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Volumn 19, Issue 8, 2013, Pages 823-835

Amyloid β-Peptide (1-42)-induced oxidative stress in alzheimer disease: Importance in disease pathogenesis and progression

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENOLASE; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; BRAIN PROTEIN; FREE RADICAL; GAMMA SECRETASE; LIPID; METHIONINE; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; PEPTIDYLPROLYL ISOMERASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE;

EID: 84877072330     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.5027     Document Type: Review
Times cited : (450)

References (174)
  • 2
    • 0037010314 scopus 로고    scopus 로고
    • Remarkable increase in the concentration of 8-hydroxyguanosine in cerebrospinal fluid from patients with Alzheimer's disease
    • Abe T, Tohgi H, Isobe C, Murata T, and Sato C. Remarkable increase in the concentration of 8-hydroxyguanosine in cerebrospinal fluid from patients with Alzheimer's disease. J Neurosci Res 70: 447-450, 2002.
    • (2002) J Neurosci Res , vol.70 , pp. 447-450
    • Abe, T.1    Tohgi, H.2    Isobe, C.3    Murata, T.4    Sato, C.5
  • 4
    • 79951560784 scopus 로고    scopus 로고
    • Redox proteomics analysis of brains from subjects with amnestic mild cognitive impairment compared to brains from subjects with preclinical Alzheimer's disease: Insights into memory loss in MCI
    • Aluise CD, Robinson RAS, Cai JA, Pierce WM, Markesbery WR, and Butterfield DA. Redox proteomics analysis of brains from subjects with amnestic mild cognitive impairment compared to brains from subjects with preclinical Alzheimer's disease: insights into memory loss in MCI. J Alzheimers Dis 23: 257-269, 2011.
    • (2011) J Alzheimers Dis , vol.23 , pp. 257-269
    • Aluise, C.D.1    Robinson, R.A.S.2    Cai, J.A.3    Pierce, W.M.4    Markesbery, W.R.5    Butterfield, D.A.6
  • 5
    • 33947140574 scopus 로고    scopus 로고
    • Pin1 in Alzheimer's disease: Multiple substrates, one regulatory mechanism
    • Balastik M, Lim J, Pastorino L, and Lu KP. Pin1 in Alzheimer's disease: multiple substrates one regulatory mechanism? Biochim Biophys Acta 1772: 422-429, 2007
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 422-429
    • Balastik, M.1    Lim, J.2    Pastorino, L.3    Lu, K.P.4
  • 7
    • 80052829260 scopus 로고    scopus 로고
    • Oxidative and nitrosative modifications of biliverdin reductase-A in the brain of subjects with Alzheimer's disease and amnestic mild cognitive impairment
    • Barone E, Di Domenico F, Cenini G, Sultana R, Coccia R, Preziosi P, Perluigi M, Mancuso C, and Butterfield DA. Oxidative and nitrosative modifications of biliverdin reductase-A in the brain of subjects with Alzheimer's disease and amnestic mild cognitive impairment. J Alzheimers Dis 25: 623-633, 2011.
    • (2011) J Alzheimers Dis , vol.25 , pp. 623-633
    • Barone, E.1    Di Domenico, F.2    Cenini, G.3    Sultana, R.4    Coccia, R.5    Preziosi, P.6    Perluigi, M.7    Mancuso, C.8    Butterfield, D.A.9
  • 8
    • 84861601576 scopus 로고    scopus 로고
    • Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment
    • Barone E, Di Domenico F, Sultana R, Coccia R, Mancuso C, Perluigi M, and Butterfield DA. Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment. Free Radic Biol Med 52: 2292-2301, 2012.
    • (2012) Free Radic Biol Med , vol.52 , pp. 2292-2301
    • Barone, E.1    Di Domenico, F.2    Sultana, R.3    Coccia, R.4    Mancuso, C.5    Perluigi, M.6    Butterfield, D.A.7
  • 10
    • 10844269704 scopus 로고    scopus 로고
    • Role of phenylalanine 20 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity
    • Boyd-Kimball D, Mohmmad Abdul H, Reed T, Sultana R, and Butterfield DA. Role of phenylalanine 20 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity. Chem Res Toxicol 17: 1743-1749, 2004.
    • (2004) Chem Res Toxicol , vol.17 , pp. 1743-1749
    • Boyd-Kimball, D.1    Mohmmad Abdul, H.2    Reed, T.3    Sultana, R.4    Butterfield, D.A.5
  • 11
    • 33745990556 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): Implications for Alzheimer's disease
    • Boyd-Kimball D, Poon HF, Lynn BC, Cai J, Pierce WM, Jr., Klein JB, Ferguson J, Link CD, and Butterfield DA. Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): implications for Alzheimer's disease. Neurobiol Aging 27: 1239-1249, 2006.
    • (2006) Neurobiol Aging , vol.27 , pp. 1239-1249
    • Boyd-Kimball, D.1    Poon, H.F.2    Lynn, B.C.3    Cai, J.4    Pierce Jr., W.M..5    Klein, J.B.6    Ferguson, J.7    Link, C.D.8    Butterfield, D.A.9
  • 12
    • 54249103057 scopus 로고    scopus 로고
    • Drug development based on the metals hypothesis of Alzheimer's disease
    • Bush AI. Drug development based on the metals hypothesis of Alzheimer's disease. J Alzheimers Dis 15: 223-240, 2008.
    • (2008) J Alzheimers Dis , vol.15 , pp. 223-240
    • Bush, A.I.1
  • 13
    • 0030928406 scopus 로고    scopus 로고
    • Beta-Amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield DA. beta-Amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem Res Toxicol 10: 495-506, 1997.
    • (1997) Chem Res Toxicol , vol.10 , pp. 495-506
    • Butterfield, D.A.1
  • 15
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity
    • Butterfield DA, and Boyd-Kimball D. The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim Biophys Acta 1703: 149-156, 2005.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 16
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • Butterfield DA, Castegna A, Lauderback CM, and Drake J. Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death. Neurobiol Aging 23: 655-664, 2002.
    • (2002) Neurobiol Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 17
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide
    • Butterfield DA, Drake J, Pocernich C, and Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol Med 7: 548-554, 2001.
