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Volumn 1842, Issue 8, 2014, Pages 1208-1218

Oxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases

Author keywords

Misfolded proteins; Neurodegenerative diseases; Nrf2 ARE pathway; Oxidative stress

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; BASIC LEUCINE ZIPPER TRANSCRIPTION FACTOR; BILIRUBIN; BILIVERDIN; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE A4; HUNTINGTIN; KELCH LIKE ECH ASSOCIATED PROTEIN 1; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA; METALLOTHIONEIN III; PEROXIREDOXIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); TAU PROTEIN; THIOREDOXIN; TRANSCRIPTION FACTOR MAF; TRANSCRIPTION FACTOR NRF2; TYROSINE 3 MONOOXYGENASE;

EID: 84903270398     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2013.12.011     Document Type: Review
Times cited : (241)

References (165)
  • 2
    • 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., Calkins M.J., Chan K., Kan Y.W., Johnson J.A. 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    Calkins, M.J.2    Chan, K.3    Kan, Y.W.4    Johnson, J.A.5
  • 3
    • 0037996661 scopus 로고    scopus 로고
    • Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress
    • Shih A.Y., Johnson D.A., Wong G., Kraft A.D., Jiang L., Erb H., Johnson J.A., Murphy T.H. Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress. J. Neurosci. 2003, 23:3394-3406.
    • (2003) J. Neurosci. , vol.23 , pp. 3394-3406
    • Shih, A.Y.1    Johnson, D.A.2    Wong, G.3    Kraft, A.D.4    Jiang, L.5    Erb, H.6    Johnson, J.A.7    Murphy, T.H.8
  • 5
    • 84884863139 scopus 로고    scopus 로고
    • Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis
    • Dasuri K., Zhang L., Keller J.N. Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis. Free Radic. Biol. Med. 2013, 62:170-185.
    • (2013) Free Radic. Biol. Med. , vol.62 , pp. 170-185
    • Dasuri, K.1    Zhang, L.2    Keller, J.N.3
  • 9
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery W.R., Lovell M.A. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol. Aging 1998, 19:33-36.
    • (1998) Neurobiol. Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 10
    • 33744935554 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in mild cognitive impairment and early Alzheimer's disease
    • Williams T.I., Lynn B.C., Markesbery W.R., Lovell M.A. Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in mild cognitive impairment and early Alzheimer's disease. Neurobiol. Aging 2006, 27:1094-1099.
    • (2006) Neurobiol. Aging , vol.27 , pp. 1094-1099
    • Williams, T.I.1    Lynn, B.C.2    Markesbery, W.R.3    Lovell, M.A.4
  • 12
    • 0031722955 scopus 로고    scopus 로고
    • Presence of 4-hydroxynonenal in cerebrospinal fluid of patients with sporadic amyotrophic lateral sclerosis
    • Smith R.G., Henry Y.K., Mattson M.P., Appel S.H. Presence of 4-hydroxynonenal in cerebrospinal fluid of patients with sporadic amyotrophic lateral sclerosis. Ann. Neurol. 1998, 44:696-699.
    • (1998) Ann. Neurol. , vol.44 , pp. 696-699
    • Smith, R.G.1    Henry, Y.K.2    Mattson, M.P.3    Appel, S.H.4
  • 13
    • 2442701519 scopus 로고    scopus 로고
    • Increased lipid peroxidation in sera of ALS patients: a potential biomarker of disease burden
    • Simpson E.P., Henry Y.K., Henkel J.S., Smith R.G., Appel S.H. Increased lipid peroxidation in sera of ALS patients: a potential biomarker of disease burden. Neurology 2004, 62:1758-1765.
    • (2004) Neurology , vol.62 , pp. 1758-1765
    • Simpson, E.P.1    Henry, Y.K.2    Henkel, J.S.3    Smith, R.G.4    Appel, S.H.5
  • 14
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • Sayre L.M., Zelasko D.A., Harris P.L., Perry G., Salomon R.G., Smith M.A. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J. Neurochem. 1997, 68:2092-2097.
    • (1997) J. Neurochem. , vol.68 , pp. 2092-2097
    • Sayre, L.M.1    Zelasko, D.A.2    Harris, P.L.3    Perry, G.4    Salomon, R.G.5    Smith, M.A.6
  • 16
    • 0031768026 scopus 로고    scopus 로고
    • Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients
    • Pedersen W.A., Fu W., Keller J.N., Markesbery W.R., Appel S., Smith R.G., Kasarskis E., Mattson M.P. Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. Ann. Neurol. 1998, 44:819-824.
    • (1998) Ann. Neurol. , vol.44 , pp. 819-824
    • Pedersen, W.A.1    Fu, W.2    Keller, J.N.3    Markesbery, W.R.4    Appel, S.5    Smith, R.G.6    Kasarskis, E.7    Mattson, M.P.8
  • 17
    • 0030805622 scopus 로고    scopus 로고
    • A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease
    • Alam Z.I., Daniel S.E., Lees A.J., Marsden D.C., Jenner P., Halliwell B. A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J. Neurochem. 1997, 69:1326-1329.
