related factor 2 (NRF2) protein stability by proteasome-mediated degradation
    • Kang H.J., et al. CR6-interacting factor 1 (CRIF1) regulates NF-E2-related factor 2 (NRF2) protein stability by proteasome-mediated degradation. J. Biol. Chem. 2010, 285:21258-21268.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21258-21268
    • Kang, H.J.1
  • 119
    • 84887365249 scopus 로고    scopus 로고
    • Mechanism of androgen receptor corepression by CKBP2/CRIF1, a multifunctional transcription factor coregulator expressed in prostate cancer
    • Tan J.A., et al. Mechanism of androgen receptor corepression by CKBP2/CRIF1, a multifunctional transcription factor coregulator expressed in prostate cancer. Mol. Cell. Endocrinol. 2014, 382:302-313.
    • (2014) Mol. Cell. Endocrinol. , vol.382 , pp. 302-313
    • Tan, J.A.1
  • 120
    • 84880063584 scopus 로고    scopus 로고
    • Seven in absentia homolog 2 (Siah2) protein is a regulator of NF-E2-related factor 2 (Nrf2)
    • Baba K., et al. Seven in absentia homolog 2 (Siah2) protein is a regulator of NF-E2-related factor 2 (Nrf2). J. Biol. Chem. 2013, 288:18393-18405.
    • (2013) J. Biol. Chem. , vol.288 , pp. 18393-18405
    • Baba, K.1
  • 121
    • 84885599237 scopus 로고    scopus 로고
    • SIAH ubiquitin ligases target the nonreceptor tyrosine kinase ACK1 for ubiquitinylation and proteasomal degradation
    • Buchwald M., et al. SIAH ubiquitin ligases target the nonreceptor tyrosine kinase ACK1 for ubiquitinylation and proteasomal degradation. Oncogene 2013, 32:4913-4920.
    • (2013) Oncogene , vol.32 , pp. 4913-4920
    • Buchwald, M.1
  • 122
    • 84877913024 scopus 로고    scopus 로고
    • Trafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleus
    • Malloy M.T., et al. Trafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleus. J. Biol. Chem. 2013, 288:14569-14583.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14569-14583
    • Malloy, M.T.1
  • 123
    • 66349129338 scopus 로고    scopus 로고
    • Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response
    • Sun Z., et al. Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response. Mol. Cell. Biol. 2009, 29:2658-2672.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2658-2672
    • Sun, Z.1
  • 124
    • 79954424076 scopus 로고    scopus 로고
    • Nrf2: control of sensitivity to carcinogens
    • Slocum S.L., Kensler T.W. Nrf2: control of sensitivity to carcinogens. Arch. Toxicol. 2011, 85:273-284.
    • (2011) Arch. Toxicol. , vol.85 , pp. 273-284
    • Slocum, S.L.1    Kensler, T.W.2
  • 125
    • 84867034260 scopus 로고    scopus 로고
    • Role of nrf2 in oxidative stress and toxicity
    • Ma Q. Role of nrf2 in oxidative stress and toxicity. Annu. Rev. Pharmacol. Toxicol. 2013, 53:401-426.
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 401-426
    • Ma, Q.1
  • 126
    • 84867917942 scopus 로고    scopus 로고
    • Targeting of Nrf2 induces DNA damage signaling and protects colonic epithelial cells from ionizing radiation
    • Kim S.B., et al. Targeting of Nrf2 induces DNA damage signaling and protects colonic epithelial cells from ionizing radiation. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:E2949-E2955.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Kim, S.B.1
  • 127
    • 84878009975 scopus 로고    scopus 로고
    • Antioxidant-mediated up-regulation of OGG1 via NRF2 induction is associated with inhibition of oxidative DNA damage in estrogen-induced breast cancer
    • Singh B., et al. Antioxidant-mediated up-regulation of OGG1 via NRF2 induction is associated with inhibition of oxidative DNA damage in estrogen-induced breast cancer. BMC Cancer 2013, 13:253.
    • (2013) BMC Cancer , vol.13 , pp. 253
    • Singh, B.1
  • 128
    • 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., et al. 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
  • 129
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • Kwak M.K., et al. 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
  • 130
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress
    • Pickering A.M., et al. Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress. J. Biol. Chem. 2012, 287:10021-10031.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10021-10031
    • Pickering, A.M.1
  • 131
    • 77950907407 scopus 로고    scopus 로고
    • Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts
    • Kapeta S., et al. Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts. J. Biol. Chem. 2010, 285:8171-8184.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8171-8184
    • Kapeta, S.1
  • 132
    • 70449674487 scopus 로고    scopus 로고
    • Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2)
    • Arlt A., et al. Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2). Oncogene 2009, 28:3983-3996.
