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Volumn 8, Issue 4, 2009, Pages 285-305

Biomarkers of oxidative and nitrosative damage in Alzheimer's disease and mild cognitive impairment

Author keywords

Alzheimer's disease; Free radicals; Mild cognitive impairment; Nitrosative stress; Oxidative stress

Indexed keywords

3 NITROTYROSINE; 4 HYDROXYNONENAL; ACROLEIN; AMINO ACID DERIVATIVE; BIOLOGICAL MARKER; CROTONALDEHYDE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; ISOPROSTANE DERIVATIVE; LIPID; MALONALDEHYDE; NEUROFURAN DERIVATIVE; NEUROPROSTANE DERIVATIVE; NITRATE; NITRIC OXIDE; NITRITE; NITROGEN DIOXIDE; NUCLEIC ACID; OXYGEN; PEROXY RADICAL; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 69049109744     PISSN: 15681637     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.arr.2009.04.002     Document Type: Short Survey
Times cited : (210)

References (350)
  • 1
    • 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. 3 (2002) 447-450
    • (2002) J. Neurosci. Res. , vol.3 , pp. 447-450
    • Abe, T.1    Tohgi, H.2    Isobe, C.3    Murata, T.4    Sato, C.5
  • 2
    • 0032734510 scopus 로고    scopus 로고
    • DNA strand breaks in Alzheimer's disease
    • Adamec E., Vonsattel J.P., and Nixon R.A. DNA strand breaks in Alzheimer's disease. Brain Res. 1-2 (1999) 67-77
    • (1999) Brain Res. , vol.1-2 , pp. 67-77
    • Adamec, E.1    Vonsattel, J.P.2    Nixon, R.A.3
  • 4
    • 13244270042 scopus 로고    scopus 로고
    • Protein glycation, oxidation and nitration adduct residues and free adducts of cerebrospinal fluid in Alzheimer's disease and link to cognitive impairment
    • Ahmed N., Ahmed U., Thornalley P.J., Hager K., Fleischer G., and Munch G. Protein glycation, oxidation and nitration adduct residues and free adducts of cerebrospinal fluid in Alzheimer's disease and link to cognitive impairment. J. Neurochem. 2 (2005) 255-263
    • (2005) J. Neurochem. , vol.2 , pp. 255-263
    • Ahmed, N.1    Ahmed, U.2    Thornalley, P.J.3    Hager, K.4    Fleischer, G.5    Munch, G.6
  • 6
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames B.N., Shigenaga M.K., and Hagen T.M. Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. U.S.A. 17 (1993) 7915-7922
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.17 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 7
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: cause or consequence?
    • Andersen J.K. Oxidative stress in neurodegeneration: cause or consequence?. Nat. Med. (2004) S18-S25
    • (2004) Nat. Med.
    • Andersen, J.K.1
  • 8
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • Anderson A.J., Su J.H., and Cotman C.W. DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J. Neurosci. 5 (1996) 1710-1719
    • (1996) J. Neurosci. , vol.5 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 10
    • 38449114957 scopus 로고    scopus 로고
    • Measurement of products of docosahexaenoic acid peroxidation, neuroprostanes, and neurofurans
    • Arneson K.O., and Roberts II L.J. Measurement of products of docosahexaenoic acid peroxidation, neuroprostanes, and neurofurans. Methods Enzymol. (2007) 127-143
    • (2007) Methods Enzymol. , pp. 127-143
    • Arneson, K.O.1    Roberts II, L.J.2
  • 11
    • 33750898439 scopus 로고    scopus 로고
    • Revised criteria for mild cognitive impairment: validation within a longitudinal population study
    • Artero S., Petersen R., Touchon J., and Ritchie K. Revised criteria for mild cognitive impairment: validation within a longitudinal population study. Dement. Geriatr. Cogn. Disord. 5-6 (2006) 465-470
    • (2006) Dement. Geriatr. Cogn. Disord. , vol.5-6 , pp. 465-470
    • Artero, S.1    Petersen, R.2    Touchon, J.3    Ritchie, K.4
  • 12
    • 33846226106 scopus 로고    scopus 로고
    • Determination of malondialdehyde, reduced glutathione levels and APOE4 allele frequency in late-onset Alzheimer's disease in Denizli, Turkey
    • Aybek H., Ercan F., Aslan D., and Sahiner T. Determination of malondialdehyde, reduced glutathione levels and APOE4 allele frequency in late-onset Alzheimer's disease in Denizli, Turkey. Clin. Biochem. 3-4 (2007) 172-176
    • (2007) Clin. Biochem. , vol.3-4 , pp. 172-176
    • Aybek, H.1    Ercan, F.2    Aslan, D.3    Sahiner, T.4
  • 13
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban R.S., Nemoto S., and Finkel T. Mitochondria, oxidants, and aging. Cell 4 (2005) 483-495
    • (2005) Cell , vol.4 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 14
    • 0028129137 scopus 로고
    • Evidence of an oxidative challenge in the Alzheimer's brain
    • Balazs L., and Leon M. Evidence of an oxidative challenge in the Alzheimer's brain. Neurochem. Res. 9 (1994) 1131-1137
    • (1994) Neurochem. Res. , vol.9 , pp. 1131-1137
    • Balazs, L.1    Leon, M.2
  • 16
    • 4544322045 scopus 로고    scopus 로고
    • Free radicals and aging
    • Barja G. Free radicals and aging. Trends Neurosci. 10 (2004) 595-600
    • (2004) Trends Neurosci. , vol.10 , pp. 595-600
    • Barja, G.1
  • 18
    • 27844525474 scopus 로고    scopus 로고
    • Accumulation of lipid peroxidation-derived DNA lesions: potential lead markers for chemoprevention of inflammation-driven malignancies
    • Bartsch H., and Nair J. Accumulation of lipid peroxidation-derived DNA lesions: potential lead markers for chemoprevention of inflammation-driven malignancies. Mutat. Res. 1-2 (2005) 34-44
    • (2005) Mutat. Res. , vol.1-2 , pp. 34-44
    • Bartsch, H.1    Nair, J.2
  • 19
    • 33846205620 scopus 로고    scopus 로고
    • The contribution of the DNA damage response to neuronal viability
    • Barzilai A. The contribution of the DNA damage response to neuronal viability. Antioxid. Redox Signal. 2 (2007) 211-218
    • (2007) Antioxid. Redox Signal. , vol.2 , pp. 211-218
    • Barzilai, A.1
  • 20
    • 0842302396 scopus 로고    scopus 로고
    • Isoprostanes: novel bioactive products of lipid peroxidation
    • Basu S. Isoprostanes: novel bioactive products of lipid peroxidation. Free Radic. Res. 2 (2004) 105-122
    • (2004) Free Radic. Res. , vol.2 , pp. 105-122
    • Basu, S.1
  • 22
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal M.F. Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 4 (2005) 495-505
    • (2005) Ann. Neurol. , vol.4 , pp. 495-505
    • Beal, M.F.1
  • 23
    • 1542381057 scopus 로고    scopus 로고
    • Cell cycle regulation of neuronal apoptosis in development and disease
    • Becker E.B., and Bonni A. Cell cycle regulation of neuronal apoptosis in development and disease. Prog. Neurobiol. 1 (2004) 1-25
    • (2004) Prog. Neurobiol. , vol.1 , pp. 1-25
    • Becker, E.B.1    Bonni, A.2
  • 24
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman K.B., and Ames B.N. The free radical theory of aging matures. Physiol. Rev. 2 (1998) 547-581
    • (1998) Physiol. Rev. , vol.2 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 25
    • 39749157595 scopus 로고    scopus 로고
    • Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer's disease from mild cognitive impairment
    • Bermejo P., Martin-Aragon S., Benedi J., Susin C., Felici E., Gil P., Ribera J.M., and Villar A.M. Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer's disease from mild cognitive impairment. Free Radic. Res. 2 (2008) 162-170
    • (2008) Free Radic. Res. , vol.2 , pp. 162-170
    • Bermejo, P.1    Martin-Aragon, S.2    Benedi, J.3    Susin, C.4    Felici, E.5    Gil, P.6    Ribera, J.M.7    Villar, A.M.8
  • 26
    • 0033774075 scopus 로고    scopus 로고
    • Cognitive decline is associated with systemic oxidative stress: the EVA study. Etude du Vieillissement Arteriel
    • Berr C., Balansard B., Arnaud J., Roussel A.M., and Alperovitch A. Cognitive decline is associated with systemic oxidative stress: the EVA study. Etude du Vieillissement Arteriel. J. Am. Geriatr. Soc. 10 (2000) 1285-1291
    • (2000) J. Am. Geriatr. Soc. , vol.10 , pp. 1285-1291
    • Berr, C.1    Balansard, B.2    Arnaud, J.3    Roussel, A.M.4    Alperovitch, A.5
  • 29
    • 24044475562 scopus 로고    scopus 로고
    • Hypothetical role of RNA damage avoidance in preventing human disease
    • Bregeon D., and Sarasin A. Hypothetical role of RNA damage avoidance in preventing human disease. Mutat. Res. 1-2 (2005) 293-302
    • (2005) Mutat. Res. , vol.1-2 , pp. 293-302
    • Bregeon, D.1    Sarasin, A.2
  • 30
    • 40149100476 scopus 로고    scopus 로고
    • Regulation of proteasome-mediated protein degradation during oxidative stress and aging
    • Breusing N., and Grune T. Regulation of proteasome-mediated protein degradation during oxidative stress and aging. Biol. Chem. 3 (2008) 203-209
    • (2008) Biol. Chem. , vol.3 , pp. 203-209
    • Breusing, N.1    Grune, T.2
  • 32
    • 1842505677 scopus 로고    scopus 로고
    • Proteomics: a new approach to investigate oxidative stress in Alzheimer's disease brain
    • Butterfield D.A. Proteomics: a new approach to investigate oxidative stress in Alzheimer's disease brain. Brain Res. 1-2 (2004) 1-7
    • (2004) Brain Res. , vol.1-2 , pp. 1-7
    • Butterfield, D.A.1
  • 33
    • 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 D.A., 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. 1 (2007) 61-72
    • (2007) J. Alzheimers Dis. , vol.1 , pp. 61-72
    • Butterfield, D.A.1    Sultana, R.2
  • 34
    • 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 D.A., Poon H.F., St Clair D., Keller J.N., Pierce W.M., Klein J.B., and Markesbery W.R. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol. Dis. 2 (2006) 223-232
    • (2006) Neurobiol. Dis. , vol.2 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, D.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6    Markesbery, W.R.7
  • 35
    • 33644987632 scopus 로고    scopus 로고
    • Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment
    • Butterfield D.A., Reed T., Perluigi M., De Marco C., Coccia R., Cini C., and Sultana R. Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment. Neurosci. Lett. 3 (2006) 170-173
    • (2006) Neurosci. Lett. , vol.3 , pp. 170-173
    • Butterfield, D.A.1    Reed, T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Cini, C.6    Sultana, R.7
  • 36
    • 34247142905 scopus 로고    scopus 로고
    • Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: implications for the role of nitration in the progression of Alzheimer's disease
    • Butterfield D.A., Reed T.T., Perluigi M., De Marco C., Coccia R., Keller J.N., Markesbery W.R., and Sultana R. Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: implications for the role of nitration in the progression of Alzheimer's disease. Brain Res. (2007) 243-248
    • (2007) Brain Res. , pp. 243-248
    • Butterfield, D.A.1    Reed, T.T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Keller, J.N.6    Markesbery, W.R.7    Sultana, R.8
  • 37
    • 0034864018 scopus 로고    scopus 로고
    • Mitochondrial involvement in brain function and dysfunction: relevance to aging, neurodegenerative disorders and longevity
    • Calabrese V., Scapagnini G., Giuffrida Stella A.M., Bates T.E., and Clark J.B. Mitochondrial involvement in brain function and dysfunction: relevance to aging, neurodegenerative disorders and longevity. Neurochem. Res. 6 (2001) 739-764
    • (2001) Neurochem. Res. , vol.6 , pp. 739-764
    • Calabrese, V.1    Scapagnini, G.2    Giuffrida Stella, A.M.3    Bates, T.E.4    Clark, J.B.5
  • 40
    • 0032905632 scopus 로고    scopus 로고
    • Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease
    • Calingasan N.Y., Uchida K., and Gibson G.E. Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease. J. Neurochem. 2 (1999) 751-756
    • (1999) J. Neurochem. , vol.2 , pp. 751-756
    • Calingasan, N.Y.1    Uchida, K.2    Gibson, G.E.3
  • 41
    • 38949205552 scopus 로고    scopus 로고
    • Delineating the mechanism of Alzheimer's disease A beta peptide neurotoxicity
    • Cappai R., and Barnham K.J. Delineating the mechanism of Alzheimer's disease A beta peptide neurotoxicity. Neurochem. Res. 3 (2008) 526-532
    • (2008) Neurochem. Res. , vol.3 , pp. 526-532
    • Cappai, R.1    Barnham, K.J.2
  • 42
    • 3042596594 scopus 로고    scopus 로고
    • Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins
    • Carini M., Aldini G., and Facino R.M. Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins. Mass Spectrom. Rev. 4 (2004) 281-305
    • (2004) Mass Spectrom. Rev. , vol.4 , pp. 281-305
    • Carini, M.1    Aldini, G.2    Facino, R.M.3
  • 45
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol. Med. 4 (2002) 562-571
    • (2002) Free Radic. Biol. Med. , vol.4 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 46
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II. Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A., Aksenov M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II. Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J. Neurochem. 6 (2002) 1524-1532
    • (2002) J. Neurochem. , vol.6 , 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
  • 49
    • 0029871412 scopus 로고    scopus 로고
    • Peripheral antioxidant enzyme activities and selenium in elderly subjects and in dementia of Alzheimer's type-place of the extracellular glutathione peroxidase
    • Ceballos-Picot I., Merad-Boudia M., Nicole A., Thevenin M., Hellier G., Legrain S., and Berr C. Peripheral antioxidant enzyme activities and selenium in elderly subjects and in dementia of Alzheimer's type-place of the extracellular glutathione peroxidase. Free Radic. Biol. Med. 4 (1996) 579-587
    • (1996) Free Radic. Biol. Med. , vol.4 , pp. 579-587
    • Ceballos-Picot, I.1    Merad-Boudia, M.2    Nicole, A.3    Thevenin, M.4    Hellier, G.5    Legrain, S.6    Berr, C.7
  • 50
    • 34249810042 scopus 로고    scopus 로고
    • Oxidative inactivation of the proteasome in Alzheimer's disease
    • Cecarini V., Ding Q., and Keller J.N. Oxidative inactivation of the proteasome in Alzheimer's disease. Free Radic. Res. 6 (2007) 673-680
    • (2007) Free Radic. Res. , vol.6 , pp. 673-680
    • Cecarini, V.1    Ding, Q.2    Keller, J.N.3
  • 52
    • 45049086702 scopus 로고    scopus 로고
    • Effects of oxidative and nitrosative stress in brain on p53 proapoptotic protein in amnestic mild cognitive impairment and Alzheimer disease
    • Cenini G., Sultana R., Memo M., and Butterfield D.A. Effects of oxidative and nitrosative stress in brain on p53 proapoptotic protein in amnestic mild cognitive impairment and Alzheimer disease. Free Radic. Biol. Med. 1 (2008) 81-85
    • (2008) Free Radic. Biol. Med. , vol.1 , pp. 81-85
    • Cenini, G.1    Sultana, R.2    Memo, M.3    Butterfield, D.A.4
  • 53
    • 44149095262 scopus 로고    scopus 로고
    • Elevated levels of pro-apoptotic p53 and its oxidative modification by the lipid peroxidation product, HNE, in brain from subjects with amnestic mild cognitive impairment and Alzheimer's disease
    • Cenini G., Sultana R., Memo M., and Butterfield D.A. Elevated levels of pro-apoptotic p53 and its oxidative modification by the lipid peroxidation product, HNE, in brain from subjects with amnestic mild cognitive impairment and Alzheimer's disease. J. Cell Mol. Med. 12 (2008) 987-994
    • (2008) J. Cell Mol. Med. , vol.12 , pp. 987-994
    • Cenini, G.1    Sultana, R.2    Memo, M.3    Butterfield, D.A.4
  • 54
    • 34247363723 scopus 로고    scopus 로고
    • Oxidative modification of proteins: age-related changes
    • Chakravarti B., and Chakravarti D.N. Oxidative modification of proteins: age-related changes. Gerontology 3 (2007) 128-139
    • (2007) Gerontology , vol.3 , pp. 128-139
    • Chakravarti, B.1    Chakravarti, D.N.2
  • 55
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 3 (1979) 527-605
    • (1979) Physiol. Rev. , vol.3 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 56
    • 34250898788 scopus 로고    scopus 로고
    • Effect of aldehydes derived from oxidative deamination and oxidative stress on beta-amyloid aggregation; pathological implications to Alzheimer's disease
    • Chen K., Kazachkov M., and Yu P.H. Effect of aldehydes derived from oxidative deamination and oxidative stress on beta-amyloid aggregation; pathological implications to Alzheimer's disease. J. Neural. Transm. 6 (2007) 835-839
    • (2007) J. Neural. Transm. , vol.6 , pp. 835-839
    • Chen, K.1    Kazachkov, M.2    Yu, P.H.3
  • 57
    • 51849150799 scopus 로고    scopus 로고
    • Lipid peroxidation up-regulates BACE1 expression in vivo: a possible early event of amyloidogenesis in Alzheimer's disease
    • Chen L., Na R., Gu M., Richardson A., and Ran Q. Lipid peroxidation up-regulates BACE1 expression in vivo: a possible early event of amyloidogenesis in Alzheimer's disease. J. Neurochem. 1 (2008) 197-207
    • (2008) J. Neurochem. , vol.1 , pp. 197-207
    • Chen, L.1    Na, R.2    Gu, M.3    Richardson, A.4    Ran, Q.5
  • 60
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J., Levey A.I., Weintraub S.T., Rees H.D., Gearing M., Chin L.S., and Li L. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 13 (2004) 13256-13264
    • (2004) J. Biol. Chem. , vol.13 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 62
    • 0000825475 scopus 로고
    • The absence of a pyrimidine dimer repair mechanism in mammalian mitochondria
    • Clayton D.A., Doda J.N., and Friedberg E.C. The absence of a pyrimidine dimer repair mechanism in mammalian mitochondria. Proc. Natl. Acad. Sci. U.S.A. 7 (1974) 2777-2781
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.7 , pp. 2777-2781
    • Clayton, D.A.1    Doda, J.N.2    Friedberg, E.C.3
  • 63
    • 0023642584 scopus 로고
    • Production of superoxide anions by a CNS macrophage, the microglia
    • Colton C.A., and Gilbert D.L. Production of superoxide anions by a CNS macrophage, the microglia. FEBS Lett. 2 (1987) 284-288
    • (1987) FEBS Lett. , vol.2 , pp. 284-288
    • Colton, C.A.1    Gilbert, D.L.2
  • 64
    • 0041846404 scopus 로고    scopus 로고
    • Quantitative assessment of DNA fragmentation and beta-amyloid deposition in insular cortex and midfrontal gyrus from patients with Alzheimer's disease
    • Colurso G.J., Nilson J.E., and Vervoort L.G. Quantitative assessment of DNA fragmentation and beta-amyloid deposition in insular cortex and midfrontal gyrus from patients with Alzheimer's disease. Life Sci. 14 (2003) 1795-1803
    • (2003) Life Sci. , vol.14 , pp. 1795-1803
    • Colurso, G.J.1    Nilson, J.E.2    Vervoort, L.G.3
  • 66
    • 0036697124 scopus 로고    scopus 로고
    • Isoprostanes as a biomarker of lipid peroxidation in humans: physiology, pharmacology and clinical implications
    • Cracowski J.L., Durand T., and Bessard G. Isoprostanes as a biomarker of lipid peroxidation in humans: physiology, pharmacology and clinical implications. Trends Pharmacol. Sci. 8 (2002) 360-366
    • (2002) Trends Pharmacol. Sci. , vol.8 , pp. 360-366
    • Cracowski, J.L.1    Durand, T.2    Bessard, G.3
  • 68
    • 34447634140 scopus 로고    scopus 로고
    • The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer's disease
    • Crouch P.J., White A.R., and Bush A.I. The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer's disease. FEBS J. 15 (2007) 3775-3783
    • (2007) FEBS J. , vol.15 , pp. 3775-3783
    • Crouch, P.J.1    White, A.R.2    Bush, A.I.3
  • 69
    • 0029073807 scopus 로고
    • The role of peroxynitrite in nitric oxide-mediated toxicity
    • Crow J.P., and Beckman J.S. The role of peroxynitrite in nitric oxide-mediated toxicity. Curr. Top. Microbiol. Immunol. (1995) 57-73
    • (1995) Curr. Top. Microbiol. Immunol. , pp. 57-73
    • Crow, J.P.1    Beckman, J.S.2
  • 70
    • 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 C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S., Beyreuther K., Barrow C.J., Masters C.L., Bush A.I., and Barnham K.J. 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. 23 (2001) 20466-20473
    • (2001) J. Biol. Chem. , vol.23 , 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
  • 76
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A., Mina E., Glabe C., and Busciglio J. Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 22 (2006) 6011-6018
    • (2006) J. Neurosci. , vol.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 77
    • 62349084020 scopus 로고    scopus 로고
    • Glutathionylation of the Pro-apoptotic Protein p53 in Alzheimer's Disease Brain: Implications for AD Pathogenesis
    • Di Domenico F., Cenini G., Sultana R., Perluigi M., Uberti D., Memo M., and Butterfield A.D. Glutathionylation of the Pro-apoptotic Protein p53 in Alzheimer's Disease Brain: Implications for AD Pathogenesis. Neurochem. Res. 4 (2009) 727-733
    • (2009) Neurochem. Res. , vol.4 , pp. 727-733
    • Di Domenico, F.1    Cenini, G.2    Sultana, R.3    Perluigi, M.4    Uberti, D.5    Memo, M.6    Butterfield, A.D.7
  • 78
    • 0035451913 scopus 로고    scopus 로고
    • Proteasomes and proteasome inhibition in the central nervous system
    • Ding Q., and Keller J.N. Proteasomes and proteasome inhibition in the central nervous system. Free Radic. Biol. Med. 5 (2001) 574-584
    • (2001) Free Radic. Biol. Med. , vol.5 , pp. 574-584
    • Ding, Q.1    Keller, J.N.2
  • 79
    • 27144494994 scopus 로고    scopus 로고
    • Ribosome dysfunction is an early event in Alzheimer's disease
    • Ding Q., Markesbery W.R., Chen Q., Li F., and Keller J.N. Ribosome dysfunction is an early event in Alzheimer's disease. J. Neurosci. 40 (2005) 9171-9175
    • (2005) J. Neurosci. , vol.40 , pp. 9171-9175
    • Ding, Q.1    Markesbery, W.R.2    Chen, Q.3    Li, F.4    Keller, J.N.5
  • 80
    • 33745096512 scopus 로고    scopus 로고
    • Decreased RNA, and increased RNA oxidation, in ribosomes from early Alzheimer's disease
    • Ding Q., Markesbery W.R., Cecarini V., and Keller J.N. Decreased RNA, and increased RNA oxidation, in ribosomes from early Alzheimer's disease. Neurochem. Res. 5 (2006) 705-710
    • (2006) Neurochem. Res. , vol.5 , pp. 705-710
    • Ding, Q.1    Markesbery, W.R.2    Cecarini, V.3    Keller, J.N.4
  • 81
    • 33847192092 scopus 로고    scopus 로고
    • Oxidative damage, protein synthesis, and protein degradation in Alzheimer's disease
    • Ding Q., Dimayuga E., and Keller J.N. Oxidative damage, protein synthesis, and protein degradation in Alzheimer's disease. Curr. Alzheimer Res. 1 (2007) 73-79
    • (2007) Curr. Alzheimer Res. , vol.1 , pp. 73-79
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 82
    • 34548528955 scopus 로고    scopus 로고
    • Oxidative status and prevalent cardiovascular disease in patients with chronic renal failure treated by hemodialysis
    • Dirican M., Sarandol E., Serdar Z., Ocak N., and Dilek K. Oxidative status and prevalent cardiovascular disease in patients with chronic renal failure treated by hemodialysis. Clin. Nephrol. 3 (2007) 144-150
    • (2007) Clin. Nephrol. , vol.3 , pp. 144-150
    • Dirican, M.1    Sarandol, E.2    Serdar, Z.3    Ocak, N.4    Dilek, K.5
  • 84
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 1 (2002) 47-95
    • (2002) Physiol. Rev. , vol.1 , pp. 47-95
    • Droge, W.1
  • 85
    • 45349112521 scopus 로고
    • O6-methylguanine-DNA methyltransferase in lymphocytes of the elderly with and without Alzheimer's disease
    • Edwards J.A., Wang L.G., Setlow R.B., and Kaminskas E. O6-methylguanine-DNA methyltransferase in lymphocytes of the elderly with and without Alzheimer's disease. Mutat. Res. 5-6 (1989) 267-272
    • (1989) Mutat. Res. , vol.5-6 , pp. 267-272
    • Edwards, J.A.1    Wang, L.G.2    Setlow, R.B.3    Kaminskas, E.4
  • 88
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 1 (1991) 81-128
    • (1991) Free Radic. Biol. Med. , vol.1 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 91
    • 0024455022 scopus 로고
    • Oxidative DNA and RNA damage in the livers of Sprague-Dawley rats treated with the hepatocarcinogen 2-nitropropane
    • Fiala E.S., Conaway C.C., and Mathis J.E. Oxidative DNA and RNA damage in the livers of Sprague-Dawley rats treated with the hepatocarcinogen 2-nitropropane. Cancer Res 20 (1989) 5518-5522
    • (1989) Cancer Res , vol.20 , pp. 5518-5522
    • Fiala, E.S.1    Conaway, C.C.2    Mathis, J.E.3
  • 93
    • 33845518305 scopus 로고    scopus 로고
    • DNA repair in neurons: so if they don't divide what's to repair?
