메뉴 건너뛰기




Volumn 88, Issue Part B, 2015, Pages 147-157

Structural and functional characterization of Nrf2 degradation by glycogen synthase kinase 3/β-TrCP

Author keywords

Cell signaling; GSK 3; Nrf2; Oxidative stress; TrCP

Indexed keywords

AXIN; AXIN1 PROTEIN; BETA TRANSDUCIN REPEAT CONTAINING PROTEIN; G PROTEIN COUPLED RECEPTOR; GLYCOGEN SYNTHASE KINASE 3; IONOTROPIC RECEPTOR; KELCH LIKE ECH ASSOCIATED PROTEIN 1; METABOTROPIC RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; TRANSCRIPTION FACTOR NRF2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; WNT PROTEIN;

EID: 84970004975     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.04.029     Document Type: Review
Times cited : (213)

References (126)
  • 6
    • 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 Antioxidants & redox signaling 13 2010 1665 1678
    • (2010) Antioxidants & Redox Signaling , vol.13 , pp. 1665-1678
    • Itoh, K.1    Mimura, J.2    Yamamoto, M.3
  • 8
    • 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, J.D. Engel, and M. Yamamoto Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain Genes & development 13 1999 76 86
    • (1999) Genes & Development , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 10
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: Oxidative stress sensing by a Cul3-Keap1 ligase
    • S.B. Cullinan, J.D. Gordan, J. Jin, J.W. Harper, and J.A. Diehl The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase Molecular and cellular biology 24 2004 8477 8486
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 11
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • D.D. Zhang, S.C. Lo, J.V. Cross, D.J. Templeton, and M. Hannink Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex Molecular and cellular biology 24 2004 10941 10953
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 12
    • 84872850686 scopus 로고    scopus 로고
    • Keap1/Nrf2/ARE redox-sensitive signaling system as a pharmacological target
    • N.K. Zenkov, E.B. Menshchikova, and V.O. Tkachev Keap1/Nrf2/ARE redox-sensitive signaling system as a pharmacological target Biochemistry. Biokhimiia 78 2013 19 36
    • (2013) Biochemistry. Biokhimiia , vol.78 , pp. 19-36
    • Zenkov, N.K.1    Menshchikova, E.B.2    Tkachev, V.O.3
  • 16
    • 84863763926 scopus 로고    scopus 로고
    • Effect of graded Nrf2 activation on phase-I and -II drug metabolizing enzymes and transporters in mouse liver
    • K.C. Wu, J.Y. Cui, and C.D. Klaassen Effect of graded Nrf2 activation on phase-I and -II drug metabolizing enzymes and transporters in mouse liver PloS one 7 2012 e39006
    • (2012) PloS One , vol.7 , pp. e39006
    • Wu, K.C.1    Cui, J.Y.2    Klaassen, C.D.3
  • 18
    • 84885944468 scopus 로고    scopus 로고
    • The emerging role of the Nrf2-Keap1 signaling pathway in cancer
    • M.C. Jaramillo, and D.D. Zhang The emerging role of the Nrf2-Keap1 signaling pathway in cancer Genes & development 27 2013 2179 2191
    • (2013) Genes & Development , vol.27 , pp. 2179-2191
    • Jaramillo, M.C.1    Zhang, D.D.2
  • 19
    • 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
    • M. McMahon, N. Thomas, K. Itoh, M. Yamamoto, and J.D. Hayes 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 The Journal of biological chemistry 279 2004 31556 31567
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 31556-31567
    • McMahon, M.1    Thomas, N.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 22
    • 25844490465 scopus 로고    scopus 로고
    • The C. Elegans p38 MAPK pathway regulates nuclear localization of the transcription factor SKN-1 in oxidative stress response
    • H. Inoue, N. Hisamoto, J.H. An, R.P. Oliveira, E. Nishida, T.K. Blackwell, and K. Matsumoto The C. elegans p38 MAPK pathway regulates nuclear localization of the transcription factor SKN-1 in oxidative stress response Genes & development 19 2005 2278 2283
    • (2005) Genes & Development , vol.19 , pp. 2278-2283
    • Inoue, H.1    Hisamoto, N.2    An, J.H.3    Oliveira, R.P.4    Nishida, E.5    Blackwell, T.K.6    Matsumoto, K.7
  • 25
    • 0242666198 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression
    • D.A. Bloom, and 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 The Journal of biological chemistry 278 2003 44675 44682
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 44675-44682
    • Bloom, D.A.1    Jaiswal, A.K.2
  • 26