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 19
    • 33847069643 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: An initial assessment
    • Butterfield DA, Gnjec A, Poon HF, Castegna A, Pierce WM, Klein JB, and Martins RN. Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment. J Alzheimers Dis 10: 391-397, 2006.
    • (2006) J Alzheimers Dis , vol.10 , pp. 391-397
    • Butterfield, D.A.1    Gnjec, A.2    Poon, H.F.3    Castegna, A.4    Pierce, W.M.5    Klein, J.B.6    Martins, R.N.7
  • 21
    • 0035997233 scopus 로고    scopus 로고
    • Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide 1-42
    • Butterfield DA, and Kanski J.Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide 1-42. Peptides 23: 1299-1309, 2002.
    • (2002) Peptides , vol.23 , pp. 1299-1309
    • Butterfield, D.A.1    Kanski, J.2
  • 22
    • 70350129134 scopus 로고    scopus 로고
    • Multifunctional roles of enolase in Alzheimer's disease brain: Beyond altered glucose metabolism
    • Butterfield DA, and Lange ML. Multifunctional roles of enolase in Alzheimer's disease brain: beyond altered glucose metabolism. J Neurochem 111: 915-933, 2009.
    • (2009) J Neurochem , vol.111 , pp. 915-933
    • Butterfield, D.A.1    Lange, M.L.2
  • 23
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid betapeptide-associated free radical oxidative stress
    • Butterfield DA, and Lauderback CM. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid betapeptide-associated free radical oxidative stress. Free Radic Biol Med 32: 1050-1060, 2002.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 25
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease
    • Butterfield DA, Poon HF, Clair DS, Keller JN, Pierce WM, Klein JB, and Markesbery WR. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol Dis 22: 223-232, 2006.
    • (2006) Neurobiol Dis , vol.22 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    Clair, D.S.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6    Markesbery, W.R.7
  • 26
    • 34548588380 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in Alzheimer's disease and mild cognitive impairment: Insights into the progression of this dementing disorder
    • Butterfield DA, and Sultana R. Redox proteomics identification of oxidatively modified brain proteins in Alzheimer's disease and mild cognitive impairment: insights into the progression of this dementing disorder. J Alzheimers Dis 12: 61-72, 2007.
    • (2007) J Alzheimers Dis , vol.12 , pp. 61-72
    • Butterfield, D.A.1    Sultana, R.2
  • 29
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinaserelated protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, and Butterfield DA. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinaserelated protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 82: 1524-1532, 2002.
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 32
    • 9444271637 scopus 로고    scopus 로고
    • The N-terminal copper-binding domain of the amyloid precursor protein protects against Cu2 + neurotoxicity in vivo
    • Cerpa WF, Barria MI, Chacon MA, Suazo M, Gonzalez M, Opazo C, Bush AI, and Inestrosa NC. The N-terminal copper-binding domain of the amyloid precursor protein protects against Cu2 + neurotoxicity in vivo. FASEB J 18: 1701-1703, 2004.
    • (2004) FASEB J , vol.18 , pp. 1701-1703
    • Cerpa, W.F.1    Barria, M.I.2    Chacon, M.A.3    Suazo, M.4    Gonzalez, M.5    Opazo, C.6    Bush, A.I.7    Inestrosa, N.C.8
  • 33
    • 0037461347 scopus 로고    scopus 로고
    • Mild cognitive impairment: Can FDG-PET predict who is to rapidly convert to Alzheimer's disease
    • Chetelat G, Desgranges B, de la Sayette V, Viader F, Eustache F, and Baron JC. Mild cognitive impairment: can FDG-PET predict who is to rapidly convert to Alzheimer's disease? Neurology 60: 1374-1377, 2003.
    • (2003) Neurology , vol.60 , pp. 1374-1377
    • Chetelat, G.1    Desgranges, B.2    De La Sayette, V.3    Viader, F.4    Eustache, F.5    Baron, J.C.6
  • 34
    • 20144379890 scopus 로고    scopus 로고
    • FDG-PET measurement is more accurate than neuropsychological assessments to predict global cognitive deterioration in patients with mild cognitive impairment
    • Chetelat G, Eustache F, Viader F, De La Sayette V, Pelerin A, Mezenge F, Hannequin D, Dupuy B, Baron JC, and Desgranges B. FDG-PET measurement is more accurate than neuropsychological assessments to predict global cognitive deterioration in patients with mild cognitive impairment. Neurocase 11: 14-25, 2005.
    • (2005) Neurocase , vol.11 , pp. 14-25
    • Chetelat, G.1    Eustache, F.2    Viader, F.3    De La Sayette, V.4    Pelerin, A.5    Mezenge, F.6    Hannequin, D.7    Dupuy, B.8    Baron, J.C.9    Desgranges, B.10
  • 36
    • 32644475566 scopus 로고    scopus 로고
    • Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: An intriguing role for methionine 35
    • Clementi ME, Pezzotti M, Orsini F, Sampaolese B, Mezzogori D, Grassi C, Giardina B, and Misiti F. Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: an intriguing role for methionine 35. Biochem Biophys Res Commun 342: 206-213, 2006.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 206-213
    • Clementi, M.E.1    Pezzotti, M.2    Orsini, F.3    Sampaolese, B.4    Mezzogori, D.5    Grassi, C.6    Giardina, B.7    Misiti, F.8
  • 37
    • 0026333250 scopus 로고
    • Beta-amyloid increases neuronal susceptibility to injury by glucose deprivation
    • Copani A, Koh JY, and Cotman CW. Beta-amyloid increases neuronal susceptibility to injury by glucose deprivation. Neuroreport 2: 763-765, 1991.
    • (1991) Neuroreport , vol.2 , pp. 763-765
    • Copani, A.1    Koh, J.Y.2    Cotman, C.W.3
  • 38
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain CC, Ali F, Volitakis I, Cherny RA, Norton RS, Beyreuther K, Barrow CJ, Masters CL, Bush AI, and Barnham KJ. Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J Biol Chem 276: 20466-20473, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 39
    • 33947390936 scopus 로고    scopus 로고
    • Attenuated cytotoxicity but enhanced betafibril of a mutant amyloid beta-peptide with a methionine to cysteine substitution
    • Dai XL, Sun YX, and Jiang ZF. Attenuated cytotoxicity but enhanced betafibril of a mutant amyloid beta-peptide with a methionine to cysteine substitution. FEBS Lett 581: 1269-1274, 2007.