    • (1997) J. Neurochem. , vol.69 , pp. 1326-1329
    • Alam, Z.I.1    Daniel, S.E.2    Lees, A.J.3    Marsden, D.C.4    Jenner, P.5    Halliwell, B.6
  • 18
    • 0031962268 scopus 로고    scopus 로고
    • Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay
    • Floor E., Wetzel M.G. Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay. J. Neurochem. 1998, 70:268-275.
    • (1998) J. Neurochem. , vol.70 , pp. 268-275
    • Floor, E.1    Wetzel, M.G.2
  • 19
    • 20444373701 scopus 로고    scopus 로고
    • Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
    • Pamplona R., Dalfo E., Ayala V., Bellmunt M.J., Prat J., Ferrer I., Portero-Otin M. Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. J. Biol. Chem. 2005, 280:21522-21530.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21522-21530
    • Pamplona, R.1    Dalfo, E.2    Ayala, V.3    Bellmunt, M.J.4    Prat, J.5    Ferrer, I.6    Portero-Otin, M.7
  • 21
    • 0030898724 scopus 로고    scopus 로고
    • An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease
    • Lyras L., Cairns N.J., Jenner A., Jenner P., Halliwell B. An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease. J. Neurochem. 1997, 68:2061-2069.
    • (1997) J. Neurochem. , vol.68 , pp. 2061-2069
    • Lyras, L.1    Cairns, N.J.2    Jenner, A.3    Jenner, P.4    Halliwell, B.5
  • 22
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling A.C., Schulz J.B., Brown R.H., Beal M.F. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 1993, 61:2322-2325.
    • (1993) J. Neurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown, R.H.3    Beal, M.F.4
  • 27
    • 0026578425 scopus 로고
    • Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent tau and accumulation of abnormal tau-isoforms (A68 proteins)
    • Bramblett G.T., Trojanowski J.Q., Lee V.M. Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent tau and accumulation of abnormal tau-isoforms (A68 proteins). Lab. Invest. 1992, 66:212-222.
    • (1992) Lab. Invest. , vol.66 , pp. 212-222
    • Bramblett, G.T.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 28
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley K., Maidt M.L., Yu Z., Sang H., Markesbery W.R., Floyd R.A. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 1998, 18:8126-8132.
    • (1998) J. Neurosci. , vol.18 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 30
    • 0030878073 scopus 로고    scopus 로고
    • Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8-hydroxyguanine levels in substantia nigra
    • Alam Z.I., Jenner A., Daniel S.E., Lees A.J., Cairns N., Marsden C.D., Jenner P., Halliwell B. Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J. Neurochem. 1997, 69:1196-1203.
    • (1997) J. Neurochem. , vol.69 , pp. 1196-1203
    • Alam, Z.I.1    Jenner, A.2    Daniel, S.E.3    Lees, A.J.4    Cairns, N.5    Marsden, C.D.6    Jenner, P.7    Halliwell, B.8
  • 32
    • 0035105715 scopus 로고    scopus 로고
    • Ratio of 8-hydroxyguanine in intact DNA to free 8-hydroxyguanine is increased in Alzheimer disease ventricular cerebrospinal fluid
    • Lovell M.A., Markesbery W.R. Ratio of 8-hydroxyguanine in intact DNA to free 8-hydroxyguanine is increased in Alzheimer disease ventricular cerebrospinal fluid. Arch. Neurol. 2001, 58:392-396.
    • (2001) Arch. Neurol. , vol.58 , pp. 392-396
    • Lovell, M.A.1    Markesbery, W.R.2
  • 33
    • 84860451153 scopus 로고    scopus 로고
    • Urinary 8-hydroxy-2'-deoxyguanosine level and plasma paraoxonase 1 activity with Alzheimer's disease
    • Zengi O., Karakas A., Ergun U., Senes M., Inan L., Yucel D. Urinary 8-hydroxy-2'-deoxyguanosine level and plasma paraoxonase 1 activity with Alzheimer's disease. Clin. Chem. Lab. Med. 2012, 50:529-534.
    • (2012) Clin. Chem. Lab. Med. , vol.50 , pp. 529-534
    • Zengi, O.1    Karakas, A.2    Ergun, U.3    Senes, M.4    Inan, L.5    Yucel, D.6
  • 34
    • 13244275028 scopus 로고    scopus 로고
    • Oxidative stress and metal content in blood and cerebrospinal fluid of amyotrophic lateral sclerosis patients with and without a Cu, Zn-superoxide dismutase mutation
    • Ihara Y., Nobukuni K., Takata H., Hayabara T. Oxidative stress and metal content in blood and cerebrospinal fluid of amyotrophic lateral sclerosis patients with and without a Cu, Zn-superoxide dismutase mutation. Neurol. Res. 2005, 27:105-108.
    • (2005) Neurol. Res. , vol.27 , pp. 105-108
    • Ihara, Y.1    Nobukuni, K.2    Takata, H.3    Hayabara, T.4
  • 35
    • 41049090802 scopus 로고    scopus 로고
    • Increased mitochondrial oxidative damage and oxidative DNA damage contributes to the neurodegenerative process in sporadic amyotrophic lateral sclerosis
    • Murata T., Ohtsuka C., Terayama Y. Increased mitochondrial oxidative damage and oxidative DNA damage contributes to the neurodegenerative process in sporadic amyotrophic lateral sclerosis. Free Radic. Res. 2008, 42:221-225.