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • H.C. Huang, T. Nguyen, and C.B. Pickett Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription The Journal of biological chemistry 277 2002 42769 42774
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 42769-42774
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 27
    • 84874111758 scopus 로고    scopus 로고
    • The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation
    • H.K. Bryan, A. Olayanju, C.E. Goldring, and B.K. Park The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation Biochemical pharmacology 85 2013 705 717
    • (2013) Biochemical Pharmacology , vol.85 , pp. 705-717
    • Bryan, H.K.1    Olayanju, A.2    Goldring, C.E.3    Park, B.K.4
  • 30
    • 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
    • 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 Journal of biochemical and molecular toxicology 22 2008 63 76
    • (2008) Journal of Biochemical and Molecular Toxicology , vol.22 , pp. 63-76
    • Apopa, P.L.1    He, X.2    Ma, Q.3
  • 31
    • 34447526197 scopus 로고    scopus 로고
    • GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2
    • 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 The Journal of biological chemistry 282 2007 16502 16510
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 16502-16510
    • Jain, A.K.1    Jaiswal, A.K.2
  • 32
    • 80051690439 scopus 로고    scopus 로고
    • Src subfamily kinases regulate nuclear export and degradation of transcription factor Nrf2 to switch off Nrf2-mediated antioxidant activation of cytoprotective gene expression
    • S.K. Niture, A.K. Jain, P.M. Shelton, and A.K. Jaiswal Src subfamily kinases regulate nuclear export and degradation of transcription factor Nrf2 to switch off Nrf2-mediated antioxidant activation of cytoprotective gene expression The Journal of biological chemistry 286 2011 28821 28832
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 28821-28832
    • Niture, S.K.1    Jain, A.K.2    Shelton, P.M.3    Jaiswal, A.K.4
  • 34
    • 0038529681 scopus 로고    scopus 로고
    • Nerve growth factor protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner
    • M. Salinas, R. Diaz, N.G. Abraham, C.M. Ruiz de Galarreta, and A. Cuadrado Nerve growth factor protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner The Journal of biological chemistry 278 2003 13898 13904
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 13898-13904
    • Salinas, M.1    Diaz, R.2    Abraham, N.G.3    Ruiz De Galarreta, C.M.4    Cuadrado, A.5
  • 35
    • 0036436025 scopus 로고    scopus 로고
    • Peroxynitrite activates NF-E2-related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat glutathione S-transferase A2 induction
    • K.W. Kang, S.H. Choi, and S.G. Kim Peroxynitrite activates NF-E2-related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: the role of nitric oxide synthase in rat glutathione S-transferase A2 induction Nitric oxide: biology and chemistry / official journal of the Nitric Oxide Society 7 2002 244 253
    • (2002) Nitric Oxide: Biology and Chemistry / Official Journal of the Nitric Oxide Society , vol.7 , pp. 244-253
    • Kang, K.W.1    Choi, S.H.2    Kim, S.G.3
  • 37
    • 84923265392 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK3): Regulation, actions, and diseases
    • E. Beurel, S.F. Grieco, and R.S. Jope Glycogen synthase kinase-3 (GSK3): Regulation, actions, and diseases Pharmacology & therapeutics 148C 2015 114 131
    • (2015) Pharmacology & Therapeutics , vol.148 C , pp. 114-131
    • Beurel, E.1    Grieco, S.F.2    Jope, R.S.3
  • 40
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3 beta by phosphorylation: New kinase connections in insulin and growth-factor signalling
    • C. Sutherland, I.A. Leighton, and P. Cohen Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling The Biochemical journal 296 Pt 1 1993 15 19
    • (1993) The Biochemical Journal , vol.296 , Issue.PART 1 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 41
    • 0028177965 scopus 로고
    • The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro
    • C. Sutherland, and P. Cohen The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro FEBS letters 338 1994 37 42
    • (1994) FEBS Letters , vol.338 , pp. 37-42
    • Sutherland, C.1    Cohen, P.2
  • 42
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation
    • V. Stambolic, and J.R. Woodgett Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation The Biochemical journal 303 Pt 3 1994 701 704