    • (2007) FEBS Lett , vol.581 , pp. 1269-1274
    • Dai, X.L.1    Sun, Y.X.2    Jiang, Z.F.3
  • 42
    • 33745096512 scopus 로고    scopus 로고
    • Decreased RNA, and increased RNA oxidation, in ribosomes from early Alzheimer's disease
    • Ding QX, Markesbery WR, Cecarini V, and Keller JN. Decreased RNA, and increased RNA oxidation, in ribosomes from early Alzheimer's disease. Neurochem Res 31: 705-710, 2006.
    • (2006) Neurochem Res , vol.31 , pp. 705-710
    • Ding, Q.X.1    Markesbery, W.R.2    Cecarini, V.3    Keller, J.N.4
  • 43
    • 12244281810 scopus 로고    scopus 로고
    • Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model
    • Drake J, Link CD, and Butterfield DA. Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model. Neurobiol Aging 24: 415-420, 2003.
    • (2003) Neurobiol Aging , vol.24 , pp. 415-420
    • Drake, J.1    Link, C.D.2    Butterfield, D.A.3
  • 45
    • 78649332606 scopus 로고    scopus 로고
    • Pin1: A new genetic link between Alzheimer's disease, cancer and aging
    • Driver JA, and Lu KP. Pin1: a new genetic link between Alzheimer's disease, cancer and aging. Curr Aging Sci 3: 158-165, 2010.
    • (2010) Curr Aging Sci , vol.3 , pp. 158-165
    • Driver, J.A.1    Lu, K.P.2
  • 46
    • 34147219544 scopus 로고    scopus 로고
    • Fronto-temporal-lobe atrophy in early-stage Alzheimer's disease identified using an improved detection methodology
    • Farrow TF, Thiyagesh SN, Wilkinson ID, Parks RW, Ingram L, and Woodruff PW. Fronto-temporal-lobe atrophy in early-stage Alzheimer's disease identified using an improved detection methodology. Psychiatry Res 155: 11-19, 2007.
    • (2007) Psychiatry Res , vol.155 , pp. 11-19
    • Farrow, T.F.1    Thiyagesh, S.N.2    Wilkinson, I.D.3    Parks, R.W.4    Ingram, L.5    Woodruff, P.W.6
  • 47
    • 0016823810 scopus 로고
    • "Mini-mental state. " A practical method for grading the cognitive state of patients for the clinician
    • Folstein MF, Folstein SE, and McHugh PR. "Mini-mental state." A practical method for grading the cognitive state of patients for the clinician. J Psychiatr Res 12: 189-198, 1975.
    • (1975) J Psychiatr Res , vol.12 , pp. 189-198
    • Folstein, M.F.1    Folstein, S.E.2    McHugh, P.R.3
  • 48
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita SP, Aksenov MY, Lovell MA, and Markesbery WR. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J Neurochem 73: 1660-1666, 1999.
    • (1999) J Neurochem , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 49
    • 0031754202 scopus 로고    scopus 로고
    • Increased nuclear DNA oxidation in the brain in Alzheimer's disease
    • Gabbita SP, Lovell MA, and Markesbery WR. Increased nuclear DNA oxidation in the brain in Alzheimer's disease. J Neurochem 71: 2034-2040, 1998.
    • (1998) J Neurochem , vol.71 , pp. 2034-2040
    • Gabbita, S.P.1    Lovell, M.A.2    Markesbery, W.R.3
  • 50
    • 79952278055 scopus 로고    scopus 로고
    • Targeting amyloid precursor protein secretases: Alzheimer's disease and beyond
    • Ganjei JK. Targeting amyloid precursor protein secretases: Alzheimer's disease and beyond. Drug News Perspect 23: 573-584, 2010.
    • (2010) Drug News Perspect , vol.23 , pp. 573-584
    • Ganjei, J.K.1
  • 52
    • 0031964036 scopus 로고    scopus 로고
    • Relationship between plaques, tangles, and loss of cortical cholinergic fibers in Alzheimer disease
    • Geula C, Mesulam MM, Saroff DM, and Wu CK. Relationship between plaques, tangles, and loss of cortical cholinergic fibers in Alzheimer disease. J Neuropathol Exp Neurol 57: 63-75, 1998.
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 63-75
    • Geula, C.1    Mesulam, M.M.2    Saroff, D.M.3    Wu, C.K.4
  • 53
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid accumulation and pathogenesis of Alzheimer's disease: Significance of monomeric, oligomeric and fibrillar Abeta
    • Glabe CC. Amyloid accumulation and pathogenesis of Alzheimer's disease: significance of monomeric, oligomeric and fibrillar Abeta. Subcell Biochem 38: 167-177, 2005.
    • (2005) Subcell Biochem , vol.38 , pp. 167-177
    • Glabe, C.C.1
  • 54
    • 84880186196 scopus 로고    scopus 로고
    • Segregation of a missense mutation in the amyloid beta-protein precursor gene with familial Alzheimer's disease
    • Goate A. Segregation of a missense mutation in the amyloid beta-protein precursor gene with familial Alzheimer's disease. J Alzheimers Dis 9: 341-347, 2006.
    • (2006) J Alzheimers Dis , vol.9 , pp. 341-347
    • Goate, A.1
  • 55
    • 84655162701 scopus 로고    scopus 로고
    • Twenty years of Alzheimer's diseasecausing mutations
    • Goate A, and Hardy J. Twenty years of Alzheimer's diseasecausing mutations. J Neurochem 120 Suppl 1: 3-8, 2012.
    • (2012) J Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 3-8
    • Goate, A.1    Hardy, J.2
  • 57
    • 0038326624 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment
    • Guillozet AL, Weintraub S, Mash DC, and Mesulam MM. Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment. Arch Neurol 60: 729-736, 2003.