    • (2008) Free Radic. Res. , vol.42 , pp. 221-225
    • Murata, T.1    Ohtsuka, C.2    Terayama, Y.3
  • 38
    • 0033520166 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex
    • Polidori M.C., Mecocci P., Browne S.E., Senin U., Beal M.F. Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex. Neurosci. Lett. 1999, 272:53-56.
    • (1999) Neurosci. Lett. , vol.272 , pp. 53-56
    • Polidori, M.C.1    Mecocci, P.2    Browne, S.E.3    Senin, U.4    Beal, M.F.5
  • 39
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J., Dexter D.T., Lees A.J., Daniel S., Agid Y., Javoy-Agid F., Jenner P., Marsden C.D. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann. Neurol. 1994, 36:348-355.
    • (1994) Ann. Neurol. , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 40
    • 0026644192 scopus 로고
    • Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease
    • Sofic E., Lange K.W., Jellinger K., Riederer P. Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci. Lett. 1992, 142:128-130.
    • (1992) Neurosci. Lett. , vol.142 , pp. 128-130
    • Sofic, E.1    Lange, K.W.2    Jellinger, K.3    Riederer, P.4
  • 41
    • 0030724621 scopus 로고    scopus 로고
    • Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease
    • Pearce R.K., Owen A., Daniel S., Jenner P., Marsden C.D. Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease. J. Neural Transm. 1997, 104:661-677.
    • (1997) J. Neural Transm. , vol.104 , pp. 661-677
    • Pearce, R.K.1    Owen, A.2    Daniel, S.3    Jenner, P.4    Marsden, C.D.5
  • 43
    • 84862325005 scopus 로고    scopus 로고
    • Mitochondria-targeted catalase reduces abnormal APP processing, amyloid beta production and BACE1 in a mouse model of Alzheimer's disease: implications for neuroprotection and lifespan extension
    • Mao P., Manczak M., Calkins M.J., Truong Q., Reddy T.P., Reddy A.P., Shirendeb U., Lo H.H., Rabinovitch P.S., Reddy P.H. Mitochondria-targeted catalase reduces abnormal APP processing, amyloid beta production and BACE1 in a mouse model of Alzheimer's disease: implications for neuroprotection and lifespan extension. Hum. Mol. Genet. 2012, 21:2973-2990.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2973-2990
    • Mao, P.1    Manczak, M.2    Calkins, M.J.3    Truong, Q.4    Reddy, T.P.5    Reddy, A.P.6    Shirendeb, U.7    Lo, H.H.8    Rabinovitch, P.S.9    Reddy, P.H.10
  • 44
    • 84870549095 scopus 로고    scopus 로고
    • Astrocyte-specific overexpression of Nrf2 delays motor pathology and synuclein aggregation throughout the CNS in the alpha-synuclein mutant (A53T) mouse model
    • Gan L., Vargas M.R., Johnson D.A., Johnson J.A. Astrocyte-specific overexpression of Nrf2 delays motor pathology and synuclein aggregation throughout the CNS in the alpha-synuclein mutant (A53T) mouse model. J. Neurosci. 2012, 32:17775-17787.
    • (2012) J. Neurosci. , vol.32 , pp. 17775-17787
    • Gan, L.1    Vargas, M.R.2    Johnson, D.A.3    Johnson, J.A.4
  • 46
    • 33845361630 scopus 로고    scopus 로고
    • Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: mechanisms of mitochondriopathy and cell death
    • Martin L.J., Liu Z., Chen K., Price A.C., Pan Y., Swaby J.A., Golden W.C. Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: mechanisms of mitochondriopathy and cell death. J. Comp. Neurol. 2007, 500:20-46.
    • (2007) J. Comp. Neurol. , vol.500 , pp. 20-46
    • Martin, L.J.1    Liu, Z.2    Chen, K.3    Price, A.C.4    Pan, Y.5    Swaby, J.A.6    Golden, W.C.7
  • 47
    • 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., Chan K., Asunis I., Cao A., Kan Y.W. 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    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 48
    • 33644641067 scopus 로고    scopus 로고
    • The mammalian cap and collar family of transcription factors
    • Alam J. The mammalian cap and collar family of transcription factors. Antioxid. Redox Signal. 2006, 8:39-42.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 39-42
    • Alam, J.1
  • 49
    • 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
  • 50
    • 0024997241 scopus 로고
    • Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants
    • Rushmore T.H., Pickett C.B. Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. J. Biol. Chem. 1990, 265:14648-14653.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14648-14653
    • Rushmore, T.H.1    Pickett, C.B.2
  • 51
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 1999, 13:76-86.
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 52
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., O'Connor T., Yamamoto M. Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cells 2003, 8:379-391.
    • (2003) Genes Cells , vol.8 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 53
    • 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
    • Cullinan S.B., Gordan J.D., Jin J., Harper J.W., Diehl J.A. The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase. Mol. Cell Biol. 2004, 24:8477-8486.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 54
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon M., Itoh K., Yamamoto M., Hayes J.D. Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem. 2003, 278:21592-21600.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 55
    • 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
  • 56
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang D.D., Lo S.C., Cross J.V., Templeton D.J., Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol. Cell Biol. 2004, 24:10941-10953.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 58
    • 4844225631 scopus 로고    scopus 로고
    • Genetic dissection of systemic autoimmune disease in Nrf2-deficient mice
    • Li J., Stein T.D., Johnson J.A. Genetic dissection of systemic autoimmune disease in Nrf2-deficient mice. Physiol. Genomics 2004, 18:261-272.