    • (1994) The Biochemical Journal , vol.303 , Issue.PART 3 , pp. 701-704
    • Stambolic, V.1    Woodgett, J.R.2
  • 43
    • 0032746343 scopus 로고    scopus 로고
    • Role of protein kinase B and the MAP kinase cascade in mediating the EGF-dependent inhibition of glycogen synthase kinase 3 in Swiss 3T3 cells
    • M. Shaw, and P. Cohen Role of protein kinase B and the MAP kinase cascade in mediating the EGF-dependent inhibition of glycogen synthase kinase 3 in Swiss 3T3 cells FEBS letters 461 1999 120 124
    • (1999) FEBS Letters , vol.461 , pp. 120-124
    • Shaw, M.1    Cohen, P.2
  • 44
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • D.A. Cross, D.R. Alessi, P. Cohen, M. Andjelkovich, and B.A. Hemmings Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B Nature 378 1995 785 789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 46
    • 84884903877 scopus 로고    scopus 로고
    • Activator or inhibitor? GSK-3 as a new drug target
    • F. Takahashi-Yanaga Activator or inhibitor? GSK-3 as a new drug target Biochemical pharmacology 86 2013 191 199
    • (2013) Biochemical Pharmacology , vol.86 , pp. 191-199
    • Takahashi-Yanaga, F.1
  • 47
    • 0037044838 scopus 로고    scopus 로고
    • Ceramide and reactive oxygen species generated by H2O2 induce caspase-3-independent degradation of Akt/protein kinase B
    • D. Martin, M. Salinas, N. Fujita, T. Tsuruo, and A. Cuadrado Ceramide and reactive oxygen species generated by H2O2 induce caspase-3-independent degradation of Akt/protein kinase B The Journal of biological chemistry 277 2002 42943 42952
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 42943-42952
    • Martin, D.1    Salinas, M.2    Fujita, N.3    Tsuruo, T.4    Cuadrado, A.5
  • 48
    • 49749117926 scopus 로고    scopus 로고
    • Functional interference between glycogen synthase kinase-3 beta and the transcription factor Nrf2 in protection against kainate-induced hippocampal cell death
    • A.I. Rojo, P. Rada, J. Egea, A.O. Rosa, M.G. Lopez, and A. Cuadrado Functional interference between glycogen synthase kinase-3 beta and the transcription factor Nrf2 in protection against kainate-induced hippocampal cell death Molecular and cellular neurosciences 39 2008 125 132
    • (2008) Molecular and Cellular Neurosciences , vol.39 , pp. 125-132
    • Rojo, A.I.1    Rada, P.2    Egea, J.3    Rosa, A.O.4    Lopez, M.G.5    Cuadrado, A.6
  • 49
    • 33744950387 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2
    • 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 The Journal of biological chemistry 281 2006 14841 14851
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 14841-14851
    • Salazar, M.1    Rojo, A.I.2    Velasco, D.3    De Sagarra, R.M.4    Cuadrado, A.5
  • 51
    • 18944373186 scopus 로고    scopus 로고
    • Keap1 regulates the oxidation-sensitive shuttling of Nrf2 into and out of the nucleus via a Crm1-dependent nuclear export mechanism
    • M. Velichkova, and T. Hasson Keap1 regulates the oxidation-sensitive shuttling of Nrf2 into and out of the nucleus via a Crm1-dependent nuclear export mechanism Molecular and cellular biology 25 2005 4501 4513
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 4501-4513
    • Velichkova, M.1    Hasson, T.2
  • 52
    • 5444269904 scopus 로고    scopus 로고
    • Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition
    • B.P. Zhou, J. Deng, W. Xia, J. Xu, Y.M. Li, M. Gunduz, and M.C. Hung Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition Nature cell biology 6 2004 931 940
    • (2004) Nature Cell Biology , vol.6 , pp. 931-940
    • Zhou, B.P.1    Deng, J.2    Xia, W.3    Xu, J.4    Li, Y.M.5    Gunduz, M.6    Hung, M.C.7
  • 54
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin
    • E. Latres, D.S. Chiaur, and M. Pagano The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin Oncogene 18 1999 849 854
    • (1999) Oncogene , vol.18 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 55
    • 0032577899 scopus 로고    scopus 로고
    • WNT-1 and HGF regulate GSK3 beta activity and beta-catenin signaling in mammary epithelial cells
    • J. Papkoff, and M. Aikawa WNT-1 and HGF regulate GSK3 beta activity and beta-catenin signaling in mammary epithelial cells Biochemical and biophysical research communications 247 1998 851 858
    • (1998) Biochemical and Biophysical Research Communications , vol.247 , pp. 851-858