    • Fishel M.L., Vasko M.R., and Kelley M.R. DNA repair in neurons: so if they don't divide what's to repair?. Mutat. Res. 1-2 (2007) 24-36
    • (2007) Mutat. Res. , vol.1-2 , pp. 24-36
    • Fishel, M.L.1    Vasko, M.R.2    Kelley, M.R.3
  • 95
    • 0037411512 scopus 로고    scopus 로고
    • Biological markers for therapeutic trials in Alzheimer's disease. Proceedings of the biological markers working group; NIA initiative on neuroimaging in Alzheimer's disease
    • Frank R.A., Galasko D., Hampel H., Hardy J., de Leon M.J., Mehta P.D., Rogers J., Siemers E., and Trojanowski J.Q. Biological markers for therapeutic trials in Alzheimer's disease. Proceedings of the biological markers working group; NIA initiative on neuroimaging in Alzheimer's disease. Neurobiol. Aging 4 (2003) 521-536
    • (2003) Neurobiol. Aging , vol.4 , pp. 521-536
    • Frank, R.A.1    Galasko, D.2    Hampel, H.3    Hardy, J.4    de Leon, M.J.5    Mehta, P.D.6    Rogers, J.7    Siemers, E.8    Trojanowski, J.Q.9
  • 96
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein
    • Friguet B., and Szweda L.I. Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett. 1 (1997) 21-25
    • (1997) FEBS Lett. , vol.1 , pp. 21-25
    • Friguet, B.1    Szweda, L.I.2
  • 97
    • 0031754202 scopus 로고    scopus 로고
    • Increased nuclear DNA oxidation in the brain in Alzheimer's disease
    • Gabbita S.P., Lovell M.A., and Markesbery W.R. Increased nuclear DNA oxidation in the brain in Alzheimer's disease. J. Neurochem. 5 (1998) 2034-2040
    • (1998) J. Neurochem. , vol.5 , pp. 2034-2040
    • Gabbita, S.P.1    Lovell, M.A.2    Markesbery, W.R.3
  • 98
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita S.P., Aksenov M.Y., Lovell M.A., and Markesbery W.R. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J. Neurochem. 4 (1999) 1660-1666
    • (1999) J. Neurochem. , vol.4 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 99
    • 0030000652 scopus 로고    scopus 로고
    • Cognitive impairment and mortality in a cohort of elderly people
    • Gale C.R., Martyn C.N., and Cooper C. Cognitive impairment and mortality in a cohort of elderly people. BMJ 7031 (1996) 608-611
    • (1996) BMJ , vol.7031 , pp. 608-611
    • Gale, C.R.1    Martyn, C.N.2    Cooper, C.3
  • 100
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • Glabe C.G. Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol. Aging 4 (2006) 570-575
    • (2006) Neurobiol. Aging , vol.4 , pp. 570-575
    • Glabe, C.G.1
  • 101
    • 4644240857 scopus 로고    scopus 로고
    • Reduced concentrations of several vitamins in normal weight patients with late-onset dementia of the Alzheimer type without vascular disease
    • Glaso M., Nordbo G., Diep L., and Bohmer T. Reduced concentrations of several vitamins in normal weight patients with late-onset dementia of the Alzheimer type without vascular disease. J. Nutr. Health Aging 5 (2004) 407-413
    • (2004) J. Nutr. Health Aging , vol.5 , pp. 407-413
    • Glaso, M.1    Nordbo, G.2    Diep, L.3    Bohmer, T.4
  • 102
    • 0345701340 scopus 로고    scopus 로고
    • Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells
    • Gomez-Ramos A., Diaz-Nido J., Smith M.A., Perry G., and Avila J. Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells. J. Neurosci Res. 6 (2003) 863-870
    • (2003) J. Neurosci Res. , vol.6 , pp. 863-870
    • Gomez-Ramos, A.1    Diaz-Nido, J.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 103
    • 0027478197 scopus 로고
    • The thiobarbituric acid assay reflects susceptibility to oxygen induced lipid peroxidation in vitro rather than levels of lipid hydroperoxides in vivo: a methodological approach
    • Gotz M.E., Dirr A., Freyberger A., Burger R., and Riederer P. The thiobarbituric acid assay reflects susceptibility to oxygen induced lipid peroxidation in vitro rather than levels of lipid hydroperoxides in vivo: a methodological approach. Neurochem. Int. 3 (1993) 255-262
    • (1993) Neurochem. Int. , vol.3 , pp. 255-262
    • Gotz, M.E.1    Dirr, A.2    Freyberger, A.3    Burger, R.4    Riederer, P.5
  • 104
    • 0032033832 scopus 로고    scopus 로고
    • Consensus report of the working group on: "Molecular and biochemical markers of alzheimer's disease". The Ronald and Nancy Reagan Research Institute of the Alzheimer's Association and the National Institute on Aging Working Group
    • Growdon J. Consensus report of the working group on: "Molecular and biochemical markers of alzheimer's disease". The Ronald and Nancy Reagan Research Institute of the Alzheimer's Association and the National Institute on Aging Working Group. Neurobiol Aging 2 (1998) 109-116
    • (1998) Neurobiol Aging , vol.2 , pp. 109-116
    • Growdon, J.1
  • 105
    • 0020018148 scopus 로고
    • Free-radical damage to lipids, amino acids, carbohydrates and nucleic acids determined by thiobarbituric acid reactivity
    • Gutteridge J.M. Free-radical damage to lipids, amino acids, carbohydrates and nucleic acids determined by thiobarbituric acid reactivity. Int. J. Biochem. 7 (1982) 649-653
    • (1982) Int. J. Biochem. , vol.7 , pp. 649-653
    • Gutteridge, J.M.1
  • 106
    • 0025369970 scopus 로고
    • The measurement and mechanism of lipid peroxidation in biological systems
    • Gutteridge J.M., and Halliwell B. The measurement and mechanism of lipid peroxidation in biological systems. Trends Biochem. Sci. 4 (1990) 129-135
    • (1990) Trends Biochem. Sci. , vol.4 , pp. 129-135
    • Gutteridge, J.M.1    Halliwell, B.2
  • 107
    • 0025699758 scopus 로고
    • Brain membrane fluidity and lipid peroxidation in Alzheimer's disease
    • Hajimohammadreza I., and Brammer M. Brain membrane fluidity and lipid peroxidation in Alzheimer's disease. Neurosci. Lett. 2-3 (1990) 333-337
    • (1990) Neurosci. Lett. , vol.2-3 , pp. 333-337
    • Hajimohammadreza, I.1    Brammer, M.2
  • 109
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?
    • Halliwell B., and Whiteman M. Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?. Br. J. Pharmacol. 2 (2004) 231-255
    • (2004) Br. J. Pharmacol. , vol.2 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 110
    • 0345104375 scopus 로고    scopus 로고
    • Evidence against the involvement of reactive oxygen species in the pathogenesis of neuronal death in Down's syndrome and Alzheimer's disease
    • Hayn M., Kremser K., Singewald N., Cairns N., Nemethova M., Lubec B., and Lubec G. Evidence against the involvement of reactive oxygen species in the pathogenesis of neuronal death in Down's syndrome and Alzheimer's disease. Life Sci. 7 (1996) 537-544
    • (1996) Life Sci. , vol.7 , pp. 537-544
    • Hayn, M.1    Kremser, K.2    Singewald, N.3    Cairns, N.4    Nemethova, M.5    Lubec, B.6    Lubec, G.7
  • 111
    • 0042023711 scopus 로고    scopus 로고
    • Alzheimer disease in the US population: prevalence estimates using the 2000 census
    • Hebert L.E., Scherr P.A., Bienias J.L., Bennett D.A., and Evans D.A. Alzheimer disease in the US population: prevalence estimates using the 2000 census. Arch. Neurol. 8 (2003) 1119-1122
    • (2003) Arch. Neurol. , vol.8 , pp. 1119-1122
    • Hebert, L.E.1    Scherr, P.A.2    Bienias, J.L.3    Bennett, D.A.4    Evans, D.A.5
  • 115
    • 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., and Floyd R.A. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 20 (1998) 8126-8132
    • (1998) J. Neurosci. , vol.20 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 117
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease
    • Hou L., Kang I., Marchant R.E., and Zagorski M.G. Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease. J. Biol. Chem. 43 (2002) 40173-40176
    • (2002) J. Biol. Chem. , vol.43 , pp. 40173-40176
    • Hou, L.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 118
    • 0035968331 scopus 로고    scopus 로고
    • Endogenous formation of protein adducts with carcinogenic aldehydes: implications for oxidative stress
    • Ichihashi K., Osawa T., Toyokuni S., and Uchida K. Endogenous formation of protein adducts with carcinogenic aldehydes: implications for oxidative stress. J. Biol. Chem. 26 (2001) 23903-23913
    • (2001) J. Biol. Chem. , vol.26 , pp. 23903-23913
    • Ichihashi, K.1    Osawa, T.2    Toyokuni, S.3    Uchida, K.4
  • 120
    • 0036942993 scopus 로고    scopus 로고
    • Expression of 8-oxoguanine DNA glycosylase is reduced and associated with neurofibrillary tangles in Alzheimer's disease brain
    • Iida T., Furuta A., Nishioka K., Nakabeppu Y., and Iwaki T. Expression of 8-oxoguanine DNA glycosylase is reduced and associated with neurofibrillary tangles in Alzheimer's disease brain. Acta Neuropathol. 1 (2002) 20-25
    • (2002) Acta Neuropathol. , vol.1 , pp. 20-25
    • Iida, T.1    Furuta, A.2    Nishioka, K.3    Nakabeppu, Y.4    Iwaki, T.5
  • 121
    • 0037948843 scopus 로고    scopus 로고
    • Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins
    • Irie Y., Saeki M., Kamisaki Y., Martin E., and Murad F. Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins. Proc. Natl. Acad. Sci. U.S.A. 10 (2003) 5634-5639
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.10 , pp. 5634-5639
    • Irie, Y.1    Saeki, M.2    Kamisaki, Y.3    Martin, E.4    Murad, F.5
  • 123
  • 124
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • Jones D.P. Redefining oxidative stress. Antioxid. Redox Signal. 9-10 (2006) 1865-1879
    • (2006) Antioxid. Redox Signal. , vol.9-10 , pp. 1865-1879
    • Jones, D.P.1
  • 127
    • 4544225426 scopus 로고    scopus 로고
    • Detection of oxidative DNA damage in lymphocytes of patients with Alzheimer's disease
    • Kadioglu E., Sardas S., Aslan S., Isik E., and Esat Karakaya A. Detection of oxidative DNA damage in lymphocytes of patients with Alzheimer's disease. Biomarkers 2 (2004) 203-209
    • (2004) Biomarkers , vol.2 , pp. 203-209
    • Kadioglu, E.1    Sardas, S.2    Aslan, S.3    Isik, E.4    Esat Karakaya, A.5
  • 130
    • 0345601861 scopus 로고    scopus 로고
    • Can we prevent Parkinson's and Alzheimer's disease?
    • Kedar N.P. Can we prevent Parkinson's and Alzheimer's disease?. J. Postgrad. Med. 3 (2003) 236-245
    • (2003) J. Postgrad. Med. , vol.3 , pp. 236-245
    • Kedar, N.P.1
  • 131
    • 0031840571 scopus 로고    scopus 로고
    • Roles of lipid peroxidation in modulation of cellular signaling pathways, cell dysfunction, and death in the nervous system
    • Keller J.N., and Mattson M.P. Roles of lipid peroxidation in modulation of cellular signaling pathways, cell dysfunction, and death in the nervous system. Rev. Neurosci. 2 (1998) 105-116
    • (1998) Rev. Neurosci. , vol.2 , pp. 105-116
    • Keller, J.N.1    Mattson, M.P.2
  • 132
    • 0030754962 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, an aldehydic product of membrane lipid peroxidation, impairs glutamate transport and mitochondrial function in synaptosomes
    • Keller J.N., Mark R.J., Bruce A.J., Blanc E., Rothstein J.D., Uchida K., Waeg G., and Mattson M.P. 4-Hydroxynonenal, an aldehydic product of membrane lipid peroxidation, impairs glutamate transport and mitochondrial function in synaptosomes. Neuroscience 3 (1997) 685-696
    • (1997) Neuroscience , vol.3 , pp. 685-696
    • Keller, J.N.1    Mark, R.J.2    Bruce, A.J.3    Blanc, E.4    Rothstein, J.D.5    Uchida, K.6    Waeg, G.7    Mattson, M.P.8
  • 134
    • 3242690571 scopus 로고    scopus 로고
    • Increased urinary F(2)-isoprostanes levels in the patients with Alzheimer's disease
    • Kim K.M., Jung B.H., Paeng K.J., Kim I., and Chung B.C. Increased urinary F(2)-isoprostanes levels in the patients with Alzheimer's disease. Brain Res. Bull. 1 (2004) 47-51
    • (2004) Brain Res. Bull. , vol.1 , pp. 47-51
    • Kim, K.M.1    Jung, B.H.2    Paeng, K.J.3    Kim, I.4    Chung, B.C.5
  • 135
    • 0023573904 scopus 로고
    • Alzheimer's disease fibroblasts have normal repair of N-methyl-N′-nitro-N-nitrosoguanidine-induced DNA damage determined by the alkaline elution technique
    • Kinsella T.J., Dobson P.P., Fornace Jr. A.J., Barrett S.F., Ganges M.B., and Robbins J.H. Alzheimer's disease fibroblasts have normal repair of N-methyl-N′-nitro-N-nitrosoguanidine-induced DNA damage determined by the alkaline elution technique. Biochem. Biophys. Res. Commun. 2 (1987) 355-361
    • (1987) Biochem. Biophys. Res. Commun. , vol.2 , pp. 355-361
    • Kinsella, T.J.1    Dobson, P.P.2    Fornace Jr., A.J.3    Barrett, S.F.4    Ganges, M.B.5    Robbins, J.H.6
  • 136
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?
    • Klein W.L., Krafft G.A., and Finch C.E. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?. Trends Neurosci. 4 (2001) 219-224
    • (2001) Trends Neurosci. , vol.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 138
    • 34548549194 scopus 로고    scopus 로고
    • Advanced oxidation protein products, ferrous oxidation in xylenol orange, and malondialdehyde levels in thyroid cancer
    • Kosova F., Cetin B., Akinci M., Aslan S., Ari Z., Sepici A., Altan N., and Cetin A. Advanced oxidation protein products, ferrous oxidation in xylenol orange, and malondialdehyde levels in thyroid cancer. Ann. Surg. Oncol. 9 (2007) 2616-2620
    • (2007) Ann. Surg. Oncol. , vol.9 , pp. 2616-2620
    • Kosova, F.1    Cetin, B.2    Akinci, M.3    Aslan, S.4    Ari, Z.5    Sepici, A.6    Altan, N.7    Cetin, A.8
  • 140
    • 13244249527 scopus 로고    scopus 로고
    • Why do neurons enter the cell cycle?