    • (2004) Physiol. Genomics , vol.18 , pp. 261-272
    • Li, J.1    Stein, T.D.2    Johnson, J.A.3
  • 60
    • 58149232639 scopus 로고    scopus 로고
    • Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis
    • Sarlette A., Krampfl K., Grothe C., Neuhoff N., Dengler R., Petri S. Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 2008, 67:1055-1062.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 1055-1062
    • Sarlette, A.1    Krampfl, K.2    Grothe, C.3    Neuhoff, N.4    Dengler, R.5    Petri, S.6
  • 62
    • 0034622230 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase activity is increased in hippocampal pyramidal neurons of patients with Aalzheimer's disease
    • Wang Y., Santa-Cruz K., DeCarli C., Johnson J.A. NAD(P)H:quinone oxidoreductase activity is increased in hippocampal pyramidal neurons of patients with Aalzheimer's disease. Neurobiol. Aging 2000, 21:525-531.
    • (2000) Neurobiol. Aging , vol.21 , pp. 525-531
    • Wang, Y.1    Santa-Cruz, K.2    DeCarli, C.3    Johnson, J.A.4
  • 63
    • 0033036818 scopus 로고    scopus 로고
    • Quinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer's disease
    • Raina A.K., Templeton D.J., Deak J.C., Perry G., Smith M.A. Quinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer's disease. Redox Rep. 1999, 4:23-27.
    • (1999) Redox Rep. , vol.4 , pp. 23-27
    • Raina, A.K.1    Templeton, D.J.2    Deak, J.C.3    Perry, G.4    Smith, M.A.5
  • 65
    • 0032031011 scopus 로고    scopus 로고
    • Neural heme oxygenase-1 expression in idiopathic Parkinson's disease
    • Schipper H.M., Liberman A., Stopa E.G. Neural heme oxygenase-1 expression in idiopathic Parkinson's disease. Exp. Neurol. 1998, 150:60-68.
    • (1998) Exp. Neurol. , vol.150 , pp. 60-68
    • Schipper, H.M.1    Liberman, A.2    Stopa, E.G.3
  • 66
    • 0030597071 scopus 로고    scopus 로고
    • Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease
    • Castellani R., Smith M.A., Richey P.L., Perry G. Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease. Brain Res. 1996, 737:195-200.
    • (1996) Brain Res. , vol.737 , pp. 195-200
    • Castellani, R.1    Smith, M.A.2    Richey, P.L.3    Perry, G.4
  • 67
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain
    • Schipper H.M., Cisse S., Stopa E.G. Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Ann. Neurol. 1995, 37:758-768.
    • (1995) Ann. Neurol. , vol.37 , pp. 758-768
    • Schipper, H.M.1    Cisse, S.2    Stopa, E.G.3
  • 68
    • 0033374730 scopus 로고    scopus 로고
    • Neuroprotective action of bilirubin against oxidative stress in primary hippocampal cultures
    • Dore S., Snyder S.H. Neuroprotective action of bilirubin against oxidative stress in primary hippocampal cultures. Ann. N. Y. Acad. Sci. 1999, 890:167-172.
    • (1999) Ann. N. Y. Acad. Sci. , vol.890 , pp. 167-172
    • Dore, S.1    Snyder, S.H.2
  • 69
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker R., Yamamoto Y., McDonagh A.F., Glazer A.N., Ames B.N. Bilirubin is an antioxidant of possible physiological importance. Science 1987, 235:1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 71
    • 0035233637 scopus 로고    scopus 로고
    • Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome
    • Kim S.H., Fountoulakis M., Cairns N., Lubec G. Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome. J. Neural Transm. Suppl. 2001, 223-235.
    • (2001) J. Neural Transm. Suppl. , pp. 223-235
    • Kim, S.H.1    Fountoulakis, M.2    Cairns, N.3    Lubec, G.4
  • 77
    • 79957827273 scopus 로고    scopus 로고
    • Maneb and paraquat-mediated neurotoxicity: involvement of peroxiredoxin/thioredoxin system
    • Roede J.R., Hansen J.M., Go Y.M., Jones D.P. Maneb and paraquat-mediated neurotoxicity: involvement of peroxiredoxin/thioredoxin system. Toxicol. Sci. 2011, 121:368-375.
    • (2011) Toxicol. Sci. , vol.121 , pp. 368-375
    • Roede, J.R.1    Hansen, J.M.2    Go, Y.M.3    Jones, D.P.4
  • 78
    • 24044447603 scopus 로고    scopus 로고
    • Induction of the protective antioxidant response element pathway by 6-hydroxydopamine in vivo and in vitro
    • Jakel R.J., Kern J.T., Johnson D.A., Johnson J.A. Induction of the protective antioxidant response element pathway by 6-hydroxydopamine in vivo and in vitro. Toxicol. Sci. 2005, 87:176-186.