    • Papkoff, J.1    Aikawa, M.2
  • 56
    • 33646270662 scopus 로고    scopus 로고
    • Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation
    • Y. Pan, C.B. Bai, A.L. Joyner, and B. Wang Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation Molecular and cellular biology 26 2006 3365 3377
    • (2006) Molecular and Cellular Biology , vol.26 , pp. 3365-3377
    • Pan, Y.1    Bai, C.B.2    Joyner, A.L.3    Wang, B.4
  • 58
    • 0036774807 scopus 로고    scopus 로고
    • Regulated proteolysis of Xom mediates dorsoventral pattern formation during early Xenopus development
    • Z. Zhu, and M. Kirschner Regulated proteolysis of Xom mediates dorsoventral pattern formation during early Xenopus development Developmental cell 3 2002 557 568
    • (2002) Developmental Cell , vol.3 , pp. 557-568
    • Zhu, Z.1    Kirschner, M.2
  • 59
    • 37349094929 scopus 로고    scopus 로고
    • GSK-3 beta targets Cdc25A for ubiquitin-mediated proteolysis, and GSK-3 beta inactivation correlates with Cdc25A overproduction in human cancers
    • T. Kang, Y. Wei, Y. Honaker, H. Yamaguchi, E. Appella, M.C. Hung, and H. Piwnica-Worms GSK-3 beta targets Cdc25A for ubiquitin-mediated proteolysis, and GSK-3 beta inactivation correlates with Cdc25A overproduction in human cancers Cancer cell 13 2008 36 47
    • (2008) Cancer Cell , vol.13 , pp. 36-47
    • Kang, T.1    Wei, Y.2    Honaker, Y.3    Yamaguchi, H.4    Appella, E.5    Hung, M.C.6    Piwnica-Worms, H.7
  • 61
    • 41149122298 scopus 로고    scopus 로고
    • Novel insights into FGD3, a putative GEF for Cdc42, that undergoes SCF(FWD1/beta-TrCP)-mediated proteasomal degradation analogous to that of its homologue FGD1 but regulates cell morphology and motility differently from FGD1
    • M. Hayakawa, M. Matsushima, H. Hagiwara, T. Oshima, T. Fujino, K. Ando, K. Kikugawa, H. Tanaka, K. Miyazawa, and M. Kitagawa Novel insights into FGD3, a putative GEF for Cdc42, that undergoes SCF(FWD1/beta-TrCP)-mediated proteasomal degradation analogous to that of its homologue FGD1 but regulates cell morphology and motility differently from FGD1 Genes to cells: devoted to molecular & cellular mechanisms 13 2008 329 342
    • (2008) Genes to Cells: Devoted to Molecular & Cellular Mechanisms , vol.13 , pp. 329-342
    • Hayakawa, M.1    Matsushima, M.2    Hagiwara, H.3    Oshima, T.4    Fujino, T.5    Ando, K.6    Kikugawa, K.7    Tanaka, H.8    Miyazawa, K.9    Kitagawa, M.10
  • 65
    • 71949128142 scopus 로고    scopus 로고
    • Beta-TrCP-mediated ubiquitination and degradation of PHLPP1 are negatively regulated by Akt
    • X. Li, J. Liu, and T. Gao beta-TrCP-mediated ubiquitination and degradation of PHLPP1 are negatively regulated by Akt Molecular and cellular biology 29 2009 6192 6205
    • (2009) Molecular and Cellular Biology , vol.29 , pp. 6192-6205
    • Li, X.1    Liu, J.2    Gao, T.3
  • 66
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • R.M. Feldman, C.C. Correll, K.B. Kaplan, and R.J. Deshaies A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p Cell 91 1997 221 230
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 67
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • D. Skowyra, K.L. Craig, M. Tyers, S.J. Elledge, and J.W. Harper F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex Cell 91 1997 209 219
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 68
    • 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 Molecular and cellular biology 31 2011 1121 1133
    • (2011) Molecular and Cellular Biology , 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
  • 71
    • 73549095761 scopus 로고    scopus 로고
    • A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)
    • B. Zhao, L. Li, K. Tumaneng, C.Y. Wang, and K.L. Guan A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP) Genes & development 24 2010 72 85
    • (2010) Genes & Development , vol.24 , pp. 72-85
    • Zhao, B.1    Li, L.2    Tumaneng, K.3    Wang, C.Y.4    Guan, K.L.5
  • 72
    • 34250027624 scopus 로고    scopus 로고
    • Beta-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation
    • L. Meyer, B. Deau, H. Forejtnikova, D. Dumenil, F. Margottin-Goguet, C. Lacombe, P. Mayeux, and F. Verdier beta-Trcp mediates ubiquitination and degradation of the erythropoietin receptor and controls cell proliferation Blood 109 2007 5215 5222
    • (2007) Blood , vol.109 , pp. 5215-5222
    • Meyer, L.1    Deau, B.2    Forejtnikova, H.3    Dumenil, D.4    Margottin-Goguet, F.5    Lacombe, C.6    Mayeux, P.7    Verdier, F.8
