메뉴 건너뛰기




Volumn 26, Issue 1, 2015, Pages 47-57

An overview of the molecular mechanisms and novel roles of Nrf2 in neurodegenerative disorders

Author keywords

Cerebrum actions; Molecular mechanisms; Neurodegenerative disorders; Nuclear factor erythroid 2 related factor 2

Indexed keywords

2 CYANO 3,12 DIOXOOLEANA 1,9 (11) DIEN 28 OIC ACID; 2 CYANO 3,12 DIOXOOLEANA 1,9 (11) DIEN 28 OIC ACID ETHYL AMIDE; 2 CYANO 3,12 DIOXOOLEANA 1,9 (11) DIEN 28 OIC ACID IMIDAZOLIDE; 2 CYANO 3,12 DIOXOOLEANA 1,9 (11) DIEN 28 OIC ACID METHYL AMIDE; 2 CYANO 3,12 DIOXOOLEANA 1,9 (11) DIEN 28 OIC ACID TRIFLUOROETHYL AMIDE; ANTIOXIDANT; CULLIN; CYCLIN DEPENDENT KINASE INHIBITOR 1; GLYCOGEN SYNTHASE KINASE 3BETA; HEME OXYGENASE 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 6; KELCH LIKE ECH ASSOCIATED PROTEIN 1; MANGIFERIN; N [4 [2 PYRIDYL] [1,3 THIAZOL 2 YL]] 2 (2,4,6 TRIMETHYLPHENOXY) ACETAMIDE; N,N DIMETHYLFORMAMIDE; PROTEIN KINASE C; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; RING BOX 1 PROTEIN; STRATIFIN; THIOREDOXIN REDUCTASE 1; TRANSCRIPTION FACTOR MAF; TRANSCRIPTION FACTOR NRF2; TRITERPENOID; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84923028459     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.09.002     Document Type: Short Survey
Times cited : (71)

References (99)
  • 1
    • 84867777145 scopus 로고    scopus 로고
    • The Nrf2-ARE pathway: a valuable therapeutic target for the treatment of neurodegenerative diseases
    • Joshi G., Johnson J.A. The Nrf2-ARE pathway: a valuable therapeutic target for the treatment of neurodegenerative diseases. Recent Pat CNS Drug Discov 2012, 7:218-229.
    • (2012) Recent Pat CNS Drug Discov , vol.7 , pp. 218-229
    • Joshi, G.1    Johnson, J.A.2
  • 2
    • 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., Chiba T., Takahashi S., Ishii T., Igarashi K., Katoh Y., 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    Chiba, T.2    Takahashi, S.3    Ishii, T.4    Igarashi, K.5    Katoh, Y.6
  • 3
    • 84891600336 scopus 로고    scopus 로고
    • NRF2-regulation in brain health and disease: implication of cerebral inflammation
    • Sandberg M., Patil J., D'Angelo B., Weber S.G., Mallard C. NRF2-regulation in brain health and disease: implication of cerebral inflammation. Neuropharmacology 2014, 79:298-306.
    • (2014) Neuropharmacology , vol.79 , pp. 298-306
    • Sandberg, M.1    Patil, J.2    D'Angelo, B.3    Weber, S.G.4    Mallard, C.5
  • 4
    • 84870902532 scopus 로고    scopus 로고
    • Emerging roles of Nrf2 and phase II antioxidant enzymes in neuroprotection
    • Zhang M., An C., Gao Y., Leak R.K., Chen J., Zhang F. Emerging roles of Nrf2 and phase II antioxidant enzymes in neuroprotection. Prog Neurobiol 2013, 100:30-47.
    • (2013) Prog Neurobiol , vol.100 , pp. 30-47
    • Zhang, M.1    An, C.2    Gao, Y.3    Leak, R.K.4    Chen, J.5    Zhang, F.6
  • 5
    • 84888821265 scopus 로고    scopus 로고
    • Lack of Nrf2 results in progression of proliferative lesions to neoplasms induced by long-term exposure to non-genotoxic hepatocarcinogens involving oxidative stress
    • Tasaki M., Kuroiwa Y., Inoue T., Hibi D., Matsushita K., Kijima A., et al. Lack of Nrf2 results in progression of proliferative lesions to neoplasms induced by long-term exposure to non-genotoxic hepatocarcinogens involving oxidative stress. Exp Toxicol Pathol 2014, 6:19-26.
    • (2014) Exp Toxicol Pathol , vol.6 , pp. 19-26
    • Tasaki, M.1    Kuroiwa, Y.2    Inoue, T.3    Hibi, D.4    Matsushita, K.5    Kijima, A.6
  • 6
    • 84939882297 scopus 로고    scopus 로고
    • Lagerstroemia speciosa L, attenuates apoptosis in isoproterenol-induced cardiotoxic mice by inhibiting oxidative stress: possible role of Nrf2/HO-1
    • [Epub ahead of print]
    • Sahu B.D., Kuncha M., Rachamalla S.S., Sistla R. Lagerstroemia speciosa L, attenuates apoptosis in isoproterenol-induced cardiotoxic mice by inhibiting oxidative stress: possible role of Nrf2/HO-1. Cardiovasc Toxicol 2014, [Epub ahead of print].
    • (2014) Cardiovasc Toxicol
    • Sahu, B.D.1    Kuncha, M.2    Rachamalla, S.S.3    Sistla, R.4
  • 7
    • 84900422389 scopus 로고    scopus 로고
    • The synthetic triterpenoid RTA dh404 (CDDO-dhTFEA) restores Nrf2 activity and attenuates oxidative stress, inflammation, and fibrosis in rats with chronic kidney disease
    • Aminzadeh M.A., Reisman S.A., Vaziri N.D., Khazaeli M., Yuan J., Meyer C.J. The synthetic triterpenoid RTA dh404 (CDDO-dhTFEA) restores Nrf2 activity and attenuates oxidative stress, inflammation, and fibrosis in rats with chronic kidney disease. Xenobiotica 2014, 44:570-578.
    • (2014) Xenobiotica , vol.44 , pp. 570-578
    • Aminzadeh, M.A.1    Reisman, S.A.2    Vaziri, N.D.3    Khazaeli, M.4    Yuan, J.5    Meyer, C.J.6
  • 8
    • 84883641346 scopus 로고    scopus 로고
    • Nrf2 deficiency induces oxidative stress and promotes RANKL-induced osteoclast differentiation
    • Hyeon S., Lee H., Yang Y., Jeong W. Nrf2 deficiency induces oxidative stress and promotes RANKL-induced osteoclast differentiation. Free Radic Biol Med 2013, 65:789-799.