    • Kruman I.I. Why do neurons enter the cell cycle?. Cell Cycle 6 (2004) 769-773
    • (2004) Cell Cycle , vol.6 , pp. 769-773
    • Kruman, I.I.1
  • 141
    • 34147135482 scopus 로고    scopus 로고
    • Effect of pseudophosphorylation and cross-linking by lipid peroxidation and advanced glycation end product precursors on tau aggregation and filament formation
    • Kuhla B., Haase C., Flach K., Luth H.J., Arendt T., and Munch G. Effect of pseudophosphorylation and cross-linking by lipid peroxidation and advanced glycation end product precursors on tau aggregation and filament formation. J. Biol. Chem. 10 (2007) 6984-6991
    • (2007) J. Biol. Chem. , vol.10 , pp. 6984-6991
    • Kuhla, B.1    Haase, C.2    Flach, K.3    Luth, H.J.4    Arendt, T.5    Munch, G.6
  • 143
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere M.C., Sturley S.L., and Raines R.T. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 47 (1995) 28006-28009
    • (1995) J. Biol. Chem. , vol.47 , pp. 28006-28009
    • Laboissiere, M.C.1    Sturley, S.L.2    Raines, R.T.3
  • 145
    • 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 Abeta1-42
    • Lauderback C.M., Hackett J.M., Huang F.F., Keller J.N., Szweda L.I., Markesbery W.R., and Butterfield D.A. The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Abeta1-42. J. Neurochem. 2 (2001) 413-416
    • (2001) J. Neurochem. , vol.2 , 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
  • 146
    • 2342608923 scopus 로고    scopus 로고
    • Midlife dietary intake of antioxidants and risk of late-life incident dementia: the Honolulu-Asia Aging Study
    • Laurin D., Masaki K.H., Foley D.J., White L.R., and Launer L.J. Midlife dietary intake of antioxidants and risk of late-life incident dementia: the Honolulu-Asia Aging Study. Am. J. Epidemiol. 10 (2004) 959-967
    • (2004) Am. J. Epidemiol. , vol.10 , pp. 959-967
    • Laurin, D.1    Masaki, K.H.2    Foley, D.J.3    White, L.R.4    Launer, L.J.5
  • 147
    • 34247127167 scopus 로고    scopus 로고
    • Mitochondrial DNA repair: a critical player in the response of cells of the CNS to genotoxic insults
    • LeDoux S.P., Druzhyna N.M., Hollensworth S.B., Harrison J.F., and Wilson G.L. Mitochondrial DNA repair: a critical player in the response of cells of the CNS to genotoxic insults. Neuroscience 4 (2007) 1249-1259
    • (2007) Neuroscience , vol.4 , pp. 1249-1259
    • LeDoux, S.P.1    Druzhyna, N.M.2    Hollensworth, S.B.3    Harrison, J.F.4    Wilson, G.L.5
  • 148
    • 3242737470 scopus 로고    scopus 로고
    • Challenging the amyloid cascade hypothesis: senile plaques and amyloid-beta as protective adaptations to Alzheimer disease
    • Lee H.G., Casadesus G., Zhu X., Takeda A., Perry G., and Smith M.A. Challenging the amyloid cascade hypothesis: senile plaques and amyloid-beta as protective adaptations to Alzheimer disease. Ann. N. Y. Acad. Sci. (2004) 1-4
    • (2004) Ann. N. Y. Acad. Sci. , pp. 1-4
    • Lee, H.G.1    Casadesus, G.2    Zhu, X.3    Takeda, A.4    Perry, G.5    Smith, M.A.6
  • 149
    • 34548162663 scopus 로고    scopus 로고
    • Increased urinary level of oxidized nucleosides in patients with mild-to-moderate Alzheimer's disease
    • Lee S.H., Kim I., and Chung B.C. Increased urinary level of oxidized nucleosides in patients with mild-to-moderate Alzheimer's disease. Clin. Biochem. 13-14 (2007) 936-938
    • (2007) Clin. Biochem. , vol.13-14 , pp. 936-938
    • Lee, S.H.1    Kim, I.2    Chung, B.C.3
  • 150
    • 0025776627 scopus 로고
    • Preparative steps necessary for the accurate measurement of malondialdehyde by high-performance liquid chromatography
    • Lepage G., Munoz G., Champagne J., and Roy C.C. Preparative steps necessary for the accurate measurement of malondialdehyde by high-performance liquid chromatography. Anal. Biochem. 2 (1991) 277-283
    • (1991) Anal. Biochem. , vol.2 , pp. 277-283
    • Lepage, G.1    Munoz, G.2    Champagne, J.3    Roy, C.C.4
  • 151
    • 0031110054 scopus 로고    scopus 로고
    • Terminal dUTP nick end labeling (TUNEL) positive cells in the different regions of the brain in normal aging and Alzheimer patients
    • Li W.P., Chan W.Y., Lai H.W., and Yew D.T. Terminal dUTP nick end labeling (TUNEL) positive cells in the different regions of the brain in normal aging and Alzheimer patients. J. Mol. Neurosci. 2 (1997) 75-82
    • (1997) J. Mol. Neurosci. , vol.2 , pp. 75-82
    • Li, W.P.1    Chan, W.Y.2    Lai, H.W.3    Yew, D.T.4
  • 153
    • 0024541837 scopus 로고
    • Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases
    • Linnane A.W., Marzuki S., Ozawa T., and Tanaka M. Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases. Lancet 8639 (1989) 642-645
    • (1989) Lancet , vol.8639 , pp. 642-645
    • Linnane, A.W.1    Marzuki, S.2    Ozawa, T.3    Tanaka, M.4
  • 154
    • 24944565214 scopus 로고    scopus 로고
    • Development of a method for quantification of acrolein-deoxyguanosine adducts in DNA using isotope dilution-capillary LC/MS/MS and its application to human brain tissue
    • Liu X., Lovell M.A., and Lynn B.C. Development of a method for quantification of acrolein-deoxyguanosine adducts in DNA using isotope dilution-capillary LC/MS/MS and its application to human brain tissue. Anal. Chem. 18 (2005) 5982-5989
    • (2005) Anal. Chem. , vol.18 , pp. 5982-5989
    • Liu, X.1    Lovell, M.A.2    Lynn, B.C.3
  • 155
    • 33744460225 scopus 로고    scopus 로고
    • Detection and quantification of endogenous cyclic DNA adducts derived from trans-4-hydroxy-2-nonenal in human brain tissue by isotope dilution capillary liquid chromatography nanoelectrospray tandem mass spectrometry
    • Liu X., Lovell M.A., and Lynn B.C. Detection and quantification of endogenous cyclic DNA adducts derived from trans-4-hydroxy-2-nonenal in human brain tissue by isotope dilution capillary liquid chromatography nanoelectrospray tandem mass spectrometry. Chem. Res. Toxicol. 5 (2006) 710-718
    • (2006) Chem. Res. Toxicol. , vol.5 , pp. 710-718
    • Liu, X.1    Lovell, M.A.2    Lynn, B.C.3
  • 156
    • 0028175960 scopus 로고
    • Generation of alpha-hydroxyaldehydic compounds in the course of lipid peroxidation
    • Loidl-Stahlhofen A., Hannemann K., and Spiteller G. Generation of alpha-hydroxyaldehydic compounds in the course of lipid peroxidation. Biochim. Biophys. Acta 2 (1994) 140-148
    • (1994) Biochim. Biophys. Acta , vol.2 , pp. 140-148
    • Loidl-Stahlhofen, A.1    Hannemann, K.2    Spiteller, G.3
  • 157
    • 62349129124 scopus 로고    scopus 로고
    • Neuronal mitochondrial toxicity of malondialdehyde: inhibitory effects on respiratory function and enzyme activities in rat brain mitochondria
    • Long J., Liu C., Sun L., Gao H., and Liu J. Neuronal mitochondrial toxicity of malondialdehyde: inhibitory effects on respiratory function and enzyme activities in rat brain mitochondria. Neurochem. Res. 4 (2008) 786-794
    • (2008) Neurochem. Res. , vol.4 , pp. 786-794
    • Long, J.1    Liu, C.2    Sun, L.3    Gao, H.4    Liu, J.5
  • 158
    • 42149161725 scopus 로고    scopus 로고
    • Molecular mechanisms of the conjugated alpha,beta-unsaturated carbonyl derivatives: relevance to neurotoxicity and neurodegenerative diseases
    • LoPachin R.M., Barber D.S., and Gavin T. Molecular mechanisms of the conjugated alpha,beta-unsaturated carbonyl derivatives: relevance to neurotoxicity and neurodegenerative diseases. Toxicol. Sci. 2 (2008) 235-249
    • (2008) Toxicol. Sci. , vol.2 , pp. 235-249
    • LoPachin, R.M.1    Barber, D.S.2    Gavin, T.3
  • 159
    • 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., and Markesbery W.R. Ratio of 8-hydroxyguanine in intact DNA to free 8-hydroxyguanine is increased in Alzheimer disease ventricular cerebrospinal fluid. Arch. Neurol. 3 (2001) 392-396
    • (2001) Arch. Neurol. , vol.3 , pp. 392-396
    • Lovell, M.A.1    Markesbery, W.R.2
  • 160
    • 38049010515 scopus 로고    scopus 로고
    • Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease
    • Lovell M.A., and Markesbery W.R. Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease. Nucleic Acids Res. 22 (2007) 7497-7504
    • (2007) Nucleic Acids Res. , vol.22 , pp. 7497-7504
    • Lovell, M.A.1    Markesbery, W.R.2
  • 161
    • 38149087424 scopus 로고    scopus 로고
    • Oxidatively modified RNA in mild cognitive impairment
    • Lovell M.A., and Markesbery W.R. Oxidatively modified RNA in mild cognitive impairment. Neurobiol. Dis. 2 (2008) 169-175
    • (2008) Neurobiol. Dis. , vol.2 , pp. 169-175
    • Lovell, M.A.1    Markesbery, W.R.2
  • 162
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • Lovell M.A., Ehmann W.D., Butler S.M., and Markesbery W.R. Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease. Neurology 8 (1995) 1594-1601
    • (1995) Neurology , vol.8 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 163
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease
    • Lovell M.A., Ehmann W.D., Mattson M.P., and Markesbery W.R. Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease. Neurobiol. Aging 5 (1997) 457-461
    • (1997) Neurobiol. Aging , vol.5 , pp. 457-461
    • Lovell, M.A.1    Ehmann, W.D.2    Mattson, M.P.3    Markesbery, W.R.4
  • 165
    • 0032933750 scopus 로고    scopus 로고
    • Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF
    • Lovell M.A., Gabbita S.P., and Markesbery W.R. Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF. J. Neurochem. 2 (1999) 771-776
    • (1999) J. Neurochem. , vol.2 , pp. 771-776
    • Lovell, M.A.1    Gabbita, S.P.2    Markesbery, W.R.3
  • 166
    • 0034667741 scopus 로고    scopus 로고
    • Acrolein, a product of lipid peroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures
    • Lovell M.A., Xie C., and Markesbery W.R. Acrolein, a product of lipid peroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures. Free Radic. Biol. Med. 8 (2000) 714-720
    • (2000) Free Radic. Biol. Med. , vol.8 , pp. 714-720
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 167
    • 0033984570 scopus 로고    scopus 로고
    • Decreased base excision repair and increased helicase activity in Alzheimer's disease brain
    • Lovell M.A., Xie C., and Markesbery W.R. Decreased base excision repair and increased helicase activity in Alzheimer's disease brain. Brain Res. 1 (2000) 116-123
    • (2000) Brain Res. , vol.1 , pp. 116-123
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 168
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • Lovell M.A., Xie C., and Markesbery W.R. Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures. Neurobiol. Aging 2 (2001) 187-194
    • (2001) Neurobiol. Aging , vol.2 , pp. 187-194
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 169
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • Lu T., Pan Y., Kao S.Y., Li C., Kohane I., Chan J., and Yankner B.A. Gene regulation and DNA damage in the ageing human brain. Nature 6994 (2004) 883-891
    • (2004) Nature , vol.6994 , pp. 883-891
    • Lu, T.1    Pan, Y.2    Kao, S.Y.3    Li, C.4    Kohane, I.5    Chan, J.6    Yankner, B.A.7
  • 170
    • 0030806869 scopus 로고    scopus 로고
    • DNA damage distribution in the human brain as shown by in situ end labeling; area-specific differences in aging and Alzheimer disease in the absence of apoptotic morphology
    • Lucassen P.J., Chung W.C., Kamphorst W., and Swaab D.F. DNA damage distribution in the human brain as shown by in situ end labeling; area-specific differences in aging and Alzheimer disease in the absence of apoptotic morphology. J. Neuropathol. Exp. Neurol. 8 (1997) 887-900
    • (1997) J. Neuropathol. Exp. Neurol. , vol.8 , pp. 887-900
    • Lucassen, P.J.1    Chung, W.C.2    Kamphorst, W.3    Swaab, D.F.4
  • 171
    • 0037320324 scopus 로고    scopus 로고
    • Antioxidant vitamin intake and risk of Alzheimer disease
    • Luchsinger J.A., Tang M.X., Shea S., and Mayeux R. Antioxidant vitamin intake and risk of Alzheimer disease. Arch. Neurol. 2 (2003) 203-208
    • (2003) Arch. Neurol. , vol.2 , pp. 203-208
    • Luchsinger, J.A.1    Tang, M.X.2    Shea, S.3    Mayeux, R.4
  • 172
    • 0038266652 scopus 로고    scopus 로고
    • DNA damage caused by lipid peroxidation products
    • Luczaj W., and Skrzydlewska E. DNA damage caused by lipid peroxidation products. Cell Mol. Biol. Lett. 2 (2003) 391-413
    • (2003) Cell Mol. Biol. Lett. , vol.2 , pp. 391-413
    • Luczaj, W.1    Skrzydlewska, E.2
  • 173