    • (2005) Toxicol. Sci. , vol.87 , pp. 176-186
    • Jakel, R.J.1    Kern, J.T.2    Johnson, D.A.3    Johnson, J.A.4
  • 82
    • 58149379610 scopus 로고    scopus 로고
    • Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis
    • Vargas M.R., Johnson D.A., Sirkis D.W., Messing A., Johnson J.A. Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis. J. Neurosci. 2008, 28:13574-13581.
    • (2008) J. Neurosci. , vol.28 , pp. 13574-13581
    • Vargas, M.R.1    Johnson, D.A.2    Sirkis, D.W.3    Messing, A.4    Johnson, J.A.5
  • 84
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity
    • Irizarry M.C., Growdon W., Gomez-Isla T., Newell K., George J.M., Clayton D.F., Hyman B.T. Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity. J. Neuropathol. Exp. Neurol. 1998, 57:334-337.
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 334-337
    • Irizarry, M.C.1    Growdon, W.2    Gomez-Isla, T.3    Newell, K.4    George, J.M.5    Clayton, D.F.6    Hyman, B.T.7
  • 88
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A., Masliah E., Yoshimoto M., Ge N., Flanagan L., de Silva H.A., Kittel A., Saitoh T. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995, 14:467-475.
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    de Silva, H.A.6    Kittel, A.7    Saitoh, T.8
  • 89
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • Lee F.J., Liu F., Pristupa Z.B., Niznik H.B. Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 2001, 15:916-926.
    • (2001) FASEB J. , vol.15 , pp. 916-926
    • Lee, F.J.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 91
    • 24344470188 scopus 로고    scopus 로고
    • Alpha-synuclein activation of protein phosphatase 2A reduces tyrosine hydroxylase phosphorylation in dopaminergic cells
    • Peng X., Tehranian R., Dietrich P., Stefanis L., Perez R.G. Alpha-synuclein activation of protein phosphatase 2A reduces tyrosine hydroxylase phosphorylation in dopaminergic cells. J. Cell Sci. 2005, 118:3523-3530.
    • (2005) J. Cell Sci. , vol.118 , pp. 3523-3530
    • Peng, X.1    Tehranian, R.2    Dietrich, P.3    Stefanis, L.4    Perez, R.G.5
  • 92
    • 77951239770 scopus 로고    scopus 로고
    • The transgenic overexpression of alpha-synuclein and not its related pathology associates with complex I inhibition
    • Loeb V., Yakunin E., Saada A., Sharon R. The transgenic overexpression of alpha-synuclein and not its related pathology associates with complex I inhibition. J. Biol. Chem. 2010, 285:7334-7343.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7334-7343
    • Loeb, V.1    Yakunin, E.2    Saada, A.3    Sharon, R.4
  • 94
    • 84855933800 scopus 로고    scopus 로고
    • Lewy body-related alpha-synucleinopathy in the spinal cord of cases with incidental Lewy body disease
    • Tamura T., Yoshida M., Hashizume Y., Sobue G. Lewy body-related alpha-synucleinopathy in the spinal cord of cases with incidental Lewy body disease. Neuropathology 2012, 32:13-22.
    • (2012) Neuropathology , vol.32 , pp. 13-22
    • Tamura, T.1    Yoshida, M.2    Hashizume, Y.3    Sobue, G.4
  • 95
    • 84872971205 scopus 로고    scopus 로고
    • Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of alpha-synuclein
    • Bae E.J., Ho D.H., Park E., Jung J.W., Cho K., Hong J.H., Lee H.J., Kim K.P., Lee S.J. Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of alpha-synuclein. Antioxid. Redox Signal. 2013, 18:770-783.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 770-783
    • Bae, E.J.1    Ho, D.H.2    Park, E.3    Jung, J.W.4    Cho, K.5    Hong, J.H.6    Lee, H.J.7    Kim, K.P.8    Lee, S.J.9
  • 96
    • 79151470406 scopus 로고    scopus 로고
    • The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of alpha-synuclein oligomers with distinct biochemical, morphological, and functional properties
    • Nasstrom T., Fagerqvist T., Barbu M., Karlsson M., Nikolajeff F., Kasrayan A., Ekberg M., Lannfelt L., Ingelsson M., Bergstrom J. The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of alpha-synuclein oligomers with distinct biochemical, morphological, and functional properties. Free Radic. Biol. Med. 2011, 50:428-437.
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 428-437
    • Nasstrom, T.1    Fagerqvist, T.2    Barbu, M.3    Karlsson, M.4    Nikolajeff, F.5    Kasrayan, A.6    Ekberg, M.7    Lannfelt, L.8    Ingelsson, M.9    Bergstrom, J.10
  • 97
    • 34247130917 scopus 로고    scopus 로고
    • Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation
    • Qin Z., Hu D., Han S., Reaney S.H., Di Monte D.A., Fink A.L. Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation. J. Biol. Chem. 2007, 282:5862-5870.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5862-5870
    • Qin, Z.1    Hu, D.2    Han, S.3    Reaney, S.H.4    Di Monte, D.A.5    Fink, A.L.6
  • 98
    • 0037468467 scopus 로고    scopus 로고
    • Oxidized glutathione stimulated the amyloid formation of alpha-synuclein
    • Paik S.R., Lee D., Cho H.J., Lee E.N., Chang C.S. Oxidized glutathione stimulated the amyloid formation of alpha-synuclein. FEBS Lett. 2003, 537:63-67.