    • (2013) Free Radic Biol Med , vol.65 , pp. 789-799
    • Hyeon, S.1    Lee, H.2    Yang, Y.3    Jeong, W.4
  • 9
    • 84923058292 scopus 로고    scopus 로고
    • Glutathione protects brain endothelial cells from hydrogen peroxide-induced oxidative stress by increasing nrf2 expression
    • Song J., Kang S.M., Lee W.T., Park K.A., Lee K.M., Lee J.E. Glutathione protects brain endothelial cells from hydrogen peroxide-induced oxidative stress by increasing nrf2 expression. Exp Neurobiol 2014, 23:93-103.
    • (2014) Exp Neurobiol , vol.23 , pp. 93-103
    • Song, J.1    Kang, S.M.2    Lee, W.T.3    Park, K.A.4    Lee, K.M.5    Lee, J.E.6
  • 10
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A., Kang M.I., Okawa H., Ohtsuji M., Zenke Y., Chiba T., et al. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol Cell Biol 2004, 24:7130-7139.
    • (2004) Mol Cell Biol , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6
  • 11
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M. Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J Biol Chem 2005, 280:30091-30099.
    • (2005) J Biol Chem , vol.280 , pp. 30091-30099
    • Zhang, D.D.1    Lo, S.C.2    Sun, Z.3    Habib, G.M.4    Lieberman, M.W.5    Hannink, M.6
  • 12
    • 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
  • 13
    • 33747728194 scopus 로고    scopus 로고
    • Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: a two-site interaction model for the Nrf2-Keap1 complex
    • McMahon M., Thomas N., Itoh K., Yamamoto M., Hayes J.D. Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: a two-site interaction model for the Nrf2-Keap1 complex. J Biol Chem 2006, 281:24756-24768.
    • (2006) J Biol Chem , vol.281 , pp. 24756-24768
    • McMahon, M.1    Thomas, N.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 14
    • 22544464124 scopus 로고    scopus 로고
    • Modifying specific cysteines of the electrophilie-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2
    • Eggler A.L., Liu G., Pezzuto J.M., van Breemen R.B., Mesecar A.D. Modifying specific cysteines of the electrophilie-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc Natl Acad SCi USA 2005, 102:10070-10075.
    • (2005) Proc Natl Acad SCi USA , vol.102 , pp. 10070-10075
    • Eggler, A.L.1    Liu, G.2    Pezzuto, J.M.3    van Breemen, R.B.4    Mesecar, A.D.5
  • 15
    • 0037183998 scopus 로고    scopus 로고
    • The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
    • Zipper L.M., Mulcahy R.T. The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm. J Biol Chem 2002, 277:36544-36552.
    • (2002) J Biol Chem , vol.277 , pp. 36544-36552
    • Zipper, L.M.1    Mulcahy, R.T.2
  • 16
    • 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
    • Levonen A.L., Landar A., Ramachandran A., Ceaser E.K., Dickinson D.A., Zanoni G., et al. Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem J 2004, 378:373-382.
    • (2004) Biochem J , 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
  • 17
    • 34047273206 scopus 로고    scopus 로고
    • Novel n-3 fatty acid oxidation products activate Nrf2 by destabilizing the association between Keap1 and Cullin3
    • Gao L., Wang J., Sekhar K.R., Yin H., Yared N.F., Schneider S.N., et al. Novel n-3 fatty acid oxidation products activate Nrf2 by destabilizing the association between Keap1 and Cullin3. J Biol Chem 2007, 282:2529-2537.
    • (2007) J Biol Chem , vol.282 , pp. 2529-2537
    • Gao, L.1    Wang, J.2    Sekhar, K.R.3    Yin, H.4    Yared, N.F.5    Schneider, S.N.6
  • 18
    • 44049093741 scopus 로고    scopus 로고
    • Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2
    • Theodore M., Kawai Y., Yang J., Kleshchenko Y., Reddy S.P., Villalta F., et al. Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2. J Biol Chem 2008, 283:8984-8994.
    • (2008) J Biol Chem , vol.283 , pp. 8984-8994
    • Theodore, M.1    Kawai, Y.2    Yang, J.3    Kleshchenko, Y.4    Reddy, S.P.5    Villalta, F.6
  • 19
    • 59849113546 scopus 로고    scopus 로고
    • Molecular mechanisms of Nrf2-mediated antioxidant response
    • Li W., Kong A.N. Molecular mechanisms of Nrf2-mediated antioxidant response. Mol Carcinog 2009, 48:91-104.
    • (2009) Mol Carcinog , vol.48 , pp. 91-104
    • Li, W.1    Kong, A.N.2
  • 20
    • 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
    • Bloom D.A., Jaiswal A.K. Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression. J Biol Chem 2003, 278:44675-44682.
    • (2003) J Biol Chem , vol.278 , pp. 44675-44682
    • Bloom, D.A.1    Jaiswal, A.K.2
  • 21
    • 0025948113 scopus 로고
    • The antioxidant responsive element Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore T.H., Morton M.R., Pickett C.B. The antioxidant responsive element Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem 1991, 266:11632-11639.
    • (1991) J Biol Chem , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 22
    • 40049088820 scopus 로고    scopus 로고
    • The Nrf2-Keap1 defense pathway: role in protection against drug-induced toxicity
    • Copple I.M., Goldring C.E., Kitteringham N.R., Park B.K. The Nrf2-Keap1 defense pathway: role in protection against drug-induced toxicity. Toxicology 2008, 246:24-33.
    • (2008) Toxicology , vol.246 , pp. 24-33
    • Copple, I.M.1    Goldring, C.E.2    Kitteringham, N.R.3    Park, B.K.4
  • 23
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., Kensler T.W. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol Cell Biol 2003, 23:8786-8794.
    • (2003) Mol Cell Biol , vol.23 , pp. 8786-8794
    • Kwak, M.K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 24
    • 77954374004 scopus 로고    scopus 로고
    • An autoregulatory loop between Nrf2 and Cul3-Rbx1 controls their cellular abundance
    • Kaspar J.W., Jaiswal A.K. An autoregulatory loop between Nrf2 and Cul3-Rbx1 controls their cellular abundance. J Biol Chem 2010, 285:21349-21358.