    • (2003) Arch Neurol , vol.60 , pp. 729-736
    • Guillozet, Al.1    Weintraub, S.2    Mash, D.C.3    Mesulam, M.M.4
  • 58
  • 59
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • Halliwell B, and Gutteridge JM. Biologically relevant metal ion-dependent hydroxyl radical generation. An update. FEBS Lett 307: 108-112, 1992.
    • (1992) FEBS Lett , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 60
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, and Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356, 2002.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 61
    • 0028899956 scopus 로고
    • Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat-brain
    • Hattori T, Takei N, Mizuno Y, Kato K, and Kohsaka S. Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat-brain. Neurosci Res 21: 191-198, 1995.
    • (1995) Neurosci Res , vol.21 , pp. 191-198
    • Hattori, T.1    Takei, N.2    Mizuno, Y.3    Kato, K.4    Kohsaka, S.5
  • 62
    • 0042023711 scopus 로고    scopus 로고
    • Alzheimer disease in the US population-prevalence estimates using the 2000 census
    • Hebert LE, Scherr PA, Bienias JL, Bennett DA, and Evans DA. Alzheimer disease in the US population-prevalence estimates using the 2000 census. Arch Neurol 60: 1119-1122, 2003.
    • (2003) Arch Neurol , vol.60 , pp. 1119-1122
    • Hebert, L.E.1    Scherr, P.A.2    Bienias, J.L.3    Bennett, D.A.4    Evans, D.A.5
  • 64
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates regionspecific accumulation
    • Hensley K, Maidt ML, Yu ZQ, Sang H, Markesbery WR, and Floyd RA. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates regionspecific accumulation. J Neurosci 18: 8126-8132, 1998.
    • (1998) J Neurosci , vol.18 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.Q.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 69
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N, Hartmann T, Pantel J, Schroder J, Zerfass R, Forstl H, Sandbrink R, Masters CL, and Beyreuther K. Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J Biol Chem 271: 22908-22914, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 71
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, and Lansbury PT, Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-4697, 1993.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 72
    • 79956320988 scopus 로고    scopus 로고
    • Age-dependent accumulation of soluble amyloid beta (Abeta) oligomers reverses the neuroprotective effect of soluble amyloid precursor protein-alpha (sAPP(alpha)) by modulating phosphatidylinositol 3-kinase (PI3K)/Akt-GSK-3beta pathway in Alzheimer mouse model
    • Jimenez S, Torres M, Vizuete M, Sanchez-Varo R, Sanchez-Mejias E, Trujillo-Estrada L, Carmona-Cuenca I, Caballero C, Ruano D, Gutierrez A, and Vitorica J. Age-dependent accumulation of soluble amyloid beta (Abeta) oligomers reverses the neuroprotective effect of soluble amyloid precursor protein-alpha (sAPP(alpha)) by modulating phosphatidylinositol 3-kinase (PI3K)/Akt-GSK-3beta pathway in Alzheimer mouse model. J Biol Chem 286: 18414-18425, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 18414-18425
    • Jimenez, S.1    Torres, M.2    Vizuete, M.3    Sanchez-Varo, R.4    Sanchez-Mejias, E.5    Trujillo-Estrada, L.6    Carmona-Cuenca, I.7    Caballero, C.8    Ruano, D.9    Gutierrez, A.10    Vitorica, J.11
  • 73
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • Jin M, Shepardson N, Yang T, Chen G, Walsh D, and Selkoe DJ. Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc Natl Acad Sci U S A 108: 5819-5824, 2011.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 75
    • 78449282609 scopus 로고    scopus 로고
    • Metals, oxidative stress and neurodegenerative disorders
    • Jomova K, Vondrakova D, Lawson M, and Valko M. Metals, oxidative stress and neurodegenerative disorders. Mol Cell Biochem 345: 91-104, 2010.
    • (2010) Mol Cell Biochem , vol.345 , pp. 91-104
    • Jomova, K.1    Vondrakova, D.2    Lawson, M.3    Valko, M.4
  • 76
    • 84859428415 scopus 로고    scopus 로고
    • Vitamin e in aging, dementia, and Alzheimer's disease
    • Joshi YB, and Pratico D. Vitamin E in aging, dementia, and Alzheimer's disease. Biofactors 38: 90-97, 2012.
    • (2012) Biofactors , vol.38 , pp. 90-97
    • Joshi, Y.B.1    Pratico, D.2
  • 77
    • 0032401643 scopus 로고    scopus 로고
    • Biomarkers of oxidative stress are significantly elevated in Down syndrome
    • Jovanovic SV, Clements D, and MacLeod K. Biomarkers of oxidative stress are significantly elevated in Down syndrome. Free Radic Biol Med 25: 1044-1048, 1998.
    • (1998) Free Radic Biol Med , vol.25 , pp. 1044-1048
    • Jovanovic, S.V.1    Clements, D.2    Macleod, K.3
  • 78
    • 0036087081 scopus 로고    scopus 로고
    • The hydrophobic environment of Met35 of Alzheimer's Abeta(1-42) is important for the neurotoxic and oxidative properties of the peptide
    • Kanski J, Aksenova M, and Butterfield DA. The hydrophobic environment of Met35 of Alzheimer's Abeta(1-42) is important for the neurotoxic and oxidative properties of the peptide. Neurotox Res 4: 219-223, 2002.
    • (2002) Neurotox Res , vol.4 , pp. 219-223
    • Kanski, J.1    Aksenova, M.2    Butterfield, D.A.3
  • 79
    • 0036591863 scopus 로고    scopus 로고
    • Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide
    • Kanski J, Aksenova M, Schoneich C, and Butterfield DA. Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide. Free Radic Biol Med 32: 1205-1211, 2002.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1205-1211
    • Kanski, J.1    Aksenova, M.2    Schoneich, C.3    Butterfield, D.A.4
  • 80
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • Katzman R, and Saitoh T. Advances in Alzheimer's disease. FASEB J 5: 278-286, 1991.