    • (2009) Oncogene , vol.28 , pp. 3983-3996
    • Arlt, A.1
  • 133
    • 79952202823 scopus 로고    scopus 로고
    • High basal nuclear levels of Nrf2 in acute myeloid leukemia reduces sensitivity to proteasome inhibitors
    • Rushworth S.A., et al. High basal nuclear levels of Nrf2 in acute myeloid leukemia reduces sensitivity to proteasome inhibitors. Cancer Res. 2011, 71:1999-2009.
    • (2011) Cancer Res. , vol.71 , pp. 1999-2009
    • Rushworth, S.A.1
  • 134
    • 84885177241 scopus 로고    scopus 로고
    • Inhibition of the Nrf2 transcription factor by the alkaloid trigonelline renders pancreatic cancer cells more susceptible to apoptosis through decreased proteasomal gene expression and proteasome activity
    • Arlt A., et al. Inhibition of the Nrf2 transcription factor by the alkaloid trigonelline renders pancreatic cancer cells more susceptible to apoptosis through decreased proteasomal gene expression and proteasome activity. Oncogene 2013, 32:4825-4835.
    • (2013) Oncogene , vol.32 , pp. 4825-4835
    • Arlt, A.1
  • 135
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B., et al. Autophagy in immunity and inflammation. Nature 2011, 469:323-335.
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1
  • 136
    • 84892185934 scopus 로고    scopus 로고
    • Early signalling events of autophagy
    • Gallagher L.E., Chan E.Y. Early signalling events of autophagy. Essays Biochem. 2013, 55:1-15.
    • (2013) Essays Biochem. , vol.55 , pp. 1-15
    • Gallagher, L.E.1    Chan, E.Y.2
  • 137
    • 84883414890 scopus 로고    scopus 로고
    • The LIR motif - crucial for selective autophagy
    • Birgisdottir Å.B., et al. The LIR motif - crucial for selective autophagy. J. Cell Sci. 2013, 126:3237-3247.
    • (2013) J. Cell Sci. , vol.126 , pp. 3237-3247
    • Birgisdottir Å, B.1
  • 138
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T., Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 2011, 7:279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 139
    • 79955492012 scopus 로고    scopus 로고
    • Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells
    • Inami Y., et al. Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells. J. Cell Biol. 2011, 193:275-284.
    • (2011) J. Cell Biol. , vol.193 , pp. 275-284
    • Inami, Y.1
  • 140
    • 14244256648 scopus 로고    scopus 로고
    • Nrf2 transcriptionally activates the mafG gene through an antioxidant response element
    • Katsuoka F., et al. Nrf2 transcriptionally activates the mafG gene through an antioxidant response element. J. Biol. Chem. 2005, 280:4483-4490.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4483-4490
    • Katsuoka, F.1
  • 141
    • 77950553993 scopus 로고    scopus 로고
    • Deficiency in the nuclear factor E2-related factor-2 transcription factor results in impaired adipogenesis and protects against diet-induced obesity
    • Pi J., et al. Deficiency in the nuclear factor E2-related factor-2 transcription factor results in impaired adipogenesis and protects against diet-induced obesity. J. Biol. Chem. 2010, 285:9292-9300.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9292-9300
    • Pi, J.1
  • 142
    • 34547592709 scopus 로고    scopus 로고
    • Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling
    • Hurd T.R., et al. Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling. J. Biol. Chem. 2007, 282:22040-22051.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22040-22051
    • Hurd, T.R.1
  • 143
    • 0022383292 scopus 로고
    • Sulfhydryl/disulfide forms of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Ness G.C., et al. Sulfhydryl/disulfide forms of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 1985, 260:16395-16399.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16395-16399
    • Ness, G.C.1
  • 144
    • 0027452703 scopus 로고
    • Oxidative inactivation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and subunit cross-linking involve different dithiol/disulfide centers
    • Cappel R.E., Gilbert H.F. Oxidative inactivation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and subunit cross-linking involve different dithiol/disulfide centers. J. Biol. Chem. 1993, 268:342-348.
    • (1993) J. Biol. Chem. , vol.268 , pp. 342-348
    • Cappel, R.E.1    Gilbert, H.F.2
  • 145
    • 82755166890 scopus 로고    scopus 로고
    • Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses
    • Anastasiou D., et al. Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 2011, 334:1278-1283.