    • (2010) J Biol Chem , vol.285 , pp. 21349-21358
    • Kaspar, J.W.1    Jaiswal, A.K.2
  • 25
    • 84866283856 scopus 로고    scopus 로고
    • Structural and functional characterization of Nrf2 degradation by the glycogen synthase kinase 3/beta-TrCP axis
    • Rada P., Rojo A.I., Evrard-Todeschi N., Innamorato N.G., Cotte A., Jaworski T., et al. Structural and functional characterization of Nrf2 degradation by the glycogen synthase kinase 3/beta-TrCP axis. Mol Cell Biol 2012, 32:3486-3499.
    • (2012) Mol Cell Biol , vol.32 , pp. 3486-3499
    • Rada, P.1    Rojo, A.I.2    Evrard-Todeschi, N.3    Innamorato, N.G.4    Cotte, A.5    Jaworski, T.6
  • 26
    • 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
    • Jain A.K., Jaiswal A.K. GSK-3beta 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
  • 27
    • 67649415378 scopus 로고    scopus 로고
    • Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2
    • Niture S.K., Jaiswal A.K. Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2. J Biol Chem 2009, 284:13856-13868.
    • (2009) J Biol Chem , vol.284 , pp. 13856-13868
    • Niture, S.K.1    Jaiswal, A.K.2
  • 28
    • 67449128222 scopus 로고    scopus 로고
    • Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response
    • Chen W., Sun Z., Wang X.J., Jiang T., Huang Z., Fang D., 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    Sun, Z.2    Wang, X.J.3    Jiang, T.4    Huang, Z.5    Fang, D.6
  • 29
    • 84883830467 scopus 로고    scopus 로고
    • Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy
    • Ichimura Y., Waguri S., Sou Y.S., Kageyama S., Hasegawa J., Ishimura R., 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    Waguri, S.2    Sou, Y.S.3    Kageyama, S.4    Hasegawa, J.5    Ishimura, R.6
  • 30
    • 81155126130 scopus 로고    scopus 로고
    • Novel insights into the regulation of antioxidant-response-element-mediated gene expression by electrophiles: induction of the transcriptional repressor BACH1 by Nrf2
    • Jyrkkanen H.K., Kuosmanen S., Heinaniemi M., Laitinen H., Kansanen E., Mella-Aho E., et al. Novel insights into the regulation of antioxidant-response-element-mediated gene expression by electrophiles: induction of the transcriptional repressor BACH1 by Nrf2. Biochem J 2011, 440:167-174.
    • (2011) Biochem J , vol.440 , pp. 167-174
    • Jyrkkanen, H.K.1    Kuosmanen, S.2    Heinaniemi, M.3    Laitinen, H.4    Kansanen, E.5    Mella-Aho, E.6
  • 31
    • 84887899587 scopus 로고    scopus 로고
    • PI3K/Akt pathway mediates Nrf2/ARE activation in human L02 hepatocytes exposed to low-concentration HBCDs
    • Zou W., Chen C., Zhong Y., An J., Zhang X., Yu Y., et al. PI3K/Akt pathway mediates Nrf2/ARE activation in human L02 hepatocytes exposed to low-concentration HBCDs. Environ Sci Technol 2013, 47:12434-12440.
    • (2013) Environ Sci Technol , vol.47 , pp. 12434-12440
    • Zou, W.1    Chen, C.2    Zhong, Y.3    An, J.4    Zhang, X.5    Yu, Y.6
  • 32
    • 84885598853 scopus 로고    scopus 로고
    • P90RSK and Nrf2 activation via MEK1/2-ERK1/2 pathways mediated by notoginsenoside R2 to prevent 6-hydroxydopamine-induced apoptotic death in SH-SY5Y cells
    • Meng X.B., Sun G.B., Wang M., Sun J., Qin M., Sun X.B. P90RSK and Nrf2 activation via MEK1/2-ERK1/2 pathways mediated by notoginsenoside R2 to prevent 6-hydroxydopamine-induced apoptotic death in SH-SY5Y cells. Evid Based Complement Alternat Med 2013, 2013:971712.
    • (2013) Evid Based Complement Alternat Med , vol.2013 , pp. 971712
    • Meng, X.B.1    Sun, G.B.2    Wang, M.3    Sun, J.4    Qin, M.5    Sun, X.B.6
  • 34
    • 84879793030 scopus 로고    scopus 로고
    • Epigenetic modifications of Nrf2 by 3,3'-diindolylmethane in vitro in TRAMP C1 cell line and in vivo TRAMP prostate tumors
    • Wu T.Y., Khor T.O., Su Z.Y., Saw C.L., Shu L., Cheung K.L., et al. Epigenetic modifications of Nrf2 by 3,3'-diindolylmethane in vitro in TRAMP C1 cell line and in vivo TRAMP prostate tumors. AAPS J 2013, 15:864-874.
    • (2013) AAPS J , vol.15 , pp. 864-874
    • Wu, T.Y.1    Khor, T.O.2    Su, Z.Y.3    Saw, C.L.4    Shu, L.5    Cheung, K.L.6
  • 35
    • 84903270398 scopus 로고    scopus 로고
    • Oxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases
    • Gan L., Johnson J.A. Oxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases. Biochim Biophys Acta 2013, 1842:1208-1218.
    • (2013) Biochim Biophys Acta , vol.1842 , pp. 1208-1218
    • Gan, L.1    Johnson, J.A.2
  • 36
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in Nrf2 transcription factor-deficient mice
    • Ramos-Gomez M., Kwak M.K., Dolan P.M., Itoh K., Yamamoto M., Talalay P., et al. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in Nrf2 transcription factor-deficient mice. Proc Natl Acad Sci U S A 2001, 98:3410-3415.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3410-3415
    • Ramos-Gomez, M.1    Kwak, M.K.2    Dolan, P.M.3    Itoh, K.4    Yamamoto, M.5    Talalay, P.6
  • 37
    • 84867031150 scopus 로고    scopus 로고
    • Mitochondrial dysfunction associated with increased oxidative stress and alpha-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue
    • Imaizumi Y., Okada Y., Akamatsu W., Koike M., Kuzumaki N., Hayakawa H., et al. Mitochondrial dysfunction associated with increased oxidative stress and alpha-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue. Mol Brain 2012, 5:35.