    • (1991) FASEB J , vol.5 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 83
    • 0032948006 scopus 로고    scopus 로고
    • Peroxynitrite-inducedalterations in synaptosomal membrane proteins: Insight into oxidative stress in Alzheimer's disease
    • Koppal T, Drake J, Yatin S, Jordan B, Varadarajan S, Bettenhausen L, andButterfieldDA. Peroxynitrite-inducedalterations in synaptosomal membrane proteins: insight into oxidative stress in Alzheimer's disease. J Neurochem 72: 310-317, 1999.
    • (1999) J Neurochem , vol.72 , pp. 310-317
    • Koppal, T.1    Drake, J.2    Yatin, S.3    Jordan, B.4    Varadarajan, S.5    Bettenhausen, L.6    Andbutterfield, D.A.7
  • 85
    • 0034925118 scopus 로고    scopus 로고
    • The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: The role of A beta 1-42
    • Lauderback CM, Hackett JM, Huang FF, Keller JN, Szweda LI, Markesbery WR, and Butterfield DA. The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of A beta 1-42. J Neurochem 78: 413-416, 2001.
    • (2001) J Neurochem , vol.78 , pp. 413-416
    • Lauderback, C.M.1    Hackett, J.M.2    Huang, F.F.3    Keller, J.N.4    Szweda, L.I.5    Markesbery, W.R.6    Butterfield, D.A.7
  • 87
  • 88
    • 38149087424 scopus 로고    scopus 로고
    • Oxidativelymodified RNA in mild cognitive impairment
    • LovellMA, and Markesbery WR. Oxidativelymodified RNA in mild cognitive impairment. Neurobiol Dis 29: 169-175, 2008.
    • (2008) Neurobiol Dis , vol.29 , pp. 169-175
    • Lovell, M.A.1    Markesbery, W.R.2
  • 89
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu PJ, Wulf G, Zhou XZ, Davies P, and Lu KP. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399: 784-788, 1999.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 90
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S, and Levine RL. Methionine in proteins defends against oxidative stress. FASEB J 23: 464-472, 2009.
    • (2009) FASEB J , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 91
    • 84863230253 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 promotes amyloid precursor protein (APP) turnover by inhibiting glycogen synthase kinase-3beta (GSK3beta) activity: Novel mechanism for Pin1 to protect against Alzheimer disease
    • Ma SL, Pastorino L, Zhou XZ, and Lu KP. Prolyl isomerase Pin1 promotes amyloid precursor protein (APP) turnover by inhibiting glycogen synthase kinase-3beta (GSK3beta) activity: novel mechanism for Pin1 to protect against Alzheimer disease. J Biol Chem 287: 6969-6973, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 6969-6973
    • Ma, S.L.1    Pastorino, L.2    Zhou, X.Z.3    Lu, K.P.4
  • 92
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid betapeptide
    • Mark RJ, Lovell MA, Markesbery WR, Uchida K, and Mattson MP. A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid betapeptide. J Neurochem 68: 255-264, 1997.
    • (1997) J Neurochem , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 93
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery WR. Oxidative stress hypothesis in Alzheimer's disease. Free Radic Biol Med 23: 134-147, 1997.
    • (1997) Free Radic Biol Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 94
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery WR, and Carney JM. Oxidative alterations in Alzheimer's disease. Brain Pathol 9: 133-146, 1999.
    • (1999) Brain Pathol , vol.9 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 95
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • Markesbery WR, Kryscio RJ, Lovell MA, and Morrow JD. Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment. Ann Neurol 58: 730-735, 2005.
    • (2005) Ann Neurol , vol.58 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 96
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery WR, and Lovell MA. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol Aging 19: 33-36, 1998.
    • (1998) Neurobiol Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 100
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson MP. Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol Rev 77: 1081-1132, 1997.
    • (1997) Physiol Rev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 103
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • Mecocci P, MacGarvey U, and Beal MF. Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Ann Neurol 36: 747-751, 1994.
    • (1994) Ann Neurol , vol.36 , pp. 747-751
    • Mecocci, P.1    Macgarvey, U.2    Beal, M.F.3
  • 106
    • 77249086074 scopus 로고    scopus 로고
    • Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1-42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and function
    • Misiti F, Clementi ME, and Giardina B. Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1-42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and function. Neurochem Int 56: 597-602, 2010.
    • (2010) Neurochem Int , vol.56 , pp. 597-602
    • Misiti, F.1    Clementi, M.E.2    Giardina, B.3
  • 107
    • 33645106304 scopus 로고    scopus 로고
    • Mutations in amyloid precursor protein and presenilin-1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid beta-peptide (1-42), HO and kainic acid: Implications for Alzheimer's disease
    • Mohmmad Abdul H, Sultana R, Keller JN, St Clair DK, Markesbery WR, and Butterfield DA. Mutations in amyloid precursor protein and presenilin-1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid beta-peptide (1-42), HO and kainic acid: implications for Alzheimer's disease. J Neurochem 96: 1322-1335, 2006.
    • (2006) J Neurochem , vol.96 , pp. 1322-1335
    • Mohmmad Abdul, H.1    Sultana, R.2    Keller, J.N.3    St Clair, D.K.4    Markesbery, W.R.5    Butterfield, D.A.6
  • 113
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, and Tessier-Lavigne M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457: 981-989, 2009.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 118
    • 69249212154 scopus 로고    scopus 로고
    • Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein
    • Park SA, Shaked GM, Bredesen DE, and Koo EH. Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein. Biochem Biophys Res Commun 388: 450-455, 2009.
    • (2009) Biochem Biophys Res Commun , vol.388 , pp. 450-455
    • Park, S.A.1    Shaked, G.M.2    Bredesen, D.E.3    Koo, E.H.4
  • 119
    • 80051723535 scopus 로고    scopus 로고
    • The identification of protein biomarkers for oxidative stress in Down syndrome
    • Perluigi M, and Butterfield DA. The identification of protein biomarkers for oxidative stress in Down syndrome. Expert Rev Proteomics 8: 427-429, 2011.
    • (2011) Expert Rev Proteomics , vol.8 , pp. 427-429
    • Perluigi, M.1    Butterfield, D.A.2
  • 120
    • 84855583479 scopus 로고    scopus 로고
    • Oxidative stress and Down syndrome: A route toward Alzheimer-like dementia
    • Perluigi M, and Butterfield DA. Oxidative stress and Down syndrome: a route toward Alzheimer-like dementia. Curr Gerontol Geriatr Res 2012: 724904, 2012.