    • (2003) FEBS Lett. , vol.537 , pp. 63-67
    • Paik, S.R.1    Lee, D.2    Cho, H.J.3    Lee, E.N.4    Chang, C.S.5
  • 99
    • 84875935759 scopus 로고    scopus 로고
    • Role of alpha-synuclein aggregation and the nuclear factor E2-related factor 2/heme oxygenase-1 pathway in iron-induced neurotoxicity
    • He Q., Song N., Jia F., Xu H., Yu X., Xie J., Jiang H. Role of alpha-synuclein aggregation and the nuclear factor E2-related factor 2/heme oxygenase-1 pathway in iron-induced neurotoxicity. Int. J. Biochem. Cell Biol. 2013, 45:1019-1030.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 1019-1030
    • He, Q.1    Song, N.2    Jia, F.3    Xu, H.4    Yu, X.5    Xie, J.6    Jiang, H.7
  • 100
    • 80052277569 scopus 로고    scopus 로고
    • Genetic activation of Nrf2 signaling is sufficient to ameliorate neurodegenerative phenotypes in a Drosophila model of Parkinson's disease
    • Barone M.C., Sykiotis G.P., Bohmann D. Genetic activation of Nrf2 signaling is sufficient to ameliorate neurodegenerative phenotypes in a Drosophila model of Parkinson's disease. Dis. Model. Mech. 2011, 4:701-707.
    • (2011) Dis. Model. Mech. , vol.4 , pp. 701-707
    • Barone, M.C.1    Sykiotis, G.P.2    Bohmann, D.3
  • 101
    • 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., Cuadrado A. 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    Cuadrado, A.7
  • 102
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: renovation of cells and tissues
    • Mizushima N., Komatsu M. Autophagy: renovation of cells and tissues. Cell 2011, 147:728-741.
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 104
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon R.A. The role of autophagy in neurodegenerative disease. Nat. Med. 2013, 19:983-997.
    • (2013) Nat. Med. , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 105
    • 84860833596 scopus 로고    scopus 로고
    • Regional deficiencies in chaperone-mediated autophagy underlie alpha-synuclein aggregation and neurodegeneration
    • Malkus K.A., Ischiropoulos H. Regional deficiencies in chaperone-mediated autophagy underlie alpha-synuclein aggregation and neurodegeneration. Neurobiol. Dis. 2012, 46:732-744.
    • (2012) Neurobiol. Dis. , vol.46 , pp. 732-744
    • Malkus, K.A.1    Ischiropoulos, H.2
  • 106
    • 84863456841 scopus 로고    scopus 로고
    • Conditional expression of Parkinson's disease-related mutant alpha-synuclein in the midbrain dopaminergic neurons causes progressive neurodegeneration and degradation of transcription factor nuclear receptor related 1
    • Lin X., Parisiadou L., Sgobio C., Liu G., Yu J., Sun L., Shim H., Gu X.L., Luo J., Long C.X., Ding J., Mateo Y., Sullivan P.H., Wu L.G., Goldstein D.S., Lovinger D., Cai H. Conditional expression of Parkinson's disease-related mutant alpha-synuclein in the midbrain dopaminergic neurons causes progressive neurodegeneration and degradation of transcription factor nuclear receptor related 1. J. Neurosci. 2012, 32:9248-9264.
    • (2012) J. Neurosci. , vol.32 , pp. 9248-9264
    • Lin, X.1    Parisiadou, L.2    Sgobio, C.3    Liu, G.4    Yu, J.5    Sun, L.6    Shim, H.7    Gu, X.L.8    Luo, J.9    Long, C.X.10    Ding, J.11    Mateo, Y.12    Sullivan, P.H.13    Wu, L.G.14    Goldstein, D.S.15    Lovinger, D.16    Cai, H.17
  • 107
    • 78049383132 scopus 로고    scopus 로고
    • Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo
    • Chinta S.J., Mallajosyula J.K., Rane A., Andersen J.K. Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neurosci. Lett. 2010, 486:235-239.
    • (2010) Neurosci. Lett. , vol.486 , pp. 235-239
    • Chinta, S.J.1    Mallajosyula, J.K.2    Rane, A.3    Andersen, J.K.4
  • 110
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process
    • De Strooper B. Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process. Physiol. Rev. 2010, 90:465-494.
    • (2010) Physiol. Rev. , vol.90 , pp. 465-494
    • De Strooper, B.1
  • 112
    • 84880262652 scopus 로고    scopus 로고
    • Attenuation of beta-amyloid-induced oxidative cell death by sulforaphane via activation of NF-E2-related factor 2
    • Lee C., Park G.H., Lee S.R., Jang J.H. Attenuation of beta-amyloid-induced oxidative cell death by sulforaphane via activation of NF-E2-related factor 2. Oxid. Med. Cell. Longev. 2013, 2013:313510.