    • (2012) Mol Brain , vol.5 , pp. 35
    • Imaizumi, Y.1    Okada, Y.2    Akamatsu, W.3    Koike, M.4    Kuzumaki, N.5    Hayakawa, H.6
  • 39
    • 84874633349 scopus 로고    scopus 로고
    • Administration of the Nrf2-ARE activators sulforaphane and carnosic acid attenuates 4-hydroxy-2-nonenal-induced mitochondrial dysfunction ex vivo
    • Miller D.M., Singh I.N., Wang J.A., Hall E.D. Administration of the Nrf2-ARE activators sulforaphane and carnosic acid attenuates 4-hydroxy-2-nonenal-induced mitochondrial dysfunction ex vivo. Free Radic Biol Med 2013, 57:1-9.
    • (2013) Free Radic Biol Med , vol.57 , pp. 1-9
    • Miller, D.M.1    Singh, I.N.2    Wang, J.A.3    Hall, E.D.4
  • 40
    • 84881228158 scopus 로고    scopus 로고
    • Impairment of autophagy: from hereditary disorder to drug intoxication
    • Aki T., Funakoshi T., Unuma K., Uemura K. Impairment of autophagy: from hereditary disorder to drug intoxication. Toxicology 2013, 311:205-215.
    • (2013) Toxicology , vol.311 , pp. 205-215
    • Aki, T.1    Funakoshi, T.2    Unuma, K.3    Uemura, K.4
  • 41
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M., Kurokawa H., Waguri S., Taguchi K., Kobayashi A., Ichimura Y., 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    Kurokawa, H.2    Waguri, S.3    Taguchi, K.4    Kobayashi, A.5    Ichimura, Y.6
  • 42
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62
    • Lau A., Wang X.J., Zhao F., Villeneuve N.F., Wu T., Jiang T., 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    Wang, X.J.2    Zhao, F.3    Villeneuve, N.F.4    Wu, T.5    Jiang, T.6
  • 43
    • 84871440902 scopus 로고    scopus 로고
    • Dual TNFalpha-induced effects on NRF2 mediated antioxidant defence in astrocyte-rich cultures: role of protein kinase activation
    • Correa F., Mallard C., Nilsson M., Sandberg M. Dual TNFalpha-induced effects on NRF2 mediated antioxidant defence in astrocyte-rich cultures: role of protein kinase activation. Neurochem Res 2012, 37:2842-2855.
    • (2012) Neurochem Res , vol.37 , pp. 2842-2855
    • Correa, F.1    Mallard, C.2    Nilsson, M.3    Sandberg, M.4
  • 44
    • 57449111441 scopus 로고    scopus 로고
    • Regulatory potential for concerted modulation of Nrf2- and Nfkb1-mediated gene expression in inflammation and carcinogenesis
    • Nair S., Doh S.T., Chan J.Y., Kong A.N., Cai L. Regulatory potential for concerted modulation of Nrf2- and Nfkb1-mediated gene expression in inflammation and carcinogenesis. Br J Cancer 2008, 99:2070-2082.
    • (2008) Br J Cancer , vol.99 , pp. 2070-2082
    • Nair, S.1    Doh, S.T.2    Chan, J.Y.3    Kong, A.N.4    Cai, L.5
  • 46
    • 84886237017 scopus 로고    scopus 로고
    • Sulforaphane ameliorates the development of experimental autoimmune encephalomyelitis by antagonizing oxidative stress and Th17-related inflammation in mice
    • Li B., Cui W., Liu J., Li R., Liu Q., Xie X.H., et al. Sulforaphane ameliorates the development of experimental autoimmune encephalomyelitis by antagonizing oxidative stress and Th17-related inflammation in mice. Exp Neurol 2013, 250:239-249.
    • (2013) Exp Neurol , vol.250 , pp. 239-249
    • Li, B.1    Cui, W.2    Liu, J.3    Li, R.4    Liu, Q.5    Xie, X.H.6
  • 47
    • 79957515007 scopus 로고    scopus 로고
    • Pharmacological targeting of the transcription factor Nrf2 at the basal ganglia provides disease modifying therapy for experimental parkinsonism
    • Jazwa A., Rojo A.I., Innamorato N.G., Hesse M., Fernandez-Ruiz J., Cuadrado A. Pharmacological targeting of the transcription factor Nrf2 at the basal ganglia provides disease modifying therapy for experimental parkinsonism. Antioxid Redox Signal 2011, 14:2347-2360.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2347-2360
    • Jazwa, A.1    Rojo, A.I.2    Innamorato, N.G.3    Hesse, M.4    Fernandez-Ruiz, J.5    Cuadrado, A.6
  • 49
    • 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
  • 50
    • 84896456479 scopus 로고    scopus 로고
    • Efficacy and safety of BG-12 (dimethyl fumarate) and other disease-modifying therapies for the treatment of relapsing-remitting multiple sclerosis: a systematic review and mixed treatment comparison
    • Hutchinson M., Fox R.J., Havrdova E., Kurukulasuriya N.C., Sarda S.P., Agarwal S., et al. Efficacy and safety of BG-12 (dimethyl fumarate) and other disease-modifying therapies for the treatment of relapsing-remitting multiple sclerosis: a systematic review and mixed treatment comparison. Curr Med Res Opin 2014, 30:613-627.
    • (2014) Curr Med Res Opin , vol.30 , pp. 613-627
    • Hutchinson, M.1    Fox, R.J.2    Havrdova, E.3    Kurukulasuriya, N.C.4    Sarda, S.P.5    Agarwal, S.6
  • 51
    • 84866900065 scopus 로고    scopus 로고
    • Mechanisms of oxidative damage in multiple sclerosis and neurodegenerative diseases: therapeutic modulation via fumaric acid esters
    • Lee D.H., Gold R., Linker R.A. Mechanisms of oxidative damage in multiple sclerosis and neurodegenerative diseases: therapeutic modulation via fumaric acid esters. Int J Mol Sci 2012, 13:11783-11803.
    • (2012) Int J Mol Sci , vol.13 , pp. 11783-11803
    • Lee, D.H.1    Gold, R.2    Linker, R.A.3
  • 52
    • 84858648216 scopus 로고    scopus 로고
    • Fumarates promote cytoprotection of central nervous system cells against oxidative stress via the nuclear factor (erythroid-derived 2)-like 2 pathway
    • Scannevin R.H., Chollate S., Jung M.Y., Shackett M., Patel H., Bista P., et al. Fumarates promote cytoprotection of central nervous system cells against oxidative stress via the nuclear factor (erythroid-derived 2)-like 2 pathway. J Pharmacol Exp Ther 2012, 341:274-284.