  • 73
    • 84881476323 scopus 로고    scopus 로고
    • Nrf2 is controlled by two distinct beta-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity
    • S. Chowdhry, Y. Zhang, M. McMahon, C. Sutherland, A. Cuadrado, and J.D. Hayes Nrf2 is controlled by two distinct beta-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity Oncogene 32 2013 3765 3781
    • (2013) Oncogene , vol.32 , pp. 3765-3781
    • Chowdhry, S.1    Zhang, Y.2    McMahon, M.3    Sutherland, C.4    Cuadrado, A.5    Hayes, J.D.6
  • 74
    • 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
    • M. McMahon, N. Thomas, K. Itoh, M. Yamamoto, and J.D. Hayes 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 The Journal of biological chemistry 281 2006 24756 24768
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 24756-24768
    • McMahon, M.1    Thomas, N.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 75
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
    • 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 Biological chemistry 387 2006 1311 1320
    • (2006) Biological Chemistry , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 80
    • 0026808555 scopus 로고
    • Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes
    • N. Goode, K. Hughes, J.R. Woodgett, and P.J. Parker Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes The Journal of biological chemistry 267 1992 16878 16882
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 16878-16882
    • Goode, N.1    Hughes, K.2    Woodgett, J.R.3    Parker, P.J.4
  • 81
    • 0032563295 scopus 로고    scopus 로고
    • Activation of Akt/protein kinase B by G protein-coupled receptors. A role for alpha and beta gamma subunits of heterotrimeric G proteins acting through phosphatidylinositol-3-OH kinasegamma
    • C. Murga, L. Laguinge, R. Wetzker, A. Cuadrado, and J.S. Gutkind Activation of Akt/protein kinase B by G protein-coupled receptors. A role for alpha and beta gamma subunits of heterotrimeric G proteins acting through phosphatidylinositol-3-OH kinasegamma The Journal of biological chemistry 273 1998 19080 19085
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 19080-19085
    • Murga, C.1    Laguinge, L.2    Wetzker, R.3    Cuadrado, A.4    Gutkind, J.S.5
  • 82
    • 67650475217 scopus 로고    scopus 로고
    • The muscarinic M1 receptor activates Nrf2 through a signaling cascade that involves protein kinase C and inhibition of GSK-3beta: Connecting neurotransmission with neuroprotection
    • S. Espada, A.I. Rojo, M. Salinas, and A. Cuadrado The muscarinic M1 receptor activates Nrf2 through a signaling cascade that involves protein kinase C and inhibition of GSK-3beta: connecting neurotransmission with neuroprotection Journal of neurochemistry 110 2009 1107 1119
    • (2009) Journal of Neurochemistry , vol.110 , pp. 1107-1119
    • Espada, S.1    Rojo, A.I.2    Salinas, M.3    Cuadrado, A.4
  • 84
    • 37249031483 scopus 로고    scopus 로고
    • Gi-coupled P2Y-ADP receptor mediates GSK-3 phosphorylation and beta-catenin nuclear translocation in granule neurons
    • F. Ortega, R. Perez-Sen, and M.T. Miras-Portugal Gi-coupled P2Y-ADP receptor mediates GSK-3 phosphorylation and beta-catenin nuclear translocation in granule neurons Journal of neurochemistry 104 2008 62 73
    • (2008) Journal of Neurochemistry , vol.104 , pp. 62-73
    • Ortega, F.1    Perez-Sen, R.2    Miras-Portugal, M.T.3
  • 87
    • 0037695122 scopus 로고    scopus 로고
    • Human herpesvirus 8-encoded vGPCR activates nuclear factor of activated T cells and collaborates with human immunodeficiency virus type 1 Tat
    • S. Pati, J.S. Foulke Jr., O. Barabitskaya, J. Kim, B.C. Nair, D. Hone, J. Smart, R.A. Feldman, and M. Reitz Human herpesvirus 8-encoded vGPCR activates nuclear factor of activated T cells and collaborates with human immunodeficiency virus type 1 Tat Journal of virology 77 2003 5759 5773
    • (2003) Journal of Virology , vol.77 , pp. 5759-5773
    • Pati, S.1    Foulke, J.S.2    Barabitskaya, O.3    Kim, J.4    Nair, B.C.5    Hone, D.6    Smart, J.7    Feldman, R.A.8    Reitz, M.9
  • 88
    • 1942489300 scopus 로고    scopus 로고
    • Kaposi sarcoma-associated herpesvirus (KSHV) induces heme oxygenase-1 expression and activity in KSHV-infected endothelial cells