    • 0037145738 scopus 로고    scopus 로고
    • Aberrant expression of NOS isoforms in Alzheimer's disease is structurally related to nitrotyrosine formation
    • Luth H.J., Munch G., and Arendt T. Aberrant expression of NOS isoforms in Alzheimer's disease is structurally related to nitrotyrosine formation. Brain Res. 1-2 (2002) 135-143
    • (2002) Brain Res. , vol.1-2 , pp. 135-143
    • Luth, H.J.1    Munch, G.2    Arendt, T.3
  • 174
    • 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., and Halliwell B. An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease. J. Neurochem. 5 (1997) 2061-2069
    • (1997) J. Neurochem. , vol.5 , pp. 2061-2069
    • Lyras, L.1    Cairns, N.J.2    Jenner, A.3    Jenner, P.4    Halliwell, B.5
  • 175
    • 34347383021 scopus 로고    scopus 로고
    • Nitric oxide and nitroxidative stress in Alzheimer's disease
    • Malinski T. Nitric oxide and nitroxidative stress in Alzheimer's disease. J. Alzheimers Dis. 2 (2007) 207-218
    • (2007) J. Alzheimers Dis. , vol.2 , pp. 207-218
    • Malinski, T.1
  • 178
  • 180
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery W.R., and Carney J.M. Oxidative alterations in Alzheimer's disease. Brain Pathol. 1 (1999) 133-146
    • (1999) Brain Pathol. , vol.1 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 181
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery W.R., and Lovell M.A. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol. Aging 1 (1998) 33-36
    • (1998) Neurobiol. Aging , vol.1 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 182
    • 34447279020 scopus 로고    scopus 로고
    • Damage to lipids, proteins, DNA, and RNA in mild cognitive impairment
    • Markesbery W.R., and Lovell M.A. Damage to lipids, proteins, DNA, and RNA in mild cognitive impairment. Arch. Neurol. 7 (2007) 954-956
    • (2007) Arch. Neurol. , vol.7 , pp. 954-956
    • Markesbery, W.R.1    Lovell, M.A.2
  • 183
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • Markesbery W.R., Kryscio R.J., Lovell M.A., and Morrow J.D. Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment. Ann. Neurol. 5 (2005) 730-735
    • (2005) Ann. Neurol. , vol.5 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 184
    • 0042847291 scopus 로고    scopus 로고
    • Neurotoxic mechanisms caused by the Alzheimer's disease-linked Swedish amyloid precursor protein mutation: oxidative stress, caspases, and the JNK pathway
    • Marques C.A., Keil U., Bonert A., Steiner B., Haass C., Muller W.E., and Eckert A. Neurotoxic mechanisms caused by the Alzheimer's disease-linked Swedish amyloid precursor protein mutation: oxidative stress, caspases, and the JNK pathway. J. Biol. Chem. 30 (2003) 28294-28302
    • (2003) J. Biol. Chem. , vol.30 , pp. 28294-28302
    • Marques, C.A.1    Keil, U.2    Bonert, A.3    Steiner, B.4    Haass, C.5    Muller, W.E.6    Eckert, A.7
  • 185
    • 0025305245 scopus 로고
    • Chemical influences on the specificity of tyrosine phosphorylation
    • Martin B.L., Wu D., Jakes S., and Graves D.J. Chemical influences on the specificity of tyrosine phosphorylation. J. Biol. Chem. 13 (1990) 7108-7111
    • (1990) J. Biol. Chem. , vol.13 , pp. 7108-7111
    • Martin, B.L.1    Wu, D.2    Jakes, S.3    Graves, D.J.4
  • 187
    • 0038359684 scopus 로고    scopus 로고
    • Biomarkers of diabetes-associated oxidative stress and antioxidant status in young diabetic patients with or without subclinical complications
    • Martin-Gallan P., Carrascosa A., Gussinye M., and Dominguez C. Biomarkers of diabetes-associated oxidative stress and antioxidant status in young diabetic patients with or without subclinical complications. Free Radic. Biol. Med. 12 (2003) 1563-1574
    • (2003) Free Radic. Biol. Med. , vol.12 , pp. 1563-1574
    • Martin-Gallan, P.1    Carrascosa, A.2    Gussinye, M.3    Dominguez, C.4
  • 188
    • 0032007328 scopus 로고    scopus 로고
    • Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity
    • Mattson M.P. Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity. Trends Neurosci. 2 (1998) 53-57
    • (1998) Trends Neurosci. , vol.2 , pp. 53-57
    • Mattson, M.P.1
  • 189
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 7000 (2004) 631-639
    • (2004) Nature , vol.7000 , pp. 631-639
    • Mattson, M.P.1
  • 190
    • 22144483112 scopus 로고    scopus 로고
    • Supplemental use of antioxidant vitamins and subsequent risk of cognitive decline and dementia
    • Maxwell C.J., Hicks M.S., Hogan D.B., Basran J., and Ebly E.M. Supplemental use of antioxidant vitamins and subsequent risk of cognitive decline and dementia. Dement. Geriatr. Cogn. Disord. 1 (2005) 45-51
    • (2005) Dement. Geriatr. Cogn. Disord. , vol.1 , pp. 45-51
    • Maxwell, C.J.1    Hicks, M.S.2    Hogan, D.B.3    Basran, J.4    Ebly, E.M.5
  • 191
    • 0037171066 scopus 로고    scopus 로고
    • Oxidative protein damage in cells engaged in beta-amyloidosis is related to apoE genotype
    • Mazur-Kolecka B., Frackowiak J., Kowal D., Krzeslowska J., and Dickson D. Oxidative protein damage in cells engaged in beta-amyloidosis is related to apoE genotype. Neuroreport 4 (2002) 465-468
    • (2002) Neuroreport , vol.4 , pp. 465-468
    • Mazur-Kolecka, B.1    Frackowiak, J.2    Kowal, D.3    Krzeslowska, J.4    Dickson, D.5
  • 193
    • 0034834620 scopus 로고    scopus 로고
    • Increased oxidative stress in Alzheimer's disease as assessed with 4-hydroxynonenal but not malondialdehyde
    • McGrath L.T., McGleenon B.M., Brennan S., McColl D., Mc I.S., and Passmore A.P. Increased oxidative stress in Alzheimer's disease as assessed with 4-hydroxynonenal but not malondialdehyde. QJM 9 (2001) 485-490
    • (2001) QJM , vol.9 , pp. 485-490
    • McGrath, L.T.1    McGleenon, B.M.2    Brennan, S.3    McColl, D.4    Mc, I.S.5    Passmore, A.P.6
  • 194
    • 0030910847 scopus 로고    scopus 로고
    • Increased susceptibility of Alzheimer's disease temporal cortex to oxygen free radical-mediated processes
    • McIntosh L.J., Trush M.A., and Troncoso J.C. Increased susceptibility of Alzheimer's disease temporal cortex to oxygen free radical-mediated processes. Free Radic. Biol. Med. 2 (1997) 183-190
    • (1997) Free Radic. Biol. Med. , vol.2 , pp. 183-190
    • McIntosh, L.J.1    Trush, M.A.2    Troncoso, J.C.3
  • 196
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • Mecocci P., MacGarvey U., and Beal M.F. Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Ann. Neurol. 5 (1994) 747-751
    • (1994) Ann. Neurol. , vol.5 , pp. 747-751
    • Mecocci, P.1    MacGarvey, U.2    Beal, M.F.3
  • 200
    • 4544307465 scopus 로고    scopus 로고
    • Modeling mitochondrial function in aging neurons
    • Melov S. Modeling mitochondrial function in aging neurons. Trends Neurosci. 10 (2004) 601-606
    • (2004) Trends Neurosci. , vol.10 , pp. 601-606
    • Melov, S.1
  • 201
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal J.J., Gallogly M.M., Qanungo S., Sabens E.A., and Shelton M.D. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 11 (2008) 1941-1988
    • (2008) Antioxid. Redox Signal. , vol.11 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 202
    • 13644253800 scopus 로고    scopus 로고
    • Searching for the role and the most suitable biomarkers of oxidative stress in Alzheimer's disease and in other neurodegenerative diseases
    • Migliore L., Fontana I., Colognato R., Coppede F., Siciliano G., and Murri L. Searching for the role and the most suitable biomarkers of oxidative stress in Alzheimer's disease and in other neurodegenerative diseases. Neurobiol. Aging 5 (2005) 587-595
    • (2005) Neurobiol. Aging , vol.5 , pp. 587-595
    • Migliore, L.1    Fontana, I.2    Colognato, R.3    Coppede, F.4    Siciliano, G.5    Murri, L.6
  • 204
    • 0029765553 scopus 로고    scopus 로고
    • Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides
    • Miyata M., and Smith J.D. Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides. Nat. Genet. 1 (1996) 55-61
    • (1996) Nat. Genet. , vol.1 , pp. 55-61
    • Miyata, M.1    Smith, J.D.2
  • 205
    • 0031028437 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4
    • Montine K.S., Olson S.J., Amarnath V., Whetsell Jr. W.O., Graham D.G., and Montine T.J. Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4. Am. J. Pathol. 2 (1997) 437-443
    • (1997) Am. J. Pathol. , vol.2 , pp. 437-443
    • Montine, K.S.1    Olson, S.J.2    Amarnath, V.3    Whetsell Jr., W.O.4    Graham, D.G.5    Montine, T.J.6
  • 206
    • 0031594916 scopus 로고    scopus 로고
    • Cerebrospinal fluid F2-isoprostane levels are increased in Alzheimer's disease
    • Montine T.J., Markesbery W.R., Morrow J.D., and Roberts II L.J. Cerebrospinal fluid F2-isoprostane levels are increased in Alzheimer's disease. Ann. Neurol. 3 (1998) 410-413
    • (1998) Ann. Neurol. , vol.3 , pp. 410-413
    • Montine, T.J.1    Markesbery, W.R.2    Morrow, J.D.3    Roberts II, L.J.4
  • 208
    • 0032886795 scopus 로고    scopus 로고
    • The magnitude of brain lipid peroxidation correlates with the extent of degeneration but not with density of neuritic plaques or neurofibrillary tangles or with APOE genotype in Alzheimer's disease patients
    • Montine T.J., Markesbery W.R., Zackert W., Sanchez S.C., Roberts II L.J., and Morrow J.D. The magnitude of brain lipid peroxidation correlates with the extent of degeneration but not with density of neuritic plaques or neurofibrillary tangles or with APOE genotype in Alzheimer's disease patients. Am. J. Pathol. 3 (1999) 863-868
    • (1999) Am. J. Pathol. , vol.3 , pp. 863-868
    • Montine, T.J.1    Markesbery, W.R.2    Zackert, W.3    Sanchez, S.C.4    Roberts II, L.J.5    Morrow, J.D.6
  • 210
    • 0033663880 scopus 로고    scopus 로고
    • No difference in plasma or urinary F2-isoprostanes among patients with Huntington's disease or Alzheimer's disease and controls
    • Montine T.J., Shinobu L., Montine K.S., Roberts II L.J., Kowall N.W., Beal M.F., and Morrow J.D. No difference in plasma or urinary F2-isoprostanes among patients with Huntington's disease or Alzheimer's disease and controls. Ann. Neurol. 6 (2000) 950
    • (2000) Ann. Neurol. , vol.6 , pp. 950
    • Montine, T.J.1    Shinobu, L.2    Montine, K.S.3    Roberts II, L.J.4    Kowall, N.W.5    Beal, M.F.6    Morrow, J.D.7
  • 211
    • 0034745018 scopus 로고    scopus 로고
    • Cerebrospinal fluid abeta42, tau, and f2-isoprostane concentrations in patients with Alzheimer disease, other dementias, and in age-matched controls
    • Montine T.J., Kaye J.A., Montine K.S., McFarland L., Morrow J.D., and Quinn J.F. Cerebrospinal fluid abeta42, tau, and f2-isoprostane concentrations in patients with Alzheimer disease, other dementias, and in age-matched controls. Arch. Pathol. Lab. Med. 4 (2001) 510-512
    • (2001) Arch. Pathol. Lab. Med. , vol.4 , pp. 510-512
    • Montine, T.J.1    Kaye, J.A.2    Montine, K.S.3    McFarland, L.4    Morrow, J.D.5    Quinn, J.F.6
  • 213
    • 35348817935 scopus 로고    scopus 로고
    • F(2)-isoprostanes as biomarkers of late-onset Alzheimer's disease
    • Montine T.J., Quinn J., Kaye J., and Morrow J.D. F(2)-isoprostanes as biomarkers of late-onset Alzheimer's disease. J. Mol. Neurosci. 1 (2007) 114-119
    • (2007) J. Mol. Neurosci. , vol.1 , pp. 114-119
    • Montine, T.J.1    Quinn, J.2    Kaye, J.3    Morrow, J.D.4
  • 214
    • 10044235066 scopus 로고    scopus 로고
    • Isoprostanes: markers and mediators of oxidative stress
    • Montuschi P., Barnes P.J., and Roberts II L.J. Isoprostanes: markers and mediators of oxidative stress. FASEB J. 15 (2004) 1791-1800
    • (2004) FASEB J. , vol.15 , pp. 1791-1800
    • Montuschi, P.1    Barnes, P.J.2    Roberts II, L.J.3
  • 215
    • 0026021804 scopus 로고
    • Astrocytes, not neurons, produce docosahexaenoic acid (22:6 omega-3) and arachidonic acid (20:4 omega-6)
    • Moore S.A., Yoder E., Murphy S., Dutton G.R., and Spector A.A. Astrocytes, not neurons, produce docosahexaenoic acid (22:6 omega-3) and arachidonic acid (20:4 omega-6). J. Neurochem. 2 (1991) 518-524
    • (1991) J. Neurochem. , vol.2 , pp. 518-524
    • Moore, S.A.1    Yoder, E.2    Murphy, S.3    Dutton, G.R.4    Spector, A.A.5
  • 219
    • 0037178579 scopus 로고    scopus 로고
    • Dietary intake of antioxidant nutrients and the risk of incident Alzheimer disease in a biracial community study