    • (2011) Science , vol.334 , pp. 1278-1283
    • Anastasiou, D.1
  • 146
    • 84872767045 scopus 로고    scopus 로고
    • Energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase
    • Holyoak T., et al. Energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase. Biochemistry 2013, 52:466-476.
    • (2013) Biochemistry , vol.52 , pp. 466-476
    • Holyoak, T.1
  • 147
    • 84862849835 scopus 로고    scopus 로고
    • Redox implications of AMPK-mediated signal transduction beyond energetic clues
    • Cardaci S., et al. Redox implications of AMPK-mediated signal transduction beyond energetic clues. J. Cell Sci. 2012, 125:2115-2125.
    • (2012) J. Cell Sci. , vol.125 , pp. 2115-2125
    • Cardaci, S.1
  • 148
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden M.G., et al. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 2009, 324:1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1
  • 149
    • 84864674743 scopus 로고    scopus 로고
    • Nrf2 orchestrates fuel partitioning for cell proliferation
    • Hayes J.D., Ashford M.L. Nrf2 orchestrates fuel partitioning for cell proliferation. Cell Metab. 2012, 16:139-141.
    • (2012) Cell Metab. , vol.16 , pp. 139-141
    • Hayes, J.D.1    Ashford, M.L.2
  • 150
    • 84864292789 scopus 로고    scopus 로고
    • Rocking cell metabolism: revised functions of the key glycolytic regulator PKM2 in cancer
    • Chaneton B., Gottlieb E. Rocking cell metabolism: revised functions of the key glycolytic regulator PKM2 in cancer. Trends Biochem. Sci. 2012, 37:309-316.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 309-316
    • Chaneton, B.1    Gottlieb, E.2
  • 151
    • 84861320929 scopus 로고    scopus 로고
    • Teaching the design principles of metabolism
    • Rabinowitz J.D., Vastag L. Teaching the design principles of metabolism. Nat. Chem. Biol. 2012, 8:497-501.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 497-501
    • Rabinowitz, J.D.1    Vastag, L.2
  • 152
    • 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
    • Kitteringham N.R., et al. Proteomic analysis of Nrf2 deficient transgenic mice reveals cellular defence and lipid metabolism as primary Nrf2-dependent pathways in the liver. J. Proteomics 2010, 73:1612-1631.
    • (2010) J. Proteomics , vol.73 , pp. 1612-1631
    • Kitteringham, N.R.1
  • 153
    • 66249105703 scopus 로고    scopus 로고
    • ATP-citrate lyase links cellular metabolism to histone acetylation
    • Wellen K.E., et al. ATP-citrate lyase links cellular metabolism to histone acetylation. Science 2009, 324:1076-1080.
    • (2009) Science , vol.324 , pp. 1076-1080
    • Wellen, K.E.1
  • 154
    • 43249127067 scopus 로고    scopus 로고
    • Role of stearoyl-coenzyme A desaturase in regulating lipid metabolism
    • Flowers M.T., Ntambi J.M. Role of stearoyl-coenzyme A desaturase in regulating lipid metabolism. Curr. Opin. Lipidol. 2008, 19:248-256.
    • (2008) Curr. Opin. Lipidol. , vol.19 , pp. 248-256
    • Flowers, M.T.1    Ntambi, J.M.2
  • 155
    • 84868152812 scopus 로고    scopus 로고
    • Dysregulated expression of fatty acid oxidation enzymes and iron-regulatory genes in livers of Nrf2-null mice
    • Tanaka Y., et al. Dysregulated expression of fatty acid oxidation enzymes and iron-regulatory genes in livers of Nrf2-null mice. J. Gastroenterol. Hepatol. 2012, 27:1711-1717.
    • (2012) J. Gastroenterol. Hepatol. , vol.27 , pp. 1711-1717
    • Tanaka, Y.1
  • 156
    • 48749091560 scopus 로고    scopus 로고
    • Nrf2 regulates the alternative first exons of CD36 in macrophages through specific antioxidant response elements
    • Maruyama A., et al. Nrf2 regulates the alternative first exons of CD36 in macrophages through specific antioxidant response elements. Arch. Biochem. Biophys. 2008, 477:139-145.