    • S.C. McAllister, S.G. Hansen, R.A. Ruhl, C.M. Raggo, V.R. DeFilippis, D. Greenspan, K. Fruh, and A.V. Moses Kaposi sarcoma-associated herpesvirus (KSHV) induces heme oxygenase-1 expression and activity in KSHV-infected endothelial cells Blood 103 2004 3465 3473
    • (2004) Blood , vol.103 , pp. 3465-3473
    • McAllister, S.C.1    Hansen, S.G.2    Ruhl, R.A.3    Raggo, C.M.4    DeFilippis, V.R.5    Greenspan, D.6    Fruh, K.7    Moses, A.V.8
  • 90
    • 33744961436 scopus 로고    scopus 로고
    • Inhibition of heme oxygenase-1 interferes with the transforming activity of the Kaposi sarcoma herpesvirus-encoded G protein-coupled receptor
    • M.J. Marinissen, T. Tanos, M. Bolos, M.R. de Sagarra, O.A. Coso, and A. Cuadrado Inhibition of heme oxygenase-1 interferes with the transforming activity of the Kaposi sarcoma herpesvirus-encoded G protein-coupled receptor The Journal of biological chemistry 281 2006 11332 11346
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 11332-11346
    • Marinissen, M.J.1    Tanos, T.2    Bolos, M.3    De Sagarra, M.R.4    Coso, O.A.5    Cuadrado, A.6
  • 91
    • 36348990322 scopus 로고    scopus 로고
    • The Galpha12/13 family of heterotrimeric G proteins and the small GTPase RhoA link the Kaposi sarcoma-associated herpes virus G protein-coupled receptor to heme oxygenase-1 expression and tumorigenesis
    • M.J. Martin, T. Tanos, A.B. Garcia, D. Martin, J.S. Gutkind, O.A. Coso, and M.J. Marinissen The Galpha12/13 family of heterotrimeric G proteins and the small GTPase RhoA link the Kaposi sarcoma-associated herpes virus G protein-coupled receptor to heme oxygenase-1 expression and tumorigenesis The Journal of biological chemistry 282 2007 34510 34524
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 34510-34524
    • Martin, M.J.1    Tanos, T.2    Garcia, A.B.3    Martin, D.4    Gutkind, J.S.5    Coso, O.A.6    Marinissen, M.J.7
  • 92
    • 84901716846 scopus 로고    scopus 로고
    • Transcription factors Nrf2 and NF-kappaB are coordinated effectors of the Rho family, GTP-binding protein RAC1 during inflammation
    • A. Cuadrado, Z. Martin-Moldes, J. Ye, and I. Lastres-Becker Transcription factors Nrf2 and NF-kappaB are coordinated effectors of the Rho family, GTP-binding protein RAC1 during inflammation The Journal of biological chemistry 289 2014 15244 15258
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 15244-15258
    • Cuadrado, A.1    Martin-Moldes, Z.2    Ye, J.3    Lastres-Becker, I.4
  • 93
    • 77956265332 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1/CC chemokine ligand 2 enhances apoptotic cell removal by macrophages through Rac1 activation
    • T. Tanaka, M. Terada, K. Ariyoshi, and K. Morimoto Monocyte chemoattractant protein-1/CC chemokine ligand 2 enhances apoptotic cell removal by macrophages through Rac1 activation Biochemical and biophysical research communications 399 2010 677 682
    • (2010) Biochemical and Biophysical Research Communications , vol.399 , pp. 677-682
    • Tanaka, T.1    Terada, M.2    Ariyoshi, K.3    Morimoto, K.4
  • 94
    • 79956207794 scopus 로고    scopus 로고
    • MEKK3 regulates IFN-gamma production in T cells through the Rac1/2-dependent MAPK cascades
    • X. Wang, F. Zhang, F. Chen, D. Liu, Y. Zheng, Y. Zhang, C. Dong, and B. Su MEKK3 regulates IFN-gamma production in T cells through the Rac1/2-dependent MAPK cascades Journal of immunology 186 2011 5791 5800
    • (2011) Journal of Immunology , vol.186 , pp. 5791-5800
    • Wang, X.1    Zhang, F.2    Chen, F.3    Liu, D.4    Zheng, Y.5    Zhang, Y.6    Dong, C.7    Su, B.8
  • 95
    • 79955671904 scopus 로고    scopus 로고
    • Stimulating nicotinic receptors trigger multiple pathways attenuating cytotoxicity in models of Alzheimers and Parkinsons diseases
    • J. Kawamata, and S. Shimohama Stimulating nicotinic receptors trigger multiple pathways attenuating cytotoxicity in models of Alzheimers and Parkinsons diseases Journal of Alzheimers disease: JAD 24 Suppl 2 2011 95 109
    • (2011) Journal of Alzheimers Disease: JAD , vol.24 , pp. 95-109
    • Kawamata, J.1    Shimohama, S.2
  • 96
    • 75049085215 scopus 로고    scopus 로고
    • Mechanisms of neuroprotective effects of nicotine and acetylcholinesterase inhibitors: Role of alpha4 and alpha7 receptors in neuroprotection
    • A. Akaike, Y. Takada-Takatori, T. Kume, and Y. Izumi Mechanisms of neuroprotective effects of nicotine and acetylcholinesterase inhibitors: role of alpha4 and alpha7 receptors in neuroprotection Journal of molecular neuroscience: MN 40 2010 211 216