    • Morris M.C., Evans D.A., Bienias J.L., Tangney C.C., Bennett D.A., Aggarwal N., Wilson R.S., and Scherr P.A. Dietary intake of antioxidant nutrients and the risk of incident Alzheimer disease in a biracial community study. JAMA 24 (2002) 3230-3237
    • (2002) JAMA , vol.24 , pp. 3230-3237
    • Morris, M.C.1    Evans, D.A.2    Bienias, J.L.3    Tangney, C.C.4    Bennett, D.A.5    Aggarwal, N.6    Wilson, R.S.7    Scherr, P.A.8
  • 220
    • 13244279737 scopus 로고    scopus 로고
    • Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans
    • Morrow J.D. Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans. Arterioscler. Thromb. Vasc. Biol. 2 (2005) 279-286
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.2 , pp. 279-286
    • Morrow, J.D.1
  • 221
    • 0026443725 scopus 로고
    • Non-cyclooxygenase-derived prostanoids (F2-isoprostanes) are formed in situ on phospholipids
    • Morrow J.D., Awad J.A., Boss H.J., Blair I.A., and Roberts II L.J. Non-cyclooxygenase-derived prostanoids (F2-isoprostanes) are formed in situ on phospholipids. Proc. Natl. Acad. Sci. U.S.A. 22 (1992) 10721-10725
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.22 , pp. 10721-10725
    • Morrow, J.D.1    Awad, J.A.2    Boss, H.J.3    Blair, I.A.4    Roberts II, L.J.5
  • 223
    • 0025297786 scopus 로고
    • Increased levels of DNA breaks in cerebral cortex of Alzheimer's disease patients
    • Mullaart E., Boerrigter M.E., Ravid R., Swaab D.F., and Vijg J. Increased levels of DNA breaks in cerebral cortex of Alzheimer's disease patients. Neurobiol. Aging 3 (1990) 169-173
    • (1990) Neurobiol. Aging , vol.3 , pp. 169-173
    • Mullaart, E.1    Boerrigter, M.E.2    Ravid, R.3    Swaab, D.F.4    Vijg, J.5
  • 225
    • 0032518993 scopus 로고    scopus 로고
    • 1,N2-propanodeoxyguanosine adducts: potential new biomarkers of smoking-induced DNA damage in human oral tissue
    • Nath R.G., Ocando J.E., Guttenplan J.B., and Chung F.L. 1,N2-propanodeoxyguanosine adducts: potential new biomarkers of smoking-induced DNA damage in human oral tissue. Cancer Res. 4 (1998) 581-584
    • (1998) Cancer Res. , vol.4 , pp. 581-584
    • Nath, R.G.1    Ocando, J.E.2    Guttenplan, J.B.3    Chung, F.L.4
  • 226
    • 34250165391 scopus 로고    scopus 로고
    • Protein thiols and thiobarbituric acid reactive substance status in colon cancer patients
    • Nayak B.S., and Pinto S. Protein thiols and thiobarbituric acid reactive substance status in colon cancer patients. Scand. J. Gastroenterol. 7 (2007) 848-851
    • (2007) Scand. J. Gastroenterol. , vol.7 , pp. 848-851
    • Nayak, B.S.1    Pinto, S.2
  • 228
    • 0027156933 scopus 로고
    • Dynamics of lipid peroxidation and its inhibition by antioxidants
    • Niki E., Noguchi N., and Gotoh N. Dynamics of lipid peroxidation and its inhibition by antioxidants. Biochem. Soc. Trans. 2 (1993) 313-317
    • (1993) Biochem. Soc. Trans. , vol.2 , pp. 313-317
    • Niki, E.1    Noguchi, N.2    Gotoh, N.3
  • 229
    • 0032586942 scopus 로고    scopus 로고
    • F4-isoprostanes as specific marker of docosahexaenoic acid peroxidation in Alzheimer's disease
    • Nourooz-Zadeh J., Liu E.H., Yhlen B., Anggard E.E., and Halliwell B. F4-isoprostanes as specific marker of docosahexaenoic acid peroxidation in Alzheimer's disease. J. Neurochem. 2 (1999) 734-740
    • (1999) J. Neurochem. , vol.2 , pp. 734-740
    • Nourooz-Zadeh, J.1    Liu, E.H.2    Yhlen, B.3    Anggard, E.E.4    Halliwell, B.5
  • 234
    • 69049104575 scopus 로고    scopus 로고
    • Involvement of oxidative stress in the early-stage of Alzheimer's disease: implications for therapeutics
    • Nunomura A., Moreira P.I., Zhu X., Smith M.A., and Perry G. Involvement of oxidative stress in the early-stage of Alzheimer's disease: implications for therapeutics. Trends Alzheimer's Dis. Res. (2006)
    • (2006) Trends Alzheimer's Dis. Res.
    • Nunomura, A.1    Moreira, P.I.2    Zhu, X.3    Smith, M.A.4    Perry, G.5
  • 235
    • 0036174035 scopus 로고    scopus 로고
    • Malondialdehyde, superoxide dismutase, melatonin, iron, copper, and zinc blood concentrations in patients with Alzheimer disease: cross-sectional study
    • Ozcankaya R., and Delibas N. Malondialdehyde, superoxide dismutase, melatonin, iron, copper, and zinc blood concentrations in patients with Alzheimer disease: cross-sectional study. Croat. Med. J. 1 (2002) 28-32
    • (2002) Croat. Med. J. , vol.1 , pp. 28-32
    • Ozcankaya, R.1    Delibas, N.2
  • 236
    • 0028181782 scopus 로고
    • Selective increase in lipid peroxidation in the inferior temporal cortex in Alzheimer's disease
    • Palmer A.M., and Burns M.A. Selective increase in lipid peroxidation in the inferior temporal cortex in Alzheimer's disease. Brain Res. 1-2 (1994) 338-342
    • (1994) Brain Res. , vol.1-2 , pp. 338-342
    • Palmer, A.M.1    Burns, M.A.2
  • 237
    • 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., and 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. 22 (2005) 21522-21530
    • (2005) J. Biol. Chem. , vol.22 , 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
  • 238
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of oxidative stress in Alzheimer's disease
    • Pappolla M.A., Omar R.A., Kim K.S., and Robakis N.K. Immunohistochemical evidence of oxidative stress in Alzheimer's disease. Am. J. Pathol. 3 (1992) 621-628
    • (1992) Am. J. Pathol. , vol.3 , pp. 621-628
    • Pappolla, M.A.1    Omar, R.A.2    Kim, K.S.3    Robakis, N.K.4
  • 240
    • 0033004618 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxynonenal impairs glutamate and glucose transport and choline acetyltransferase activity in NSC-19 motor neuron cells
    • Pedersen W.A., Cashman N.R., and Mattson M.P. The lipid peroxidation product 4-hydroxynonenal impairs glutamate and glucose transport and choline acetyltransferase activity in NSC-19 motor neuron cells. Exp. Neurol. 1 (1999) 1-10
    • (1999) Exp. Neurol. , vol.1 , pp. 1-10
    • Pedersen, W.A.1    Cashman, N.R.2    Mattson, M.P.3
  • 241
    • 0030949126 scopus 로고    scopus 로고
    • The relation between antioxidants and memory performance in the old and very old
    • Perrig W.J., Perrig P., and Stahelin H.B. The relation between antioxidants and memory performance in the old and very old. J. Am. Geriatr. Soc. 6 (1997) 718-724
    • (1997) J. Am. Geriatr. Soc. , vol.6 , pp. 718-724
    • Perrig, W.J.1    Perrig, P.2    Stahelin, H.B.3
  • 243
    • 34848917624 scopus 로고    scopus 로고
    • Mitochondrial effects of lipid-derived neurotoxins
    • Picklo Sr. M.J., and Montine T.J. Mitochondrial effects of lipid-derived neurotoxins. J. Alzheimers Dis. 2 (2007) 185-193
    • (2007) J. Alzheimers Dis. , vol.2 , pp. 185-193
    • Picklo Sr., M.J.1    Montine, T.J.2
  • 244
    • 0029952157 scopus 로고    scopus 로고
    • Oxidative stress in clinical situations-fact or fiction?
    • Pincemail J., Defraigne J.O., and Limet R. Oxidative stress in clinical situations-fact or fiction?. Eur. J. Anaesthesiol. 3 (1996) 219-234
    • (1996) Eur. J. Anaesthesiol. , vol.3 , pp. 219-234
    • Pincemail, J.1    Defraigne, J.O.2    Limet, R.3
  • 245
    • 0036970014 scopus 로고    scopus 로고
    • Plasma susceptibility to free radical-induced antioxidant consumption and lipid peroxidation is increased in very old subjects with Alzheimer disease
    • Polidori M.C., and Mecocci P. Plasma susceptibility to free radical-induced antioxidant consumption and lipid peroxidation is increased in very old subjects with Alzheimer disease. J. Alzheimers Dis. 6 (2002) 517-522
    • (2002) J. Alzheimers Dis. , vol.6 , pp. 517-522
    • Polidori, M.C.1    Mecocci, P.2
  • 246
    • 0034883155 scopus 로고    scopus 로고
    • Peripheral non-enzymatic antioxidant changes with human aging: a selective status report
    • Polidori M.C., Cherubini A., Senin U., and Mecocci P. Peripheral non-enzymatic antioxidant changes with human aging: a selective status report. Biogerontology 2 (2001) 99-104
    • (2001) Biogerontology , vol.2 , pp. 99-104
    • Polidori, M.C.1    Cherubini, A.2    Senin, U.3    Mecocci, P.4
  • 248
    • 5644239560 scopus 로고    scopus 로고
    • Plasma antioxidant status, immunoglobulin g oxidation and lipid peroxidation in demented patients: relevance to Alzheimer disease and vascular dementia
    • Polidori M.C., Mattioli P., Aldred S., Cecchetti R., Stahl W., Griffiths H., Senin U., Sies H., and Mecocci P. Plasma antioxidant status, immunoglobulin g oxidation and lipid peroxidation in demented patients: relevance to Alzheimer disease and vascular dementia. Dement. Geriatr. Cogn. Disord. 3-4 (2004) 265-270
    • (2004) Dement. Geriatr. Cogn. Disord. , vol.3-4 , pp. 265-270
    • Polidori, M.C.1    Mattioli, P.2    Aldred, S.3    Cecchetti, R.4    Stahl, W.5    Griffiths, H.6    Senin, U.7    Sies, H.8    Mecocci, P.9
  • 249
    • 34249068577 scopus 로고    scopus 로고
    • Hallmarks of protein oxidative damage in neurodegenerative diseases: focus on Alzheimer's disease
    • Polidori M.C., Griffiths H.R., Mariani E., and Mecocci P. Hallmarks of protein oxidative damage in neurodegenerative diseases: focus on Alzheimer's disease. Amino Acids 4 (2007) 553-559
    • (2007) Amino Acids , vol.4 , pp. 553-559
    • Polidori, M.C.1    Griffiths, H.R.2    Mariani, E.3    Mecocci, P.4
  • 250
    • 0028959042 scopus 로고
    • Mechanisms of free radical oxidation of unsaturated lipids
    • Porter N.A., Caldwell S.E., and Mills K.A. Mechanisms of free radical oxidation of unsaturated lipids. Lipids 4 (1995) 277-290
    • (1995) Lipids , vol.4 , pp. 277-290
    • Porter, N.A.1    Caldwell, S.E.2    Mills, K.A.3
  • 251
    • 57649221161 scopus 로고    scopus 로고
    • Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows
    • Praticò D. Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows. Ann. N. Y. Acad. Sci. (2008) 70-78
    • (2008) Ann. N. Y. Acad. Sci. , pp. 70-78
    • Praticò, D.1
  • 252
    • 2342420034 scopus 로고    scopus 로고
    • Lipid peroxidation and oxidative imbalance: early functional events in Alzheimer's disease
    • Praticò D., and Sung S. Lipid peroxidation and oxidative imbalance: early functional events in Alzheimer's disease. J. Alzheimers Dis. 2 (2004) 171-175
    • (2004) J. Alzheimers Dis. , vol.2 , pp. 171-175
    • Praticò, D.1    Sung, S.2
  • 253
    • 0032238783 scopus 로고    scopus 로고
    • Increased F2-isoprostanes in Alzheimer's disease: evidence for enhanced lipid peroxidation in vivo
    • Praticò D., Lee V.M.Y., Trojanowski J.Q., Rokach J., and Fitzgerald G.A. Increased F2-isoprostanes in Alzheimer's disease: evidence for enhanced lipid peroxidation in vivo. FASEB J. 15 (1998) 1777-1783
    • (1998) FASEB J. , vol.15 , pp. 1777-1783
    • Praticò, D.1    Lee, V.M.Y.2    Trojanowski, J.Q.3    Rokach, J.4    Fitzgerald, G.A.5
  • 254
    • 0033762711 scopus 로고    scopus 로고
    • Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: correlation of a noninvasive index of lipid peroxidation with disease severity
    • Praticò D., Clark C.M., Lee V.M., Trojanowski J.Q., Rokach J., and FitzGerald G.A. Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: correlation of a noninvasive index of lipid peroxidation with disease severity. Ann. Neurol. 5 (2000) 809-812
    • (2000) Ann. Neurol. , vol.5 , pp. 809-812
    • Praticò, D.1    Clark, C.M.2    Lee, V.M.3    Trojanowski, J.Q.4    Rokach, J.5    FitzGerald, G.A.6
  • 255
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • Praticò D., Uryu K., Leight S., Trojanoswki J.Q., and Lee V.M. Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. J. Neurosci. 12 (2001) 4183-4187
    • (2001) J. Neurosci. , vol.12 , pp. 4183-4187
    • Praticò, D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.5
  • 256
    • 0036284936 scopus 로고    scopus 로고
    • Increase of brain oxidative stress in mild cognitive impairment: a possible predictor of Alzheimer disease
    • Praticò D., Clark C.M., Liun F., Rokach J., Lee V.Y., and Trojanowski J.Q. Increase of brain oxidative stress in mild cognitive impairment: a possible predictor of Alzheimer disease. Arch. Neurol. 6 (2002) 972-976
    • (2002) Arch. Neurol. , vol.6 , pp. 972-976
    • Praticò, D.1    Clark, C.M.2    Liun, F.3    Rokach, J.4    Lee, V.Y.5    Trojanowski, J.Q.6
  • 257
    • 0025285284 scopus 로고
    • Suggested mechanisms for the production of 4-hydroxy-2-nonenal from the autoxidation of polyunsaturated fatty acids