    • (2012) Curr Gerontol Geriatr Res , vol.2012 , pp. 724904
    • Perluigi, M.1    Butterfield, D.A.2
  • 121
    • 70350089195 scopus 로고    scopus 로고
    • Redox proteomics identification of 4-hydroxynonenal-modified brain proteins in Alzheimer's disease: Role of lipid peroxidation in Alzheimer's disease pathogenesis
    • Perluigi M, Sultana R, Cenini G, Di Domenico F, Memo M, Pierce WM, Coccia R, and Butterfield DA. Redox proteomics identification of 4-hydroxynonenal- modified brain proteins in Alzheimer's disease: role of lipid peroxidation in Alzheimer's disease pathogenesis. Proteomics Clin Appl 3: 682-693, 2009.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 682-693
    • Perluigi, M.1    Sultana, R.2    Cenini, G.3    Di Domenico, F.4    Memo, M.5    Pierce, W.M.6    Coccia, R.7    Butterfield, D.A.8
  • 122
    • 0034087231 scopus 로고    scopus 로고
    • Mild cognitive impairment: Transition between aging and Alzheimer's disease
    • Petersen RC. Mild cognitive impairment: transition between aging and Alzheimer's disease. Neurologia 15: 93-101, 2000.
    • (2000) Neurologia , vol.15 , pp. 93-101
    • Petersen, R.C.1
  • 123
    • 4544335597 scopus 로고    scopus 로고
    • Mild cognitive impairment as a diagnostic entity
    • Petersen RC. Mild cognitive impairment as a diagnostic entity. J Intern Med 256: 183-194, 2004.
    • (2004) J Intern Med , vol.256 , pp. 183-194
    • Petersen, R.C.1
  • 124
    • 66249116626 scopus 로고    scopus 로고
    • Preclinical evidence of Alzheimer changes: Convergent cerebrospinal fluid biomarker and fluorodeoxyglucose positron emission tomography findings
    • Petrie EC, Cross DJ, Galasko D, Schellenberg GD, Raskind MA, Peskind ER, and Minoshima S. Preclinical evidence of Alzheimer changes: convergent cerebrospinal fluid biomarker and fluorodeoxyglucose positron emission tomography findings. Arch Neurol 66: 632-637, 2009.
    • (2009) Arch Neurol , vol.66 , pp. 632-637
    • Petrie, E.C.1    Cross, D.J.2    Galasko, D.3    Schellenberg, G.D.4    Raskind, M.A.5    Peskind, E.R.6    Minoshima, S.7
  • 125
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG, and Cotman CW. Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity. J Neurochem 64: 253-265, 1995.
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 126
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modeling study
    • Pogocki D, and Schoneich C. Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modeling study. Chem Res Toxicol 15: 408-418, 2002.
    • (2002) Chem Res Toxicol , vol.15 , pp. 408-418
    • Pogocki, D.1    Schoneich, C.2
  • 127
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R, Lu KP, Hunter T, and Noel JP. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89: 875-886, 1997.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 128
    • 40849120274 scopus 로고    scopus 로고
    • Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: Insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease
    • ReedT, PerluigiM, SultanaR, PierceWM,Klein JB, TurnerDM, Coccia R, Markesbery WR, and Butterfield DA. Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease. Neurobiol Dis 30: 107-120, 2008.
    • (2008) Neurobiol Dis , vol.30 , pp. 107-120
    • Reed, T.1    Perluigi, M.2    Sultana, R.3    Pierce, W.M.4    Klein, J.B.5    Turner, D.M.6    Coccia, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 129
    • 67849126232 scopus 로고    scopus 로고
    • Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule
    • Reed TT, Pierce WM, Jr., Turner DM, Markesbery WR, and Butterfield DA. Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule. J Cell Mol Med 13: 2019-2029, 2009.
    • (2009) J Cell Mol Med , vol.13 , pp. 2019-2029
    • Reed, T.T.1    Pierce Jr., W.M..2    Turner, D.M.3    Markesbery, W.R.4    Butterfield, D.A.5
  • 130
    • 67349279818 scopus 로고    scopus 로고
    • Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD
    • Reed TT, Pierce WM, Markesbery WR, and Butterfield DA. Proteomic identification of HNE-bound proteins in early Alzheimer disease: insights into the role of lipid peroxidation in the progression of AD. Brain Res 1274: 66-76, 2009.
    • (2009) Brain Res , vol.1274 , pp. 66-76
    • Reed, T.T.1    Pierce, W.M.2    Markesbery, W.R.3    Butterfield, D.A.4
  • 134
    • 73949117777 scopus 로고    scopus 로고
    • Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures
    • Schmidt M, Sachse C, Richter W, Xu C, Fandrich M, and Grigorieff N. Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci U S A 106: 19813-19818, 2009.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19813-19818
    • Schmidt, M.1    Sachse, C.2    Richter, W.3    Xu, C.4    Fandrich, M.5    Grigorieff, N.6
  • 135
    • 12844260763 scopus 로고    scopus 로고
    • Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease
    • Schoneich C. Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease. Biochim Biophys Acta 1703: 111-119, 2005.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 111-119
    • Schoneich, C.1
  • 136
    • 0038676610 scopus 로고    scopus 로고
    • Free radical reactions of methionine in peptides: Mechanisms relevant to beta-amyloid oxidation and Alzheimer's disease
    • Schoneich C, Pogocki D, Hug GL, and Bobrowski K. Free radical reactions of methionine in peptides: mechanisms relevant to beta-amyloid oxidation and Alzheimer's disease. J Am Chem Soc 125: 13700-13713, 2003.
    • (2003) J Am Chem Soc , vol.125 , pp. 13700-13713
    • Schoneich, C.1    Pogocki, D.2    Hug, G.L.3    Bobrowski, K.4
  • 137
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81: 741-766, 2001.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 138
    • 33645961571 scopus 로고    scopus 로고
    • Quantification of oxidized RNAs in Alzheimer's disease
    • Shan X, and Lin CLG. Quantification of oxidized RNAs in Alzheimer's disease. Neurobiol Aging 27: 657-662, 2006.