    • (2012) J Pharmacol Exp Ther , vol.341 , pp. 274-284
    • Scannevin, R.H.1    Chollate, S.2    Jung, M.Y.3    Shackett, M.4    Patel, H.5    Bista, P.6
  • 53
    • 21144431523 scopus 로고    scopus 로고
    • The synthetic triterpenoids, CDDO and CDDO-imidazolide, are potent inducers of heme oxygenase-1 and Nrf2/ARE signaling
    • Liby K., Hock T., Yore M.M., Suh N., Place A.E., Risingsong R., et al. The synthetic triterpenoids, CDDO and CDDO-imidazolide, are potent inducers of heme oxygenase-1 and Nrf2/ARE signaling. Cancer Res 2005, 65:4789-4798.
    • (2005) Cancer Res , vol.65 , pp. 4789-4798
    • Liby, K.1    Hock, T.2    Yore, M.M.3    Suh, N.4    Place, A.E.5    Risingsong, R.6
  • 54
    • 84859759069 scopus 로고    scopus 로고
    • Triterpenoid modulation of IL-17 and Nrf-2 expression ameliorates neuroinflammation and promotes remyelination in autoimmune encephalomyelitis
    • Pareek T.K., Belkadi A., Kesavapany S., Zaremba A., Loh S.L., Bai L., et al. Triterpenoid modulation of IL-17 and Nrf-2 expression ameliorates neuroinflammation and promotes remyelination in autoimmune encephalomyelitis. Sci Rep 2011, 1:201.
    • (2011) Sci Rep , vol.1 , pp. 201
    • Pareek, T.K.1    Belkadi, A.2    Kesavapany, S.3    Zaremba, A.4    Loh, S.L.5    Bai, L.6
  • 55
    • 66749132810 scopus 로고    scopus 로고
    • Neuroprotective effects of the triterpenoid CDDO methyl amide, a potent inducer of Nrf2-mediated transcription
    • Yang L., Calingasan N.Y., Thomas B., Chaturvedi R.K., Kiaei M., Wille E.J., et al. Neuroprotective effects of the triterpenoid CDDO methyl amide, a potent inducer of Nrf2-mediated transcription. PLoS ONE 2009, 4:e5757.
    • (2009) PLoS ONE , vol.4 , pp. e5757
    • Yang, L.1    Calingasan, N.Y.2    Thomas, B.3    Chaturvedi, R.K.4    Kiaei, M.5    Wille, E.J.6
  • 56
    • 0028345209 scopus 로고
    • Coordinated expression and mechanism of induction of HSP32 (heme oxygenase-1) mRNA by hyperthermia in rat organs
    • Raju V.S., Maines M.D. Coordinated expression and mechanism of induction of HSP32 (heme oxygenase-1) mRNA by hyperthermia in rat organs. Biochim Biophys Acta 1994, 1217:273-280.
    • (1994) Biochim Biophys Acta , vol.1217 , pp. 273-280
    • Raju, V.S.1    Maines, M.D.2
  • 57
    • 65649126821 scopus 로고    scopus 로고
    • Neurodegeneration and peroxidases
    • Everse J., Coates P.W. Neurodegeneration and peroxidases. Neurobiol Aging 2009, 30:1011-1025.
    • (2009) Neurobiol Aging , vol.30 , pp. 1011-1025
    • Everse, J.1    Coates, P.W.2
  • 58
    • 37349048899 scopus 로고    scopus 로고
    • Reduction of cerebral infarction in rats by biliverdin associated with amelioration of oxidative stress
    • Deguchi K., Hayashi T., Nagotani S., Sehara Y., Zhang H., Tsuchiya A., et al. Reduction of cerebral infarction in rats by biliverdin associated with amelioration of oxidative stress. Brain Res 2008, 1188:1-8.
    • (2008) Brain Res , vol.1188 , pp. 1-8
    • Deguchi, K.1    Hayashi, T.2    Nagotani, S.3    Sehara, Y.4    Zhang, H.5    Tsuchiya, A.6
  • 59
    • 42049090394 scopus 로고    scopus 로고
    • Heme oxygenase-1 as a therapeutic target in neurodegenerative diseases and brain infections
    • Cuadrado A., Rojo A.I. Heme oxygenase-1 as a therapeutic target in neurodegenerative diseases and brain infections. Curr Pharm Des 2008, 14:429-442.
    • (2008) Curr Pharm Des , vol.14 , pp. 429-442
    • Cuadrado, A.1    Rojo, A.I.2
  • 60
    • 84896404312 scopus 로고    scopus 로고
    • Puerarin alleviates cognitive impairment and oxidative stress in APP/PS1 transgenic mice
    • Zhou Y., Xie N., Li L., Zou Y., Zhang X., Dong M. Puerarin alleviates cognitive impairment and oxidative stress in APP/PS1 transgenic mice. Int J Neuropsychopharmacol 2014, 17:635-644.
    • (2014) Int J Neuropsychopharmacol , vol.17 , pp. 635-644
    • Zhou, Y.1    Xie, N.2    Li, L.3    Zou, Y.4    Zhang, X.5    Dong, M.6
  • 61
    • 84893565750 scopus 로고    scopus 로고
    • Astroglial heme oxygenase-1 and the origin of corpora amylacea in aging and degenerating neural tissues
    • Song W., Zukor H., Liberman A., Kaduri S., Arvanitakis Z., Bennett D.A., et al. Astroglial heme oxygenase-1 and the origin of corpora amylacea in aging and degenerating neural tissues. Exp Neurol 2014, 254:78-89.
    • (2014) Exp Neurol , vol.254 , pp. 78-89
    • Song, W.1    Zukor, H.2    Liberman, A.3    Kaduri, S.4    Arvanitakis, Z.5    Bennett, D.A.6
  • 62
    • 0014842505 scopus 로고
    • One-electron-transfer reactions in biochemical systems, V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • Iyanagi T., Yamazaki I. One-electron-transfer reactions in biochemical systems, V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim Biophys Acta 1970, 216:282-294.
    • (1970) Biochim Biophys Acta , vol.216 , pp. 282-294
    • Iyanagi, T.1    Yamazaki, I.2
  • 63
    • 84893632498 scopus 로고    scopus 로고
    • Mangiferin activates Nrf2-antioxidant response element signaling without reducing the sensitivity to etoposide of human myeloid leukemia cells in vitro
    • Zhang B.P., Zhao J., Li S.S., Yang L.J., Zeng L.L., Chen Y., et al. Mangiferin activates Nrf2-antioxidant response element signaling without reducing the sensitivity to etoposide of human myeloid leukemia cells in vitro. Acta Pharmacol Sin 2014, 35:257-266.