    • (2013) Oxid. Med. Cell. Longev. , vol.2013 , pp. 313510
    • Lee, C.1    Park, G.H.2    Lee, S.R.3    Jang, J.H.4
  • 113
    • 84862823149 scopus 로고    scopus 로고
    • Allicin ameliorates cognitive deficits ageing-induced learning and memory deficits through enhancing of Nrf2 antioxidant signaling pathways
    • Li X.H., Li C.Y., Lu J.M., Tian R.B., Wei J. Allicin ameliorates cognitive deficits ageing-induced learning and memory deficits through enhancing of Nrf2 antioxidant signaling pathways. Neurosci. Lett. 2012, 514:46-50.
    • (2012) Neurosci. Lett. , vol.514 , pp. 46-50
    • Li, X.H.1    Li, C.Y.2    Lu, J.M.3    Tian, R.B.4    Wei, J.5
  • 114
    • 44249103744 scopus 로고    scopus 로고
    • Kavalactones protect neural cells against amyloid beta peptide-induced neurotoxicity via extracellular signal-regulated kinase 1/2-dependent nuclear factor erythroid 2-related factor 2 activation
    • Wruck C.J., Gotz M.E., Herdegen T., Varoga D., Brandenburg L.O., Pufe T. Kavalactones protect neural cells against amyloid beta peptide-induced neurotoxicity via extracellular signal-regulated kinase 1/2-dependent nuclear factor erythroid 2-related factor 2 activation. Mol. Pharmacol. 2008, 73:1785-1795.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1785-1795
    • Wruck, C.J.1    Gotz, M.E.2    Herdegen, T.3    Varoga, D.4    Brandenburg, L.O.5    Pufe, T.6
  • 115
    • 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
  • 116
    • 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
  • 120
    • 0027519511 scopus 로고
    • Analysis of the huntingtin gene reveals a trinucleotide-length polymorphism in the region of the gene that contains two CCG-rich stretches and a correlation between decreased age of onset of Huntington's disease and CAG repeat number
    • Rubinsztein D.C., Barton D.E., Davison B.C., Ferguson-Smith M.A. Analysis of the huntingtin gene reveals a trinucleotide-length polymorphism in the region of the gene that contains two CCG-rich stretches and a correlation between decreased age of onset of Huntington's disease and CAG repeat number. Hum. Mol. Genet. 1993, 2:1713-1715.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1713-1715
    • Rubinsztein, D.C.1    Barton, D.E.2    Davison, B.C.3    Ferguson-Smith, M.A.4
  • 121
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's disease collaborative research group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's disease collaborative research group. Cell 1993, 72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 123
    • 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., Sporn M., Dumont M., Beal M.F. 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    Sporn, M.7    Dumont, M.8    Beal, M.F.9
  • 124
    • 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., Johnson G.V. 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
    • Jin, Y.N.1    Yu, Y.V.2    Gundemir, S.3    Jo, C.4    Cui, M.5    Tieu, K.6    Johnson, G.V.7
  • 126
    • 58149083873 scopus 로고    scopus 로고
    • Selective turnover of p62/A170/SQSTM1 by autophagy
    • Ichimura Y., Kominami E., Tanaka K., Komatsu M. Selective turnover of p62/A170/SQSTM1 by autophagy. Autophagy 2008, 4:1063-1066.
    • (2008) Autophagy , vol.4 , pp. 1063-1066
    • Ichimura, Y.1    Kominami, E.2    Tanaka, K.3    Komatsu, M.4
  • 130
    • 0033823740 scopus 로고    scopus 로고
    • Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation
    • Kato S., Horiuchi S., Liu J., Cleveland D.W., Shibata N., Nakashima K., Nagai R., Hirano A., Takikawa M., Kato M., Nakano I., Ohama E. Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation. Acta Neuropathol. 2000, 100:490-505.
    • (2000) Acta Neuropathol. , vol.100 , pp. 490-505
    • Kato, S.1    Horiuchi, S.2    Liu, J.3    Cleveland, D.W.4    Shibata, N.5    Nakashima, K.6    Nagai, R.7    Hirano, A.8    Takikawa, M.9    Kato, M.10    Nakano, I.11    Ohama, E.12
  • 136
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C., Polymenidou M., Cleveland D.W. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 2010, 19:R46-R64.
    • (2010) Hum. Mol. Genet. , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 137
    • 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., Hirayama N., Ikeda J.E. 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    Hirayama, N.7    Ikeda, J.E.8
  • 139
    • 84881311668 scopus 로고    scopus 로고
    • Viral delivery of antioxidant genes as a therapeutic strategy in experimental models of amyotrophic lateral sclerosis
    • Nanou A., Higginbottom A., Valori C.F., Wyles M., Ning K., Shaw P., Azzouz M. Viral delivery of antioxidant genes as a therapeutic strategy in experimental models of amyotrophic lateral sclerosis. Mol. Ther. 2013, 21:1486-1496.
    • (2013) Mol. Ther. , vol.21 , pp. 1486-1496
    • Nanou, A.1    Higginbottom, A.2    Valori, C.F.3    Wyles, M.4    Ning, K.5    Shaw, P.6    Azzouz, M.7
  • 140
    • 84873931664 scopus 로고    scopus 로고
    • Absence of Nrf2 or its selective overexpression in neurons and muscle does not affect survival in ALS-linked mutant hSOD1 mouse models
    • Vargas M.R., Burton N.C., Kutzke J., Gan L., Johnson D.A., Schafer M., Werner S., Johnson J.A. Absence of Nrf2 or its selective overexpression in neurons and muscle does not affect survival in ALS-linked mutant hSOD1 mouse models. PLoS One 2013, 8:e56625.