    • (2006) Neurobiol Aging , vol.27 , pp. 657-662
    • Shan, X.1    Lin, C.L.G.2
  • 139
    • 0038417076 scopus 로고    scopus 로고
    • The identification and characterization of oxidized RNAs in Alzheimer's disease
    • Shan X, Tashiro H, and Lin CLG. The identification and characterization of oxidized RNAs in Alzheimer's disease. J Neurosci 23: 4913-4921, 2003.
    • (2003) J Neurosci , vol.23 , pp. 4913-4921
    • Shan, X.1    Tashiro, H.2    Lin, C.L.G.3
  • 140
    • 0034780583 scopus 로고    scopus 로고
    • Canaries in a coal mine: Cognitive markers of preclinical Alzheimer disease
    • Small BJ, Fratiglioni L, and Backman L. Canaries in a coal mine: cognitive markers of preclinical Alzheimer disease. Arch Gen Psychiatry 58: 859-860, 2001.
    • (2001) Arch Gen Psychiatry , vol.58 , pp. 859-860
    • Small, B.J.1    Fratiglioni, L.2    Backman, L.3
  • 141
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid beta peptide
    • Smith DG, Cappai R, and Barnham KJ. The redox chemistry of the Alzheimer's disease amyloid beta peptide. Biochim Biophys Acta 1768: 1976-1990, 2007.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 144
    • 1042302134 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of methionine residues of proteins in antioxidant defense and cellular regulation
    • Stadtman ER. Cyclic oxidation and reduction of methionine residues of proteins in antioxidant defense and cellular regulation. Arch Biochem Biophys 423: 2-5, 2004.
    • (2004) Arch Biochem Biophys , vol.423 , pp. 2-5
    • Stadtman, E.R.1
  • 145
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: Biological consequences
    • Stadtman ER, Moskovitz J, and Levine RL. Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 5: 577-582, 2003.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 146
    • 0034009502 scopus 로고    scopus 로고
    • Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene
    • Subramanian A, and Miller DM. Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. J Biol Chem 275: 5958-5965, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 5958-5965
    • Subramanian, A.1    Miller, D.M.2
  • 149
    • 75149118997 scopus 로고    scopus 로고
    • Role of oxidative stress in the progression of Alzheimer's disease
    • Sultana R, and Butterfield DA. Role of oxidative stress in the progression of Alzheimer's disease. J Alzheimers Dis 19: 341-353, 2010.
    • (2010) J Alzheimers Dis , vol.19 , pp. 341-353
    • Sultana, R.1    Butterfield, D.A.2
  • 150
    • 79955658979 scopus 로고    scopus 로고
    • Increased protein and lipid oxidative damage in mitochondria isolated from lymphocytes from patients with Alzheimer's disease: Insights into the role of oxidative stress in Alzheimer's disease and initial investigations into a potential biomarker for this dementing disorder
    • Sultana R, Mecocci P, Mangialasche F, Cecchetti R, Baglioni M, and Butterfield DA. Increased protein and lipid oxidative damage in mitochondria isolated from lymphocytes from patients with Alzheimer's disease: insights into the role of oxidative stress in Alzheimer's disease and initial investigations into a potential biomarker for this dementing disorder. J Alzheimers Dis 24: 77-84, 2011.
    • (2011) J Alzheimers Dis , vol.24 , pp. 77-84
    • Sultana, R.1    Mecocci, P.2    Mangialasche, F.3    Cecchetti, R.4    Baglioni, M.5    Butterfield, D.A.6
  • 151
    • 33644913675 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta(1-42)
    • Sultana R, Perluigi M, and Butterfield DA. Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta(1-42). J Chromatogr B Analyt Technol Biomed Life Sci 833: 3-11, 2006.
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.833 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 152
    • 56349091788 scopus 로고    scopus 로고
    • Protein levels and activity of some antioxidant enzymes in hippocampus of subjects with amnestic mild cognitive impairment
    • Sultana R, Piroddi M, Galli F, and Butterfield D. Protein levels and activity of some antioxidant enzymes in hippocampus of subjects with amnestic mild cognitive impairment. Neurochem Res 33: 2540-2546, 2008.
    • (2008) Neurochem Res , vol.33 , pp. 2540-2546
    • Sultana, R.1    Piroddi, M.2    Galli, F.3    Butterfield, D.4
  • 154
    • 34548172399 scopus 로고    scopus 로고
    • Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: A regional study
    • Sultana R, Reed T, Perluigi M, Coccia R, Pierce WM, and Butterfield DA. Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: a regional study. J Cell Mol Med 11: 839-851, 2007.
    • (2007) J Cell Mol Med , vol.11 , pp. 839-851
    • Sultana, R.1    Reed, T.2    Perluigi, M.3    Coccia, R.4    Pierce, W.M.5    Butterfield, D.A.6
  • 155
    • 84866857074 scopus 로고    scopus 로고
    • Do proteomics analyses provide insights into reduced oxidative stress in the brain of an Alzheimer disease transgenic mouse model with an M631L amyloid precursor protein substitution and thereby the importance of amyloid-beta-resident methionine 35 in Alzheimer disease pathogenesis
    • Sultana R, Robinson RA, Bader LangeM, Fiorini A, Galvan V, Fombonne J, Baker A, Gorostiza O, Zhang J, Cai J, Pierce WM, Bredesen DE, and Butterfield DA. Do proteomics analyses provide insights into reduced oxidative stress in the brain of an Alzheimer disease transgenic mouse model with an M.631L amyloid precursor protein substitution and thereby the importance of amyloid-beta-resident methionine 35 in Alzheimer disease pathogenesis? Antioxid Redox Signal 17: 1507-1514, 2012.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 1507-1514
    • Sultana, R.1    Robinson, R.A.2    Bader, LangeM.3    Fiorini, A.4    Galvan, V.5    Fombonne, J.6    Baker, A.7    Gorostiza, O.8    Zhang, J.9    Cai, J.10    Pierce, W.M.11    Bredesen, D.E.12    Butterfield, D.A.13
  • 156
    • 0025945872 scopus 로고
    • Neuronal survival factor from bovine brain is identical to neuron-specific enolase
    • Takei N, Kondo J, Nagaike K, Ohsawa K, Kato K, and Kohsaka S. Neuronal survival factor from bovine brain is identical to neuron-specific enolase. J Neurochem 57: 1178-1184, 1991.