    • Pryor W.A., and Porter N.A. Suggested mechanisms for the production of 4-hydroxy-2-nonenal from the autoxidation of polyunsaturated fatty acids. Free Radic. Biol. Med. 6 (1990) 541-543
    • (1990) Free Radic. Biol. Med. , vol.6 , pp. 541-543
    • Pryor, W.A.1    Porter, N.A.2
  • 260
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease
    • Reddy P.H., and Beal M.F. Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease. Trends Mol. Med. 2 (2008) 45-53
    • (2008) Trends Mol. Med. , vol.2 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 262
    • 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
    • Reed T., Perluigi M., Sultana R., Pierce W.M., Klein J.B., Turner D.M., Coccia R., Markesbery W.R., and Butterfield D.A. 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. 1 (2008) 107-120
    • (2008) Neurobiol. Dis. , vol.1 , 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
  • 263
    • 0035144956 scopus 로고    scopus 로고
    • Brain regional quantification of F-ring and D-/E-ring isoprostanes and neuroprostanes in Alzheimer's disease
    • Reich E.E., Markesbery W.R., Roberts II L.J., Swift L.L., Morrow J.D., and Montine T.J. Brain regional quantification of F-ring and D-/E-ring isoprostanes and neuroprostanes in Alzheimer's disease. Am. J. Pathol. 1 (2001) 293-297
    • (2001) Am. J. Pathol. , vol.1 , pp. 293-297
    • Reich, E.E.1    Markesbery, W.R.2    Roberts II, L.J.3    Swift, L.L.4    Morrow, J.D.5    Montine, T.J.6
  • 267
  • 268
    • 0036286490 scopus 로고    scopus 로고
    • Products of the isoprostane pathway: unique bioactive compounds and markers of lipid peroxidation
    • Roberts II L.J., and Morrow J.D. Products of the isoprostane pathway: unique bioactive compounds and markers of lipid peroxidation. Cell. Mol. Life Sci. 5 (2002) 808-820
    • (2002) Cell. Mol. Life Sci. , vol.5 , pp. 808-820
    • Roberts II, L.J.1    Morrow, J.D.2
  • 270
    • 0035997240 scopus 로고    scopus 로고
    • The state versus amyloid-beta: the trial of the most wanted criminal in Alzheimer disease
    • Rottkamp C.A., Atwood C.S., Joseph J.A., Nunomura A., Perry G., and Smith M.A. The state versus amyloid-beta: the trial of the most wanted criminal in Alzheimer disease. Peptides 7 (2002) 1333-1341
    • (2002) Peptides , vol.7 , pp. 1333-1341
    • Rottkamp, C.A.1    Atwood, C.S.2    Joseph, J.A.3    Nunomura, A.4    Perry, G.5    Smith, M.A.6
  • 271
    • 1842788079 scopus 로고    scopus 로고
    • Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease
    • Ryberg H., Soderling A.S., Davidsson P., Blennow K., Caidahl K., and Persson L.I. Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease. Neurochem. Int. 1 (2004) 57-62
    • (2004) Neurochem. Int. , vol.1 , pp. 57-62
    • Ryberg, H.1    Soderling, A.S.2    Davidsson, P.3    Blennow, K.4    Caidahl, K.5    Persson, L.I.6
  • 273
    • 34848928487 scopus 로고    scopus 로고
    • Enhanced glycation of hemoglobin and plasma proteins is associated with increased lipid peroxide levels in non-diabetic hypertensive subjects
    • Sathiyapriya V., Selvaraj N., Nandeesha H., Bobby Z., Agrawal A., and Pavithran P. Enhanced glycation of hemoglobin and plasma proteins is associated with increased lipid peroxide levels in non-diabetic hypertensive subjects. Arch. Med. Res. 8 (2007) 822-826
    • (2007) Arch. Med. Res. , vol.8 , pp. 822-826
    • Sathiyapriya, V.1    Selvaraj, N.2    Nandeesha, H.3    Bobby, Z.4    Agrawal, A.5    Pavithran, P.6
  • 274
    • 0030983405 scopus 로고    scopus 로고
    • Mechanisms of neurotoxicity associated with amyloid beta deposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal
    • Sayre L.M., Zagorski M.G., Surewicz W.K., Krafft G.A., and Perry G. Mechanisms of neurotoxicity associated with amyloid beta deposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal. Chem. Res. Toxicol. 5 (1997) 518-526
    • (1997) Chem. Res. Toxicol. , vol.5 , pp. 518-526
    • Sayre, L.M.1    Zagorski, M.G.2    Surewicz, W.K.3    Krafft, G.A.4    Perry, G.5
  • 275
    • 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., and Smith M.A. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J. Neurochem. 5 (1997) 2092-2097
    • (1997) J. Neurochem. , vol.5 , 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
  • 277
    • 0031730398 scopus 로고    scopus 로고
    • Plasma antioxidants and cognitive performance in middle-aged and older adults: results of the Austrian Stroke Prevention Study
    • Schmidt R., Hayn M., Reinhart B., Roob G., Schmidt H., Schumacher M., Watzinger N., and Launer L.J. Plasma antioxidants and cognitive performance in middle-aged and older adults: results of the Austrian Stroke Prevention Study. J. Am. Geriatr. Soc. 11 (1998) 1407-1410
    • (1998) J. Am. Geriatr. Soc. , vol.11 , pp. 1407-1410
    • Schmidt, R.1    Hayn, M.2    Reinhart, B.3    Roob, G.4    Schmidt, H.5    Schumacher, M.6    Watzinger, N.7    Launer, L.J.8
  • 278
    • 0344196903 scopus 로고    scopus 로고
    • NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?
    • Schopfer F.J., Baker P.R., and Freeman B.A. NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?. Trends Biochem. Sci. 12 (2003) 646-654
    • (2003) Trends Biochem. Sci. , vol.12 , pp. 646-654
    • Schopfer, F.J.1    Baker, P.R.2    Freeman, B.A.3
  • 279
    • 4544354817 scopus 로고    scopus 로고
    • Impact of gender on upregulation of antioxidant defence mechanisms in Alzheimer's disease brain
    • Schuessel K., Leutner S., Cairns N.J., Muller W.E., and Eckert A. Impact of gender on upregulation of antioxidant defence mechanisms in Alzheimer's disease brain. J. Neural. Transm. 9 (2004) 1167-1182
    • (2004) J. Neural. Transm. , vol.9 , pp. 1167-1182
    • Schuessel, K.1    Leutner, S.2    Cairns, N.J.3    Muller, W.E.4    Eckert, A.5
  • 281
    • 0034750776 scopus 로고    scopus 로고
    • Parkinson's disease is associated with oxidative stress: comparison of peripheral antioxidant profiles in living Parkinson's, Alzheimer's and vascular dementia patients
    • Serra J.A., Dominguez R.O., de Lustig E.S., Guareschi E.M., Famulari A.L., Bartolome E.L., and Marschoff E.R. Parkinson's disease is associated with oxidative stress: comparison of peripheral antioxidant profiles in living Parkinson's, Alzheimer's and vascular dementia patients. J. Neural. Transm. 10 (2001) 1135-1148
    • (2001) J. Neural. Transm. , vol.10 , pp. 1135-1148
    • Serra, J.A.1    Dominguez, R.O.2    de Lustig, E.S.3    Guareschi, E.M.4    Famulari, A.L.5    Bartolome, E.L.6    Marschoff, E.R.7
  • 282
    • 20444369173 scopus 로고    scopus 로고
    • Mitochondrial DNA, aconitase 'wraps' it up
    • Shadel G.S. Mitochondrial DNA, aconitase 'wraps' it up. Trends Biochem. Sci. 6 (2005) 294-296
    • (2005) Trends Biochem. Sci. , vol.6 , pp. 294-296
    • Shadel, G.S.1
  • 283
    • 33645961571 scopus 로고    scopus 로고
    • Quantification of oxidized RNAs in Alzheimer's disease
    • Shan X., and Lin C.L. Quantification of oxidized RNAs in Alzheimer's disease. Neurobiol. Aging 5 (2006) 657-662
    • (2006) Neurobiol. Aging , vol.5 , pp. 657-662
    • Shan, X.1    Lin, C.L.2
  • 284
    • 0038417076 scopus 로고    scopus 로고
    • The identification and characterization of oxidized RNAs in Alzheimer's disease
    • Shan X., Tashiro H., and Lin C.L. The identification and characterization of oxidized RNAs in Alzheimer's disease. J. Neurosci. 12 (2003) 4913-4921
    • (2003) J. Neurosci. , vol.12 , pp. 4913-4921
    • Shan, X.1    Tashiro, H.2    Lin, C.L.3
  • 285
    • 34548476954 scopus 로고    scopus 로고
    • Messenger RNA oxidation is an early event preceding cell death and causes reduced protein expression
    • Shan X., Chang Y., and Lin C.L. Messenger RNA oxidation is an early event preceding cell death and causes reduced protein expression. FASEB J. 11 (2007) 2753-2764
    • (2007) FASEB J. , vol.11 , pp. 2753-2764
    • Shan, X.1    Chang, Y.2    Lin, C.L.3
  • 286
    • 54949146482 scopus 로고    scopus 로고
    • Altered 8-oxoguanine glycosylase in mild cognitive impairment and late-stage Alzheimer's disease brain
    • Shao C., Xiong S., Li G.M., Gu L., Mao G., Markesbery W.R., and Lovell M.A. Altered 8-oxoguanine glycosylase in mild cognitive impairment and late-stage Alzheimer's disease brain. Free Radic. Biol. Med. 6 (2008) 813-819
    • (2008) Free Radic. Biol. Med. , vol.6 , pp. 813-819
    • Shao, C.1    Xiong, S.2    Li, G.M.3    Gu, L.4    Mao, G.5    Markesbery, W.R.6    Lovell, M.A.7
  • 287
    • 0033712579 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease
    • Shringarpure R., Grune T., Sitte N., and Davies K.J. 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease. Cell. Mol. Life Sci. 12 (2000) 1802-1809
    • (2000) Cell. Mol. Life Sci. , vol.12 , pp. 1802-1809
    • Shringarpure, R.1    Grune, T.2    Sitte, N.3    Davies, K.J.4
  • 288
    • 33846949357 scopus 로고    scopus 로고
    • The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation
    • Siegel S.J., Bieschke J., Powers E.T., and Kelly J.W. The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation. Biochemistry 6 (2007) 1503-1510
    • (2007) Biochemistry , vol.6 , pp. 1503-1510
    • Siegel, S.J.1    Bieschke, J.2    Powers, E.T.3    Kelly, J.W.4
  • 291
  • 292
    • 0027163166 scopus 로고
    • Differences in the fatty acid composition of the grey and white matter of different regions of the brains of patients with Alzheimer's disease and control subjects
    • Skinner E.R., Watt C., Besson J.A., and Best P.V. Differences in the fatty acid composition of the grey and white matter of different regions of the brains of patients with Alzheimer's disease and control subjects. Brain (1993) 717-725
    • (1993) Brain , pp. 717-725
    • Skinner, E.R.1    Watt, C.2    Besson, J.A.3    Best, P.V.4
  • 296
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith M.A., Harris P.L., Sayre L.M., and Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. U.S.A. 18 (1997) 9866-9868
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.18 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 298
    • 0027328852 scopus 로고
    • Protein oxidative damage is associated with life expectancy of houseflies
    • Sohal R.S., Agarwal S., Dubey A., and Orr W.C. Protein oxidative damage is associated with life expectancy of houseflies. Proc. Natl. Acad. Sci. U.S.A. 15 (1993) 7255-7259
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.15 , pp. 7255-7259
    • Sohal, R.S.1    Agarwal, S.2    Dubey, A.3    Orr, W.C.4
  • 299
    • 7244260495 scopus 로고    scopus 로고
    • Alzheimer's disease meets the ubiquitin-proteasome system
    • Song S., and Jung Y.K. Alzheimer's disease meets the ubiquitin-proteasome system. Trends Mol. Med. 11 (2004) 565-570
    • (2004) Trends Mol. Med. , vol.11 , pp. 565-570
    • Song, S.1    Jung, Y.K.2
  • 301
    • 2642680857 scopus 로고    scopus 로고
    • Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis
    • Stadelmann C., Bruck W., Bancher C., Jellinger K., and Lassmann H. Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis. J. Neuropathol. Exp. Neurol. 5 (1998) 456-464
    • (1998) J. Neuropathol. Exp. Neurol. , vol.5 , pp. 456-464
    • Stadelmann, C.1    Bruck, W.2    Bancher, C.3    Jellinger, K.4    Lassmann, H.5
  • 302
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman E.R., and Levine R.L. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 3-4 (2003) 207-218
    • (2003) Amino Acids , vol.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 303
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: biological consequences
    • Stadtman E.R., Moskovitz J., and Levine R.L. Oxidation of methionine residues of proteins: biological consequences. Antioxid. Redox Signal. 5 (2003) 577-582
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 304
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • Stocker R., and Keaney Jr. J.F. Role of oxidative modifications in atherosclerosis. Physiol. Rev. 4 (2004) 1381-1478
    • (2004) Physiol. Rev. , vol.4 , pp. 1381-1478
    • Stocker, R.1    Keaney Jr., J.F.2
  • 305
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su J.H., Anderson A.J., Cummings B.J., and Cotman C.W. Immunohistochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 18 (1994) 2529-2533
    • (1994) Neuroreport , vol.18 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 306
    • 0031558654 scopus 로고    scopus 로고
    • Neuronal DNA damage precedes tangle formation and is associated with up-regulation of nitrotyrosine in Alzheimer's disease brain