    • (2014) Acta Pharmacol Sin , vol.35 , pp. 257-266
    • Zhang, B.P.1    Zhao, J.2    Li, S.S.3    Yang, L.J.4    Zeng, L.L.5    Chen, Y.6
  • 64
    • 84864023667 scopus 로고    scopus 로고
    • Alpha-Synuclein expression and Nrf2 deficiency cooperate to aggravate protein aggregation, neuronal death and inflammation in early-stage Parkinson's disease
    • Lastres-Becker I., Ulusoy A., Innamorato N.G., Sahin G., Rabano A., Kirik D., et al. alpha-Synuclein expression and Nrf2 deficiency cooperate to aggravate protein aggregation, neuronal death and inflammation in early-stage Parkinson's disease. Hum Mol Genet 2012, 21:3173-3192.
    • (2012) Hum Mol Genet , vol.21 , pp. 3173-3192
    • Lastres-Becker, I.1    Ulusoy, A.2    Innamorato, N.G.3    Sahin, G.4    Rabano, A.5    Kirik, D.6
  • 65
    • 84863041323 scopus 로고    scopus 로고
    • Assurance of mitochondrial integrity and mammalian longevity by the p62-Keap1-Nrf2-Nqo1 cascade
    • Kwon J., Han E., Bui C.B., Shin W., Lee J., Lee S., et al. Assurance of mitochondrial integrity and mammalian longevity by the p62-Keap1-Nrf2-Nqo1 cascade. EMBO Rep 2012, 13:150-156.
    • (2012) EMBO Rep , vol.13 , pp. 150-156
    • Kwon, J.1    Han, E.2    Bui, C.B.3    Shin, W.4    Lee, J.5    Lee, S.6
  • 66
    • 0034990527 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis G., Montfort W.R. Properties and biological activities of thioredoxins. Annu Rev Biophys Biomol Struct 2001, 30:421-455.
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 421-455
    • Powis, G.1    Montfort, W.R.2
  • 69
    • 0037155817 scopus 로고    scopus 로고
    • The roles of thioredoxin in protection against oxidative stress-induced apoptosis in SH-SY5Y cells
    • Andoh T., Chock P.B., Chiueh C.C. The roles of thioredoxin in protection against oxidative stress-induced apoptosis in SH-SY5Y cells. J Biol Chem 2002, 277:9655-9660.
    • (2002) J Biol Chem , vol.277 , pp. 9655-9660
    • Andoh, T.1    Chock, P.B.2    Chiueh, C.C.3
  • 70
    • 84863518914 scopus 로고    scopus 로고
    • DJ-1 induces thioredoxin 1 expression through the Nrf2 pathway
    • Im J.Y., Lee K.W., Woo J.M., Junn E., Mouradian M.M. DJ-1 induces thioredoxin 1 expression through the Nrf2 pathway. Hum Mol Genet 2012, 21:3013-3024.
    • (2012) Hum Mol Genet , vol.21 , pp. 3013-3024
    • Im, J.Y.1    Lee, K.W.2    Woo, J.M.3    Junn, E.4    Mouradian, M.M.5
  • 72
    • 77958529500 scopus 로고    scopus 로고
    • The unfolded protein response protects from tau neurotoxicity in vivo
    • Loewen C.A., Feany M.B. The unfolded protein response protects from tau neurotoxicity in vivo. PLoS ONE 2010, 5.
    • (2010) PLoS ONE , pp. 5
    • Loewen, C.A.1    Feany, M.B.2
  • 73
    • 77649272440 scopus 로고    scopus 로고
    • Stabilization of transcription factor Nrf2 by tBHQ prevents oxidative stress-induced amyloid beta formation in NT2N neurons
    • Eftekharzadeh B., Maghsoudi N., Khodagholi F. Stabilization of transcription factor Nrf2 by tBHQ prevents oxidative stress-induced amyloid beta formation in NT2N neurons. Biochimie 2010, 92:245-253.
    • (2010) Biochimie , vol.92 , pp. 245-253
    • Eftekharzadeh, B.1    Maghsoudi, N.2    Khodagholi, F.3
  • 74
    • 84874159254 scopus 로고    scopus 로고
    • Amelioration of Alzheimer's disease by neuroprotective effect of sulforaphane in animal model
    • Kim H.V., Kim H.Y., Ehrlich H.Y., Choi S.Y., Kim D.J., Kim Y. Amelioration of Alzheimer's disease by neuroprotective effect of sulforaphane in animal model. Amyloid 2013, 20:7-12.
    • (2013) Amyloid , vol.20 , pp. 7-12
    • Kim, H.V.1    Kim, H.Y.2    Ehrlich, H.Y.3    Choi, S.Y.4    Kim, D.J.5    Kim, Y.6
  • 75
    • 62649115489 scopus 로고    scopus 로고
    • Triterpenoid CDDO-methylamide improves memory and decreases amyloid plaques in a transgenic mouse model of Alzheimer's disease
    • Dumont M., Wille E., Calingasan N.Y., Tampellini D., Williams C., Gouras G.K., et al. Triterpenoid CDDO-methylamide improves memory and decreases amyloid plaques in a transgenic mouse model of Alzheimer's disease. J Neurochem 2009, 109:502-512.
    • (2009) J Neurochem , vol.109 , pp. 502-512
    • Dumont, M.1    Wille, E.2    Calingasan, N.Y.3    Tampellini, D.4    Williams, C.5    Gouras, G.K.6
  • 76
    • 33745919520 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • de Lau L.M., Breteler M.M. Epidemiology of Parkinson's disease. Lancet Neurol 2006, 5:525-535.
    • (2006) Lancet Neurol , vol.5 , pp. 525-535
    • de Lau, L.M.1    Breteler, M.M.2
  • 77
    • 0034993599 scopus 로고    scopus 로고
    • Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: contribution to the apoptotic theory in Parkinson's disease
    • Blum D., Torch S., Lambeng N., Nissou M., Benabid A.L., Sadoul R., et al. Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: contribution to the apoptotic theory in Parkinson's disease. Prog Neurobiol 2001, 65:135-172.