    • (1991) J Neurochem , vol.57 , pp. 1178-1184
    • Takei, N.1    Kondo, J.2    Nagaike, K.3    Ohsawa, K.4    Kato, K.5    Kohsaka, S.6
  • 157
    • 38049018185 scopus 로고    scopus 로고
    • Biochemical characterization of Abeta and tau pathologies in mild cognitive impairment and Alzheimer's disease
    • Tremblay C, Pilote M, Phivilay A, Emond V, Bennett DA, and Calon F. Biochemical characterization of Abeta and tau pathologies in mild cognitive impairment and Alzheimer's disease. J Alzheimers Dis 12: 377-390, 2007.
    • (2007) J Alzheimers Dis , vol.12 , pp. 377-390
    • Tremblay, C.1    Pilote, M.2    Phivilay, A.3    Emond, V.4    Bennett, D.A.5    Calon, F.6
  • 158
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35)
    • Varadarajan S, Kanski J, Aksenova M, Lauderback C, and Butterfield DA. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35). J Am Chem Soc 123: 5625-5631, 2001.
    • (2001) J Am Chem Soc , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 159
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S, Yatin S, Aksenova M, and Butterfield DA. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 130: 184-208, 2000.
    • (2000) J Struct Biol , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 160
    • 0032880901 scopus 로고    scopus 로고
    • Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress
    • Varadarajan S, Yatin S, Kanski J, Jahanshahi F, and Butterfield DA. Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress. Brain Res Bull 50: 133-141, 1999.
    • (1999) Brain Res Bull , vol.50 , pp. 133-141
    • Varadarajan, S.1    Yatin, S.2    Kanski, J.3    Jahanshahi, F.4    Butterfield, D.A.5
  • 162
    • 0027379395 scopus 로고
    • Characterization of beta-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I, and Schenk DB. Characterization of beta-amyloid peptide from human cerebrospinal fluid. J Neurochem 61: 1965-1968, 1993.
    • (1993) J Neurochem , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 163
    • 38549152764 scopus 로고    scopus 로고
    • Why Alzheimer's is a disease of memory: The attack on synapses by A beta oligomers (ADDLs)
    • Viola KL, Velasco PT, and Klein WL. Why Alzheimer's is a disease of memory: the attack on synapses by A beta oligomers (ADDLs). J Nutr Health Aging 12: 51S-57S, 2008.
    • (2008) J Nutr Health Aging , vol.12
    • Viola, K.L.1    Velasco, P.T.2    Klein, W.L.3
  • 164
  • 166
  • 167
    • 84859610500 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid beta-protein
    • Walsh DM, and Teplow DB. Alzheimer's disease and the amyloid beta-protein. ProgMol Biol Transl Sci 107: 101-124, 2012.
    • (2012) ProgMol Biol Transl Sci , vol.107 , pp. 101-124
    • Walsh, D.M.1    Teplow, D.B.2
  • 168
    • 78650685650 scopus 로고    scopus 로고
    • Beta-Amyloid peptide increases levels of iron content and oxidative stress in human cell and Caenorhabditis elegans models of Alzheimer disease
    • Wan L, Nie G, Zhang J, Luo Y, Zhang P, Zhang Z, and Zhao B. beta-Amyloid peptide increases levels of iron content and oxidative stress in human cell and Caenorhabditis elegans models of Alzheimer disease. Free Radic Biol Med 50: 122-129, 2010.
    • (2010) Free Radic Biol Med , vol.50 , pp. 122-129
    • Wan, L.1    Nie, G.2    Zhang, J.3    Luo, Y.4    Zhang, P.5    Zhang, Z.6    Zhao, B.7
  • 169
    • 33645106680 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment
    • Wang J, Markesbery WR, and Lovell MA. Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment. J Neurochem 96: 825-832, 2006.
    • (2006) J Neurochem , vol.96 , pp. 825-832
    • Wang, J.1    Markesbery, W.R.2    Lovell, M.A.3
  • 171
    • 25444475777 scopus 로고    scopus 로고
    • Elevation of 12/15 lipoxygenase products in AD and mild cognitive impairment
    • Yao Y, Clark CM, Trojanowski JQ, Lee VM, and Pratico D. Elevation of 12/15 lipoxygenase products in AD and mild cognitive impairment. Ann Neurol 58: 623-626, 2005.
    • (2005) Ann Neurol , vol.58 , pp. 623-626
    • Yao, Y.1    Clark, C.M.2    Trojanowski, J.Q.3    Lee, V.M.4    Pratico, D.5
  • 172
    • 0033788416 scopus 로고    scopus 로고
    • Vitamin e prevents Alzheimer's amyloid beta-peptide (1-42)-induced neuronal protein oxidation and reactive oxygen species production
    • Yatin SM, Varadarajan S, and Butterfield DA. Vitamin E prevents Alzheimer's amyloid beta-peptide (1-42)-induced neuronal protein oxidation and reactive oxygen species production. J Alzheimers Dis 2: 123-131, 2000.
    • (2000) J Alzheimers Dis , vol.2 , pp. 123-131
    • Yatin, S.M.1    Varadarajan, S.2    Butterfield, D.A.3
  • 173
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42)
    • discussion 339-342
    • Yatin SM, Varadarajan S, Link CD, and Butterfield DA. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42). Neurobiol Aging 20: 325-330; discussion 339-342, 1999.
    • (1999) Neurobiol Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4
  • 174
    • 33847724188 scopus 로고    scopus 로고
    • The amyloid precursor protein: Beyond amyloid
    • Zheng H, and Koo EH. The amyloid precursor protein: beyond amyloid. Mol Neurodegener 1: 5, 2006.
    • (2006) Mol Neurodegener , vol.1 , pp. 5
    • Zheng, H.1    Koo, E.H.2


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