    • (2010) Journal of Molecular Neuroscience: MN , vol.40 , pp. 211-216
    • Akaike, A.1    Takada-Takatori, Y.2    Kume, T.3    Izumi, Y.4
  • 97
    • 62949084265 scopus 로고    scopus 로고
    • Selective alpha7 nicotinic acetylcholine receptor activation regulates glycogen synthase kinase3beta and decreases tau phosphorylation in vivo
    • R.S. Bitner, A.L. Nikkel, S. Markosyan, S. Otte, P. Puttfarcken, and M. Gopalakrishnan Selective alpha7 nicotinic acetylcholine receptor activation regulates glycogen synthase kinase3beta and decreases tau phosphorylation in vivo Brain research 1265 2009 65 74
    • (2009) Brain Research , vol.1265 , pp. 65-74
    • Bitner, R.S.1    Nikkel, A.L.2    Markosyan, S.3    Otte, S.4    Puttfarcken, P.5    Gopalakrishnan, M.6
  • 98
    • 84882642320 scopus 로고    scopus 로고
    • The microglial alpha7-acetylcholine nicotinic receptor is a key element in promoting neuroprotection by inducing heme oxygenase-1 via nuclear factor erythroid-2-related factor 2
    • E. Parada, J. Egea, I. Buendia, P. Negredo, A.C. Cunha, S. Cardoso, M.P. Soares, and M.G. Lopez The microglial alpha7-acetylcholine nicotinic receptor is a key element in promoting neuroprotection by inducing heme oxygenase-1 via nuclear factor erythroid-2-related factor 2 Antioxidants & redox signaling 19 2013 1135 1148
    • (2013) Antioxidants & Redox Signaling , vol.19 , pp. 1135-1148
    • Parada, E.1    Egea, J.2    Buendia, I.3    Negredo, P.4    Cunha, A.C.5    Cardoso, S.6    Soares, M.P.7    Lopez, M.G.8
  • 99
    • 84893752602 scopus 로고    scopus 로고
    • Neuroprotective effect of melatonin against ischemia is partially mediated by alpha-7 nicotinic receptor modulation and HO-1 overexpression
    • E. Parada, I. Buendia, R. Leon, P. Negredo, A. Romero, A. Cuadrado, M.G. Lopez, and J. Egea Neuroprotective effect of melatonin against ischemia is partially mediated by alpha-7 nicotinic receptor modulation and HO-1 overexpression Journal of pineal research 56 2014 204 212
    • (2014) Journal of Pineal Research , vol.56 , pp. 204-212
    • Parada, E.1    Buendia, I.2    Leon, R.3    Negredo, P.4    Romero, A.5    Cuadrado, A.6    Lopez, M.G.7    Egea, J.8
  • 102
    • 0029800090 scopus 로고    scopus 로고
    • Zonation of parenchymal and nonparenchymal metabolism in liver
    • K. Jungermann, and T. Kietzmann Zonation of parenchymal and nonparenchymal metabolism in liver Annual review of nutrition 16 1996 179 203
    • (1996) Annual Review of Nutrition , vol.16 , pp. 179-203
    • Jungermann, K.1    Kietzmann, T.2
  • 103
    • 84900553531 scopus 로고    scopus 로고
    • Role and regulation of beta-catenin signaling during physiological liver growth
    • S.P. Monga Role and regulation of beta-catenin signaling during physiological liver growth Gene expression 16 2014 51 62
    • (2014) Gene Expression , vol.16 , pp. 51-62
    • Monga, S.P.1
  • 110
    • 1542335553 scopus 로고    scopus 로고
    • Regulation of heme oxygenase-1 expression through the phosphatidylinositol 3-kinase/Akt pathway and the Nrf2 transcription factor in response to the antioxidant phytochemical carnosol
    • D. Martin, A.I. Rojo, M. Salinas, R. Diaz, G. Gallardo, J. Alam, C.M. De Galarreta, and A. Cuadrado Regulation of heme oxygenase-1 expression through the phosphatidylinositol 3-kinase/Akt pathway and the Nrf2 transcription factor in response to the antioxidant phytochemical carnosol The Journal of biological chemistry 279 2004 8919 8929
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 8919-8929
    • Martin, D.1    Rojo, A.I.2    Salinas, M.3    Diaz, R.4    Gallardo, G.5    Alam, J.6    De Galarreta, C.M.7    Cuadrado, A.8
  • 111
    • 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
    • I. Pitha-Rowe, K. Liby, D. Royce, and M. Sporn Synthetic triterpenoids attenuate cytotoxic retinal injury: cross-talk between Nrf2 and PI3K/AKT signaling through inhibition of the lipid phosphatase PTEN Investigative ophthalmology & visual science 50 2009 5339 5347
    • (2009) Investigative Ophthalmology & Visual Science , vol.50 , pp. 5339-5347
    • Pitha-Rowe, I.1    Liby, K.2    Royce, D.3    Sporn, M.4
  • 112
    • 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, S. Espada, J. Pedraza-Chaverri, and A. Cuadrado Signaling pathways activated by the phytochemical nordihydroguaiaretic acid contribute to a Keap1-independent regulation of Nrf2 stability: Role of glycogen synthase kinase-3 Free radical biology & medicine 52 2012 473 487