    • Su J.H., Deng G., and Cotman C.W. Neuronal DNA damage precedes tangle formation and is associated with up-regulation of nitrotyrosine in Alzheimer's disease brain. Brain Res. 1-2 (1997) 193-199
    • (1997) Brain Res. , vol.1-2 , pp. 193-199
    • Su, J.H.1    Deng, G.2    Cotman, C.W.3
  • 307
    • 0025334082 scopus 로고
    • Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro
    • Subbarao K.V., Richardson J.S., and Ang L.C. Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro. J. Neurochem. 1 (1990) 342-345
    • (1990) J. Neurochem. , vol.1 , pp. 342-345
    • Subbarao, K.V.1    Richardson, J.S.2    Ang, L.C.3
  • 308
    • 0031009367 scopus 로고    scopus 로고
    • Topographic associations between DNA fragmentation and Alzheimer's disease neuropathology in the hippocampus
    • Sugaya K., Reeves M., and McKinney M. Topographic associations between DNA fragmentation and Alzheimer's disease neuropathology in the hippocampus. Neurochem. Int. 2 (1997) 275-281
    • (1997) Neurochem. Int. , vol.2 , pp. 275-281
    • Sugaya, K.1    Reeves, M.2    McKinney, M.3
  • 310
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD
    • Sultana R., Boyd-Kimball D., Poon H.F., Cai J., Pierce W.M., Klein J.B., Merchant M., Markesbery W.R., and Butterfield D.A. Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD. Neurobiol. Aging 11 (2006) 1564-1576
    • (2006) Neurobiol. Aging , vol.11 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4    Pierce, W.M.5    Klein, J.B.6    Merchant, M.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 311
    • 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 D.A. 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. 1 (2006) 3-11
    • (2006) J. Chromatogr. B: Analyt. Technol. Biomed. Life Sci. , vol.1 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 312
    • 33947644871 scopus 로고    scopus 로고
    • Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: insights into mechanism of neurodegeneration from redox proteomics
    • Sultana R., Perluigi M., and Butterfield D.A. Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: insights into mechanism of neurodegeneration from redox proteomics. Antioxid. Redox Signal. 11-12 (2006) 2021-2037
    • (2006) Antioxid. Redox Signal. , vol.11-12 , pp. 2021-2037
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 314
    • 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.A. Protein levels and activity of some antioxidant enzymes in hippocampus of subjects with amnestic mild cognitive impairment. Neurochem. Res. 12 (2008) 2540-2546
    • (2008) Neurochem. Res. , vol.12 , pp. 2540-2546
    • Sultana, R.1    Piroddi, M.2    Galli, F.3    Butterfield, D.A.4
  • 316
    • 33745228920 scopus 로고    scopus 로고
    • The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression
    • Tamagno E., Bardini P., Guglielmotto M., Danni O., and Tabaton M. The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression. Free Radic. Biol. Med. 2 (2006) 202-212
    • (2006) Free Radic. Biol. Med. , vol.2 , pp. 202-212
    • Tamagno, E.1    Bardini, P.2    Guglielmotto, M.3    Danni, O.4    Tabaton, M.5
  • 318
    • 0033516677 scopus 로고    scopus 로고
    • Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease
    • Tohgi H., Abe T., Yamazaki K., Murata T., Ishizaki E., and Isobe C. Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease. Neurosci. Lett. 1 (1999) 52-54
    • (1999) Neurosci. Lett. , vol.1 , pp. 52-54
    • Tohgi, H.1    Abe, T.2    Yamazaki, K.3    Murata, T.4    Ishizaki, E.5    Isobe, C.6
  • 319
    • 0035867047 scopus 로고    scopus 로고
    • Sign of lipid peroxidation as measured in the urine of patients with probable Alzheimer's disease
    • Tuppo E.E., Forman L.J., Spur B.W., Chan-Ting R.E., Chopra A., and Cavalieri T.A. Sign of lipid peroxidation as measured in the urine of patients with probable Alzheimer's disease. Brain Res. Bull. 5 (2001) 565-568
    • (2001) Brain Res. Bull. , vol.5 , pp. 565-568
    • Tuppo, E.E.1    Forman, L.J.2    Spur, B.W.3    Chan-Ting, R.E.4    Chopra, A.5    Cavalieri, T.A.6
  • 320
    • 0034659147 scopus 로고    scopus 로고
    • Role of reactive aldehyde in cardiovascular diseases
    • Uchida K. Role of reactive aldehyde in cardiovascular diseases. Free Radic. Biol. Med. 12 (2000) 1685-1696
    • (2000) Free Radic. Biol. Med. , vol.12 , pp. 1685-1696
    • Uchida, K.1
  • 321
    • 0347991814 scopus 로고    scopus 로고
    • Histidine and lysine as targets of oxidative modification
    • Uchida K. Histidine and lysine as targets of oxidative modification. Amino Acids 3-4 (2003) 249-257
    • (2003) Amino Acids , vol.3-4 , pp. 249-257
    • Uchida, K.1
  • 322
    • 0037411282 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress
    • Uchida K. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog. Lipid Res. 4 (2003) 318-343
    • (2003) Prog. Lipid Res. , vol.4 , pp. 318-343
    • Uchida, K.1
  • 323
    • 0032568935 scopus 로고    scopus 로고
    • Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins
    • Uchida K., Kanematsu M., Morimitsu Y., Osawa T., Noguchi N., and Niki E. Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins. J. Biol. Chem. 26 (1998) 16058-16066
    • (1998) J. Biol. Chem. , vol.26 , pp. 16058-16066
    • Uchida, K.1    Kanematsu, M.2    Morimitsu, Y.3    Osawa, T.4    Noguchi, N.5    Niki, E.6
  • 325
    • 10844262488 scopus 로고    scopus 로고
    • Impairment of brain mitochondrial oxidative phosphorylation accompanying vitamin E oxidation induced by iron or reactive nitrogen species: a selective review
    • Vatassery G.T. Impairment of brain mitochondrial oxidative phosphorylation accompanying vitamin E oxidation induced by iron or reactive nitrogen species: a selective review. Neurochem. Res. 11 (2004) 1951-1959
    • (2004) Neurochem. Res. , vol.11 , pp. 1951-1959
    • Vatassery, G.T.1
  • 326
    • 18844408406 scopus 로고    scopus 로고
    • Glutathione conjugates of 4-hydroxy-2(E)-nonenal as biomarkers of hepatic oxidative stress-induced lipid peroxidation in rats
    • Volkel W., Alvarez-Sanchez R., Weick I., Mally A., Dekant W., and Pahler A. Glutathione conjugates of 4-hydroxy-2(E)-nonenal as biomarkers of hepatic oxidative stress-induced lipid peroxidation in rats. Free Radic. Biol. Med. 11 (2005) 1526-1536
    • (2005) Free Radic. Biol. Med. , vol.11 , pp. 1526-1536
    • Volkel, W.1    Alvarez-Sanchez, R.2    Weick, I.3    Mally, A.4    Dekant, W.5    Pahler, A.6
  • 328
    • 34249023987 scopus 로고    scopus 로고
    • The nuclear proteasome and the degradation of oxidatively damaged proteins
    • Voss P., and Grune T. The nuclear proteasome and the degradation of oxidatively damaged proteins. Amino Acids 4 (2007) 527-534
    • (2007) Amino Acids , vol.4 , pp. 527-534
    • Voss, P.1    Grune, T.2
  • 329
    • 33747687207 scopus 로고    scopus 로고
    • Plasma F2-isoprostane levels are increased in Alzheimer's disease: evidence of increased oxidative stress in vivo
    • Waddington E., Croft K., Clarnette R., Mori T., and Martins R. Plasma F2-isoprostane levels are increased in Alzheimer's disease: evidence of increased oxidative stress in vivo. Alzheimer's Rep. 2 (1999) 277-282
    • (1999) Alzheimer's Rep. , vol.2 , pp. 277-282
    • Waddington, E.1    Croft, K.2    Clarnette, R.3    Mori, T.4    Martins, R.5
  • 330
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. (2005) 359-407
    • (2005) Annu. Rev. Genet. , pp. 359-407
    • Wallace, D.C.1
  • 331
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 6880 (2002) 535-539
    • (2002) Nature , vol.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 332
    • 15644362313 scopus 로고    scopus 로고
    • In vitro photooxidation of nucleic acids by ultraviolet A radiation
    • Wamer W.G., and Wei R.R. In vitro photooxidation of nucleic acids by ultraviolet A radiation. Photochem. Photobiol. 3 (1997) 560-563
    • (1997) Photochem. Photobiol. , vol.3 , pp. 560-563
    • Wamer, W.G.1    Wei, R.R.2
  • 333
    • 18844462415 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease
    • Wang J., Xiong S., Xie C., Markesbery W.R., and Lovell M.A. Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease. J. Neurochem. 4 (2005) 953-962
    • (2005) J. Neurochem. , vol.4 , pp. 953-962
    • Wang, J.1    Xiong, S.2    Xie, C.3    Markesbery, W.R.4    Lovell, M.A.5
  • 334
    • 33645106680 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment
    • Wang J., Markesbery W.R., and Lovell M.A. Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment. J. Neurochem. 3 (2006) 825-832
    • (2006) J. Neurochem. , vol.3 , pp. 825-832
    • Wang, J.1    Markesbery, W.R.2    Lovell, M.A.3
  • 335
    • 34548802393 scopus 로고    scopus 로고
    • Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment
    • Weissman L., Jo D.G., Sorensen M.M., de Souza-Pinto N.C., Markesbery W.R., Mattson M.P., and Bohr V.A. Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment. Nucleic Acids Res. 16 (2007) 5545-5555
    • (2007) Nucleic Acids Res. , vol.16 , pp. 5545-5555
    • Weissman, L.1    Jo, D.G.2    Sorensen, M.M.3    de Souza-Pinto, N.C.4    Markesbery, W.R.5    Mattson, M.P.6    Bohr, V.A.7
  • 336
    • 18844434878 scopus 로고    scopus 로고
    • Analysis of derivatized biogenic aldehydes by LC tandem mass spectrometry
    • Williams T.I., Lovell M.A., and Lynn B.C. Analysis of derivatized biogenic aldehydes by LC tandem mass spectrometry. Anal. Chem. 10 (2005) 3383-3389
    • (2005) Anal. Chem. , vol.10 , pp. 3383-3389
    • Williams, T.I.1    Lovell, M.A.2    Lynn, B.C.3
  • 337
    • 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., and 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 8 (2006) 1094-1099
    • (2006) Neurobiol. Aging , vol.8 , pp. 1094-1099
    • Williams, T.I.1    Lynn, B.C.2    Markesbery, W.R.3    Lovell, M.A.4
  • 338
    • 0037081509 scopus 로고    scopus 로고
    • Dietary hydroxy fatty acids are absorbed in humans: implications for the measurement of 'oxidative stress' in vivo
    • Wilson R., Lyall K., Smyth L., Fernie C.E., and Riemersma R.A. Dietary hydroxy fatty acids are absorbed in humans: implications for the measurement of 'oxidative stress' in vivo. Free Radic. Biol. Med. 2 (2002) 162-168
    • (2002) Free Radic. Biol. Med. , vol.2 , pp. 162-168
    • Wilson, R.1    Lyall, K.2    Smyth, L.3    Fernie, C.E.4    Riemersma, R.A.5
  • 341
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • Yan S.D., Yan S.F., Chen X., Fu J., Chen M., Kuppusamy P., Smith M.A., Perry G., Godman G.C., Nawroth P., et al. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nat. Med. 7 (1995) 693-699
    • (1995) Nat. Med. , vol.7 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10
  • 343
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan L.J., Levine R.L., and Sohal R.S. Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl. Acad. Sci. U.S.A. 21 (1997) 11168-11172
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.21 , pp. 11168-11172
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 345
    • 0036752552 scopus 로고    scopus 로고
    • The role of polyunsaturated fatty acids in restoring the aging neuronal membrane
    • Yehuda S., Rabinovitz S., Carasso R.L., and Mostofsky D.I. The role of polyunsaturated fatty acids in restoring the aging neuronal membrane. Neurobiol. Aging 5 (2002) 843-853
    • (2002) Neurobiol. Aging , vol.5 , pp. 843-853
    • Yehuda, S.1    Rabinovitz, S.2    Carasso, R.L.3    Mostofsky, D.I.4
  • 347
    • 0033782845 scopus 로고    scopus 로고
    • Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease
    • Zhu X., Rottkamp C.A., Boux H., Takeda A., Perry G., and Smith M.A. Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease. J. Neuropathol. Exp. Neurol. 10 (2000) 880-888
    • (2000) J. Neuropathol. Exp. Neurol. , vol.10 , pp. 880-888
    • Zhu, X.1    Rottkamp, C.A.2    Boux, H.3    Takeda, A.4    Perry, G.5    Smith, M.A.6
  • 348
  • 349
    • 33947178563 scopus 로고    scopus 로고
    • Alzheimer disease, the two-hit hypothesis: an update
    • Zhu X., Lee H.G., Perry G., and Smith M.A. Alzheimer disease, the two-hit hypothesis: an update. Biochim. Biophys. Acta 4 (2007) 494-502
    • (2007) Biochim. Biophys. Acta , vol.4 , pp. 494-502
    • Zhu, X.1    Lee, H.G.2    Perry, G.3    Smith, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.