    • (2013) PLoS One , vol.8
    • Vargas, M.R.1    Burton, N.C.2    Kutzke, J.3    Gan, L.4    Johnson, D.A.5    Schafer, M.6    Werner, S.7    Johnson, J.A.8
  • 141
    • 84879676316 scopus 로고    scopus 로고
    • The modest impact of transcription factor Nrf2 on the course of disease in an ALS animal model
    • Guo Y., Zhang Y., Wen D., Duan W., An T., Shi P., Wang J., Li Z., Chen X., Li C. The modest impact of transcription factor Nrf2 on the course of disease in an ALS animal model. Lab. Invest. 2013, 93:825-833.
    • (2013) Lab. Invest. , vol.93 , pp. 825-833
    • Guo, Y.1    Zhang, Y.2    Wen, D.3    Duan, W.4    An, T.5    Shi, P.6    Wang, J.7    Li, Z.8    Chen, X.9    Li, C.10
  • 142
    • 79958262155 scopus 로고    scopus 로고
    • MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1
    • Duan W., Guo Y., Jiang H., Yu X., Li C. MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1. Brain Res. 2011, 1397:1-9.
    • (2011) Brain Res. , vol.1397 , pp. 1-9
    • Duan, W.1    Guo, Y.2    Jiang, H.3    Yu, X.4    Li, C.5
  • 143
    • 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
  • 146
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S., Nitsch R., Grune T., Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 2003, 85:115-122.
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 151
    • 72649092390 scopus 로고    scopus 로고
    • Levels of reduced and oxidized coenzyme Q-10 and 8-hydroxy-2'-deoxyguanosine in the cerebrospinal fluid of patients with living Parkinson's disease demonstrate that mitochondrial oxidative damage and/or oxidative DNA damage contributes to the neurodegenerative process
    • Isobe C., Abe T., Terayama Y. Levels of reduced and oxidized coenzyme Q-10 and 8-hydroxy-2'-deoxyguanosine in the cerebrospinal fluid of patients with living Parkinson's disease demonstrate that mitochondrial oxidative damage and/or oxidative DNA damage contributes to the neurodegenerative process. Neurosci. Lett. 2010, 469:159-163.
    • (2010) Neurosci. Lett. , vol.469 , pp. 159-163
    • Isobe, C.1    Abe, T.2    Terayama, Y.3
  • 154
    • 0025024024 scopus 로고
    • Cytochrome oxidase deficiency in Alzheimer's disease
    • Parker W.D., Filley C.M., Parks J.K. Cytochrome oxidase deficiency in Alzheimer's disease. Neurology 1990, 40:1302-1303.
    • (1990) Neurology , vol.40 , pp. 1302-1303
    • Parker, W.D.1    Filley, C.M.2    Parks, J.K.3
  • 155
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya E.M., Bowling A.C., Beal M.F. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 1994, 63:2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 156
    • 84859454704 scopus 로고    scopus 로고
    • An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
    • Guareschi S., Cova E., Cereda C., Ceroni M., Donetti E., Bosco D.A., Trotti D., Pasinelli P. An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:5074-5079.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5074-5079
    • Guareschi, S.1    Cova, E.2    Cereda, C.3    Ceroni, M.4    Donetti, E.5    Bosco, D.A.6    Trotti, D.7    Pasinelli, P.8
  • 157
    • 84859338362 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency and ATP/ADP ratio in lymphocytes of amyotrophic lateral sclerosis patients
    • Ghiasi P., Hosseinkhani S., Noori A., Nafissi S., Khajeh K. Mitochondrial complex I deficiency and ATP/ADP ratio in lymphocytes of amyotrophic lateral sclerosis patients. Neurol. Res. 2012, 34:297-303.
    • (2012) Neurol. Res. , vol.34 , pp. 297-303
    • Ghiasi, P.1    Hosseinkhani, S.2    Noori, A.3    Nafissi, S.4    Khajeh, K.5
  • 158
    • 0032745071 scopus 로고    scopus 로고
    • Mitochondrial enzyme activity in amyotrophic lateral sclerosis: implications for the role of mitochondria in neuronal cell death
    • Borthwick G.M., Johnson M.A., Ince P.G., Shaw P.J., Turnbull D.M. Mitochondrial enzyme activity in amyotrophic lateral sclerosis: implications for the role of mitochondria in neuronal cell death. Ann. Neurol. 1999, 46:787-790.
    • (1999) Ann. Neurol. , vol.46 , pp. 787-790
    • Borthwick, G.M.1    Johnson, M.A.2    Ince, P.G.3    Shaw, P.J.4    Turnbull, D.M.5
  • 159
    • 0034601407 scopus 로고    scopus 로고
    • Mitochondrial DNA deletion mutation levels are elevated in ALS brains
    • Dhaliwal G.K., Grewal R.P. Mitochondrial DNA deletion mutation levels are elevated in ALS brains. Neuroreport 2000, 11:2507-2509.
    • (2000) Neuroreport , vol.11 , pp. 2507-2509
    • Dhaliwal, G.K.1    Grewal, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.