    • (2012) Free Radical Biology & Medicine , 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    Pedraza-Chaverri, J.7    Cuadrado, A.8
  • 114
    • 84898650544 scopus 로고    scopus 로고
    • Isoquercitrin inhibits the progression of liver cancer in vivo and in vitro via the MAPK signalling pathway
    • G. Huang, B. Tang, K. Tang, X. Dong, J. Deng, L. Liao, Z. Liao, H. Yang, and S. He Isoquercitrin inhibits the progression of liver cancer in vivo and in vitro via the MAPK signalling pathway Oncology reports 31 2014 2377 2384
    • (2014) Oncology Reports , vol.31 , pp. 2377-2384
    • Huang, G.1    Tang, B.2    Tang, K.3    Dong, X.4    Deng, J.5    Liao, L.6    Liao, Z.7    Yang, H.8    He, S.9
  • 116
    • 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 Biochemical and biophysical research communications 331 2005 993 1000
    • (2005) Biochemical and Biophysical Research Communications , vol.331 , pp. 993-1000
    • Chen, C.Y.1    Jang, J.H.2    Li, M.H.3    Surh, Y.J.4
  • 117
    • 37649023810 scopus 로고    scopus 로고
    • Upregulation of heme oxygenase-1 by brazilin via the phosphatidylinositol 3-kinase/Akt and ERK pathways and its protective effect against oxidative injury
    • B.M. Choi, and B.R. Kim Upregulation of heme oxygenase-1 by brazilin via the phosphatidylinositol 3-kinase/Akt and ERK pathways and its protective effect against oxidative injury European journal of pharmacology 580 2008 12 18
    • (2008) European Journal of Pharmacology , vol.580 , pp. 12-18
    • Choi, B.M.1    Kim, B.R.2
  • 118
    • 48049089409 scopus 로고    scopus 로고
    • (-)-Epigallocatechin gallate induces Nrf2-mediated antioxidant enzyme expression via activation of PI3K and ERK in human mammary epithelial cells
    • H.K. Na, E.H. Kim, J.H. Jung, H.H. Lee, J.W. Hyun, and Y.J. Surh (-)-Epigallocatechin gallate induces Nrf2-mediated antioxidant enzyme expression via activation of PI3K and ERK in human mammary epithelial cells Archives of biochemistry and biophysics 476 2008 171 177
    • (2008) Archives of Biochemistry and Biophysics , vol.476 , pp. 171-177
    • Na, H.K.1    Kim, E.H.2    Jung, J.H.3    Lee, H.H.4    Hyun, J.W.5    Surh, Y.J.6
  • 119
    • 46749135955 scopus 로고    scopus 로고
    • The coffee diterpene kahweol induces heme oxygenase-1 via the PI3K and p38/Nrf2 pathway to protect human dopaminergic neurons from 6-hydroxydopamine-derived oxidative stress
    • Y.P. Hwang, and H.G. Jeong The coffee diterpene kahweol induces heme oxygenase-1 via the PI3K and p38/Nrf2 pathway to protect human dopaminergic neurons from 6-hydroxydopamine-derived oxidative stress FEBS letters 582 2008 2655 2662
    • (2008) FEBS Letters , vol.582 , pp. 2655-2662
    • Hwang, Y.P.1    Jeong, H.G.2
  • 120
    • 84873148285 scopus 로고    scopus 로고
    • Redox regulation of tumor suppressor PTEN in cancer and aging (Review)
    • Y. Kitagishi, and S. Matsuda Redox regulation of tumor suppressor PTEN in cancer and aging (Review) International journal of molecular medicine 31 2013 511 515
    • (2013) International Journal of Molecular Medicine , vol.31 , pp. 511-515
    • Kitagishi, Y.1    Matsuda, S.2
  • 122
    • 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
    • A.L. Levonen, A. Landar, A. Ramachandran, E.K. Ceaser, D.A. Dickinson, G. Zanoni, J.D. Morrow, and V.M. Darley-Usmar Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products The Biochemical journal 378 2004 373 382
    • (2004) The Biochemical Journal , vol.378 , 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
  • 123
    • 84897421970 scopus 로고    scopus 로고
    • The Nrf2 regulatory network provides an interface between redox and intermediary metabolism
    • J.D. Hayes, and A.T. Dinkova-Kostova The Nrf2 regulatory network provides an interface between redox and intermediary metabolism Trends in biochemical sciences 39 2014 199 218
    • (2014) Trends in Biochemical Sciences , vol.39 , pp. 199-218
    • Hayes, J.D.1    Dinkova-Kostova, A.T.2
  • 124
    • 84864348569 scopus 로고    scopus 로고
    • Nrf2 and cancer: The good, the bad and the importance of context
    • M.B. Sporn, and K.T. Liby Nrf2 and cancer: the good, the bad and the importance of context Nature reviews. Cancer 12 2012 564 571
    • (2012) Nature Reviews. Cancer , vol.12 , pp. 564-571
    • Sporn, M.B.1    Liby, K.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.