    • (2008) Arch. Biochem. Biophys. , vol.477 , pp. 139-145
    • Maruyama, A.1
  • 157
    • 84863617800 scopus 로고    scopus 로고
    • In vivo, fatty acid translocase (CD36) critically regulates skeletal muscle fuel selection, exercise performance, and training-induced adaptation of fatty acid oxidation
    • McFarlan J.T., et al. In vivo, fatty acid translocase (CD36) critically regulates skeletal muscle fuel selection, exercise performance, and training-induced adaptation of fatty acid oxidation. J. Biol. Chem. 2012, 287:23502-23516.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23502-23516
    • McFarlan, J.T.1
  • 158
    • 84892186623 scopus 로고    scopus 로고
    • Nrf2 impacts the efficiency of mitochondrial fatty acid oxidation
    • Ludtmann M.H., et al. Nrf2 impacts the efficiency of mitochondrial fatty acid oxidation. Biochem. J. 2014, 457:415-424.
    • (2014) Biochem. J. , vol.457 , pp. 415-424
    • Ludtmann, M.H.1
  • 159
    • 72649103895 scopus 로고    scopus 로고
    • Loss of Nrf2 markedly exacerbates nonalcoholic steatohepatitis
    • Chowdhry S., et al. Loss of Nrf2 markedly exacerbates nonalcoholic steatohepatitis. Free Radic. Biol. Med. 2010, 48:357-371.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 357-371
    • Chowdhry, S.1
  • 160
    • 76749149157 scopus 로고    scopus 로고
    • Deletion of nuclear factor-E2-related factor-2 leads to rapid onset and progression of nutritional steatohepatitis in mice
    • Sugimoto H., et al. Deletion of nuclear factor-E2-related factor-2 leads to rapid onset and progression of nutritional steatohepatitis in mice. Am. J. Physiol. Gastrointest. Liver Physiol. 2010, 298:G283-G294.
    • (2010) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.298
    • Sugimoto, H.1
  • 161
    • 77952952816 scopus 로고    scopus 로고
    • Enhanced expression of Nrf2 in mice attenuates the fatty liver produced by a methionine- and choline-deficient diet
    • Zhang Y.K., et al. Enhanced expression of Nrf2 in mice attenuates the fatty liver produced by a methionine- and choline-deficient diet. Toxicol. Appl. Pharmacol. 2010, 245:326-334.
    • (2010) Toxicol. Appl. Pharmacol. , vol.245 , pp. 326-334
    • Zhang, Y.K.1
  • 162
    • 84878111720 scopus 로고    scopus 로고
    • Deletion of Nrf2 leads to rapid progression of steatohepatitis in mice fed atherogenic plus high-fat diet
    • Okada K., et al. Deletion of Nrf2 leads to rapid progression of steatohepatitis in mice fed atherogenic plus high-fat diet. J. Gastroenterol. 2013, 48:620-632.
    • (2013) J. Gastroenterol. , vol.48 , pp. 620-632
    • Okada, K.1
  • 163
    • 84883205682 scopus 로고    scopus 로고
    • A diet rich in high-glucoraphanin broccoli interacts with genotype to reduce discordance in plasma metabolite profiles by modulating mitochondrial function
    • Armah C.N., et al. A diet rich in high-glucoraphanin broccoli interacts with genotype to reduce discordance in plasma metabolite profiles by modulating mitochondrial function. Am. J. Clin. Nutr. 2013, 98:712-722.
    • (2013) Am. J. Clin. Nutr. , vol.98 , pp. 712-722
    • Armah, C.N.1
  • 164
    • 84887239094 scopus 로고    scopus 로고
    • Metabolomic profiling of urine: response to a randomised, controlled feeding study of select fruits and vegetables, and application to an observational study
    • May D.H., et al. Metabolomic profiling of urine: response to a randomised, controlled feeding study of select fruits and vegetables, and application to an observational study. Br. J. Nutr. 2013, 110:1760-1770.
    • (2013) Br. J. Nutr. , vol.110 , pp. 1760-1770
    • May, D.H.1
  • 165
    • 84880682182 scopus 로고    scopus 로고
    • The Keap1-Nrf2 system prevents onset of diabetes mellitus
    • Uruno A., et al. The Keap1-Nrf2 system prevents onset of diabetes mellitus. Mol. Cell. Biol. 2013, 33:2996-3010.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2996-3010
    • Uruno, A.1
  • 166
    • 80053389113 scopus 로고    scopus 로고
    • Nrf2 represses FGF21 during long-term high-fat diet-induced obesity in mice
    • Chartoumpekis D.V., et al. Nrf2 represses FGF21 during long-term high-fat diet-induced obesity in mice. Diabetes 2011, 60:2465-2473.