    • (2001) Prog Neurobiol , vol.65 , pp. 135-172
    • Blum, D.1    Torch, S.2    Lambeng, N.3    Nissou, M.4    Benabid, A.L.5    Sadoul, R.6
  • 78
    • 0030070813 scopus 로고    scopus 로고
    • A comparative analysis of neuroblastic and substrate-adherent human neuroblastoma cell lines
    • La Quaglia M.P., Manchester K.M. A comparative analysis of neuroblastic and substrate-adherent human neuroblastoma cell lines. J Pediatr Surg 1996, 31:315-318.
    • (1996) J Pediatr Surg , vol.31 , pp. 315-318
    • La Quaglia, M.P.1    Manchester, K.M.2
  • 80
    • 84891699279 scopus 로고    scopus 로고
    • Naringenin protects against 6-OHDA-induced neurotoxicity via activation of the Nrf2/ARE signaling pathway
    • Lou H., Jing X., Wei X., Shi H., Ren D., Zhang X. Naringenin protects against 6-OHDA-induced neurotoxicity via activation of the Nrf2/ARE signaling pathway. Neuropharmacology 2014, 79:380-388.
    • (2014) Neuropharmacology , vol.79 , pp. 380-388
    • Lou, H.1    Jing, X.2    Wei, X.3    Shi, H.4    Ren, D.5    Zhang, X.6
  • 81
    • 65849512212 scopus 로고    scopus 로고
    • Nrf2 activators provide neuroprotection against 6-hydroxydopamine toxicity in rat organotypic nigrostriatal cocultures
    • Siebert A., Desai V., Chandrasekaran K., Fiskum G., Jafri M.S. Nrf2 activators provide neuroprotection against 6-hydroxydopamine toxicity in rat organotypic nigrostriatal cocultures. J Neurosci Res 2009, 87:1659-1669.
    • (2009) J Neurosci Res , vol.87 , pp. 1659-1669
    • Siebert, A.1    Desai, V.2    Chandrasekaran, K.3    Fiskum, G.4    Jafri, M.S.5
  • 82
    • 77950857170 scopus 로고    scopus 로고
    • Huntington's disease: pathogenesis to animal models
    • Kumar P., Kalonia H., Kumar A. Huntington's disease: pathogenesis to animal models. Pharmacol Rep 2010, 62:1-14.
    • (2010) Pharmacol Rep , vol.62 , pp. 1-14
    • Kumar, P.1    Kalonia, H.2    Kumar, A.3
  • 83
    • 84874564486 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and Nrf2 signaling contribute to compromised responses to oxidative stress in striatal cells expressing full-length mutant huntingtin
    • Jin Y.N., Yu Y.V., Gundemir S., Jo C., Cui M., Tieu K., et al. Impaired mitochondrial dynamics and Nrf2 signaling contribute to compromised responses to oxidative stress in striatal cells expressing full-length mutant huntingtin. PLoS ONE 2013, 8:e57932.
    • (2013) PLoS ONE , vol.8 , pp. e57932
    • Jin, Y.N.1    Yu, Y.V.2    Gundemir, S.3    Jo, C.4    Cui, M.5    Tieu, K.6
  • 84
    • 79551626268 scopus 로고    scopus 로고
    • Efficacy of fumaric acid esters in the R6/2 and YAC128 models of Huntington's disease
    • Ellrichmann G., Petrasch-Parwez E., Lee D.H., Reick C., Arning L., Saft C., et al. Efficacy of fumaric acid esters in the R6/2 and YAC128 models of Huntington's disease. PLoS ONE 2011, 6:e16172.
    • (2011) PLoS ONE , vol.6 , pp. e16172
    • Ellrichmann, G.1    Petrasch-Parwez, E.2    Lee, D.H.3    Reick, C.4    Arning, L.5    Saft, C.6
  • 85
    • 77953537441 scopus 로고    scopus 로고
    • Triterpenoids CDDO-ethyl amide and CDDO-trifluoroethyl amide improve the behavioral phenotype and brain pathology in a transgenic mouse model of Huntington's disease
    • Stack C., Ho D., Wille E., Calingasan N.Y., Williams C., Liby K., et al. Triterpenoids CDDO-ethyl amide and CDDO-trifluoroethyl amide improve the behavioral phenotype and brain pathology in a transgenic mouse model of Huntington's disease. Free Radic Biol Med 2010, 49:147-158.
    • (2010) Free Radic Biol Med , vol.49 , pp. 147-158
    • Stack, C.1    Ho, D.2    Wille, E.3    Calingasan, N.Y.4    Williams, C.5    Liby, K.6
  • 86
    • 54149084585 scopus 로고    scopus 로고
    • Multiple sclerosis
    • Compston A., Coles A. Multiple sclerosis. Lancet 2008, 372:1502-1517.
    • (2008) Lancet , vol.372 , pp. 1502-1517
    • Compston, A.1    Coles, A.2
  • 87
    • 28544450761 scopus 로고    scopus 로고
    • Experimental allergic encephalomyelitis: a misleading model of multiple sclerosis
    • Sriram S., Steiner I. Experimental allergic encephalomyelitis: a misleading model of multiple sclerosis. Ann Neurol 2005, 58:939-945.
    • (2005) Ann Neurol , vol.58 , pp. 939-945
    • Sriram, S.1    Steiner, I.2
  • 88
    • 79952136166 scopus 로고    scopus 로고
    • Fumaric acid esters exert neuroprotective effects in neuroinflammation via activation of the Nrf2 antioxidant pathway
    • Linker R.A., Lee D.H., Ryan S., van Dam A.M., Conrad R., Bista P., et al. Fumaric acid esters exert neuroprotective effects in neuroinflammation via activation of the Nrf2 antioxidant pathway. Brain 2011, 134:678-692.
    • (2011) Brain , vol.134 , pp. 678-692
    • Linker, R.A.1    Lee, D.H.2    Ryan, S.3    van Dam, A.M.4    Conrad, R.5    Bista, P.6
  • 89
    • 77951557888 scopus 로고    scopus 로고
    • The absence of the pro-antioxidant transcription factor Nrf2 exacerbates experimental autoimmune encephalomyelitis
    • Johnson D.A., Amirahmadi S., Ward C., Fabry Z., Johnson J.A. The absence of the pro-antioxidant transcription factor Nrf2 exacerbates experimental autoimmune encephalomyelitis. Toxicol Sci 2010, 114:237-246.
    • (2010) Toxicol Sci , vol.114 , pp. 237-246
    • Johnson, D.A.1    Amirahmadi, S.2    Ward, C.3    Fabry, Z.4    Johnson, J.A.5
  • 90
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • Deng H.X., Chen W., Hong S.T., Boycott K.M., Gorrie G.H., Siddique N., et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 2011, 477:211-215.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1    Chen, W.2    Hong, S.T.3    Boycott, K.M.4    Gorrie, G.H.5    Siddique, N.6
  • 91
    • 84868560352 scopus 로고    scopus 로고
    • A novel small molecule, N-(4-(2-pyridyl)(1,3-thiazol-2-yl))-2-(2,4,6-trimethylphenoxy) acetamide, selectively protects against oxidative stress-induced cell death by activating the Nrf2-ARE pathway: therapeutic implications for ALS
    • Kanno T., Tanaka K., Yanagisawa Y., Yasutake K., Hadano S., Yoshii F., et al. A novel small molecule, N-(4-(2-pyridyl)(1,3-thiazol-2-yl))-2-(2,4,6-trimethylphenoxy) acetamide, selectively protects against oxidative stress-induced cell death by activating the Nrf2-ARE pathway: therapeutic implications for ALS. Free Radic Biol Med 2012, 53:2028-2042.
    • (2012) Free Radic Biol Med , vol.53 , pp. 2028-2042
    • Kanno, T.1    Tanaka, K.2    Yanagisawa, Y.3    Yasutake, K.4    Hadano, S.5    Yoshii, F.6
  • 92
    • 84858451400 scopus 로고    scopus 로고
    • Impaired antioxydative Keap1/Nrf2 system and the downstream stress protein responses in the motor neuron of ALS model mice
    • Mimoto T., Miyazaki K., Morimoto N., Kurata T., Satoh K., Ikeda Y., et al. Impaired antioxydative Keap1/Nrf2 system and the downstream stress protein responses in the motor neuron of ALS model mice. Brain Res 2012, 1446:109-118.
    • (2012) Brain Res , vol.1446 , pp. 109-118
    • Mimoto, T.1    Miyazaki, K.2    Morimoto, N.3    Kurata, T.4    Satoh, K.5    Ikeda, Y.6
  • 93
    • 77955423158 scopus 로고    scopus 로고
    • Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell
    • Duan W., Li X., Shi J., Guo Y., Li Z., Li C. Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell. Neuroscience 2010, 169:1621-1629.
    • (2010) Neuroscience , vol.169 , pp. 1621-1629
    • Duan, W.1    Li, X.2    Shi, J.3    Guo, Y.4    Li, Z.5    Li, C.6
  • 94
    • 84881526830 scopus 로고    scopus 로고
    • Up-down regulation of HO-1 and iNOS gene expressions by ethyl pyruvate via recruiting p300 to Nrf2 and depriving It from p65
    • Kim S.W., Lee H.K., Shin J.H., Lee J.K. Up-down regulation of HO-1 and iNOS gene expressions by ethyl pyruvate via recruiting p300 to Nrf2 and depriving It from p65. Free Radic Biol Med 2013, 65:468-476.
    • (2013) Free Radic Biol Med , vol.65 , pp. 468-476
    • Kim, S.W.1    Lee, H.K.2    Shin, J.H.3    Lee, J.K.4
  • 95
    • 84887283397 scopus 로고    scopus 로고
    • Neuronal activity regulates astrocytic Nrf2 signaling
    • Habas A., Hahn J., Wang X., Margeta M. Neuronal activity regulates astrocytic Nrf2 signaling. Proc Natl Acad Sci U S A 2013, 110:18291-18296.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 18291-18296
    • Habas, A.1    Hahn, J.2    Wang, X.3    Margeta, M.4
  • 96
    • 84873466384 scopus 로고    scopus 로고
    • Acanthopanax senticosus exerts neuroprotective effects through HO-1 signaling in hippocampal and microglial cells
    • Jin M.L., Park S.Y., Kim Y.H., Park G., Lee S.J. Acanthopanax senticosus exerts neuroprotective effects through HO-1 signaling in hippocampal and microglial cells. Environ Toxicol Pharmacol 2013, 35:335-346.
    • (2013) Environ Toxicol Pharmacol , vol.35 , pp. 335-346
    • Jin, M.L.1    Park, S.Y.2    Kim, Y.H.3    Park, G.4    Lee, S.J.5
  • 97
    • 84879842266 scopus 로고    scopus 로고
    • Puerarin attenuates neuronal degeneration in the substantia nigra of 6-OHDA-lesioned rats through regulating BDNF expression and activating the Nrf2/ARE signaling pathway
    • Li R., Liang T., Xu L., Zheng N., Zhang K., Duan X. Puerarin attenuates neuronal degeneration in the substantia nigra of 6-OHDA-lesioned rats through regulating BDNF expression and activating the Nrf2/ARE signaling pathway. Brain Res 2013, 1523:1-9.
    • (2013) Brain Res , vol.1523 , pp. 1-9
    • Li, R.1    Liang, T.2    Xu, L.3    Zheng, N.4    Zhang, K.5    Duan, X.6
  • 98
    • 84879504006 scopus 로고    scopus 로고
    • Genistein attenuates ischemic oxidative damage and behavioral deficits via eNOS/Nrf2/HO-1 signaling
    • Wang R., Tu J., Zhang Q., Zhang X., Zhu Y., Ma W., et al. Genistein attenuates ischemic oxidative damage and behavioral deficits via eNOS/Nrf2/HO-1 signaling. Hippocampus 2013, 23:634-647.
    • (2013) Hippocampus , vol.23 , pp. 634-647
    • Wang, R.1    Tu, J.2    Zhang, Q.3    Zhang, X.4    Zhu, Y.5    Ma, W.6
  • 99
    • 84891589937 scopus 로고    scopus 로고
    • Antisense oligonucleotide against GSK-3beta in brain of SAMP8 mice improves learning and memory and decreases oxidative stress: involvement of transcription factor Nrf2 and implications for Alzheimer disease
    • Farr S.A., Ripley J.L., Sultana R., Zhang Z., Niehoff M.L., Platt T.L., et al. Antisense oligonucleotide against GSK-3beta in brain of SAMP8 mice improves learning and memory and decreases oxidative stress: involvement of transcription factor Nrf2 and implications for Alzheimer disease. Free Radic Biol Med 2014, 67:387-395.
    • (2014) Free Radic Biol Med , vol.67 , pp. 387-395
    • Farr, S.A.1    Ripley, J.L.2    Sultana, R.3    Zhang, Z.4    Niehoff, M.L.5    Platt, T.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.