    • (2011) Diabetes , vol.60 , pp. 2465-2473
    • Chartoumpekis, D.V.1
  • 167
    • 57349098220 scopus 로고    scopus 로고
    • Fibroblast growth factor 21 corrects obesity in mice
    • Coskun T., et al. Fibroblast growth factor 21 corrects obesity in mice. Endocrinology 2008, 149:6018-6027.
    • (2008) Endocrinology , vol.149 , pp. 6018-6027
    • Coskun, T.1
  • 168
    • 84964999321 scopus 로고    scopus 로고
    • Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration
    • Holmström K.M., et al. Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration. Biol. Open 2013, 2:761-770.
    • (2013) Biol. Open , vol.2 , pp. 761-770
    • Holmström, K.M.1
  • 169
    • 79952749190 scopus 로고    scopus 로고
    • NRF2 blockade suppresses colon tumor angiogenesis by inhibiting hypoxia-induced activation of HIF-1α
    • Kim T.H., et al. NRF2 blockade suppresses colon tumor angiogenesis by inhibiting hypoxia-induced activation of HIF-1α. Cancer Res. 2011, 71:2260-2275.
    • (2011) Cancer Res. , vol.71 , pp. 2260-2275
    • Kim, T.H.1
  • 170
    • 77957121798 scopus 로고    scopus 로고
    • Protective effect of sulforaphane against cisplatin-induced mitochondrial alterations and impairment in the activity of NAD(P)H: quinone oxidoreductase 1 and γ glutamyl cysteine ligase: studies in mitochondria isolated from rat kidney and in LLC-PK1 cells
    • Guerrero-Beltrán C.E., et al. Protective effect of sulforaphane against cisplatin-induced mitochondrial alterations and impairment in the activity of NAD(P)H: quinone oxidoreductase 1 and γ glutamyl cysteine ligase: studies in mitochondria isolated from rat kidney and in LLC-PK1 cells. Toxicol. Lett. 2010, 199:80-92.
    • (2010) Toxicol. Lett. , vol.199 , pp. 80-92
    • Guerrero-Beltrán, C.E.1
  • 171
    • 84877260204 scopus 로고    scopus 로고
    • Sulforaphane attenuates gentamicin-induced nephrotoxicity: role of mitochondrial protection
    • Negrette-Guzmán M., et al. Sulforaphane attenuates gentamicin-induced nephrotoxicity: role of mitochondrial protection. Evid. Based Complement. Alternat. Med. 2013, 2013:135314.
    • (2013) Evid. Based Complement. Alternat. Med. , vol.2013 , pp. 135314
    • Negrette-Guzmán, M.1
  • 172
    • 78751644875 scopus 로고    scopus 로고
    • Brain mitochondria from rats treated with sulforaphane are resistant to redox-regulated permeability transition
    • Greco T., Fiskum G. Brain mitochondria from rats treated with sulforaphane are resistant to redox-regulated permeability transition. J. Bioenerg. Biomembr. 2010, 42:491-497.
    • (2010) J. Bioenerg. Biomembr. , vol.42 , pp. 491-497
    • Greco, T.1    Fiskum, G.2
  • 173
    • 81855176066 scopus 로고    scopus 로고
    • Sulforaphane inhibits mitochondrial permeability transition and oxidative stress
    • Greco T., et al. Sulforaphane inhibits mitochondrial permeability transition and oxidative stress. Free Radic. Biol. Med. 2011, 51:2164-2171.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 2164-2171
    • Greco, T.1
  • 174
    • 84876031864 scopus 로고    scopus 로고
    • Dimers of mitochondrial ATP synthase form the permeability transition pore
    • Giorgio V., et al. Dimers of mitochondrial ATP synthase form the permeability transition pore. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:5887-5892.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5887-5892
    • Giorgio, V.1
  • 175
    • 84878003949 scopus 로고    scopus 로고
    • The transcription factor Nrf2 promotes survival by enhancing the expression of uncoupling protein 3 under conditions of oxidative stress
    • Anedda A., et al. The transcription factor Nrf2 promotes survival by enhancing the expression of uncoupling protein 3 under conditions of oxidative stress. Free Radic. Biol. Med. 2013, 61C:395-407.
    • (2013) Free Radic. Biol. Med. , vol.61 C , pp. 395-407
    • Anedda, A.1
  • 176
    • 57049142094 scopus 로고    scopus 로고
    • Metabolic flexibility and insulin resistance
    • Galgani J.E., et al. Metabolic flexibility and insulin resistance. Am. J. Physiol. Endocrinol. Metab. 2008, 295:E1009-E10017.
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.295
    • Galgani, J.E.1


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