메뉴 건너뛰기




Volumn 46, Issue 4, 2012, Pages 565-576

Nuclear and mitochondrial DNA oxidation in Alzheimer's disease

Author keywords

8 hydroxyguanine; BER; Hydroxyl radical; Mitochondria; Nucleus

Indexed keywords

ANTIOXIDANT; CELL NUCLEUS DNA; METAL; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 84863229887     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.3109/10715762.2011.648188     Document Type: Review
Times cited : (45)

References (179)
  • 1
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau-a toxic pas de deux in Alzheimer ' s disease
    • Ittner LM, Gotz J. Amyloid-beta and tau-a toxic pas de deux in Alzheimer ' s disease. Nat Rev Neurosci 2011;12:65-72.
    • (2011) Nat Rev Neurosci , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 3
    • 84863262231 scopus 로고    scopus 로고
    • MTOR is a potential therapeutic target for Alzhiemer ' s disease
    • Sun M-K, editor Hauppauge, NY: Nova Science Publishers, Inc. in press
    • Santos RX, Moreira PI. mTOR is a potential therapeutic target for Alzhiemer ' s disease. In: Sun M-K, editor. Cognitive Sciences. Hauppauge, NY: Nova Science Publishers, Inc.; 2012. in press.
    • (2012) Cognitive Sciences
    • Santos, R.X.1    Moreira, P.I.2
  • 4
    • 79960345867 scopus 로고    scopus 로고
    • Genetics: Fi nding risk factors
    • Eisenstein M. Genetics: fi nding risk factors. Nature 2011; 475:S20-S22.
    • (2011) Nature , vol.475
    • Eisenstein, M.1
  • 5
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer' s disease mitochondrial cascade hypothesis
    • Swerdlow RH, Burns JM, Khan SM. The Alzheimer' s disease mitochondrial cascade hypothesis. J Alzheimers Dis 2010;20(Suppl 2):S265-279.
    • (2010) J Alzheimers Dis , vol.20 , Issue.SUPPL. 2
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 7
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identifi cation of oxidatively modifi ed hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer ' s disease
    • Butterfi eld DA, Poon HF, St Clair D, Keller JN, Pierce WM, Klein JB, Markesbery WR. Redox proteomics identifi cation of oxidatively modifi ed hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer ' s disease. Neurobiol Dis 2006;22:223-232.
    • (2006) Neurobiol Dis , vol.22 , 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
  • 8
    • 27144494994 scopus 로고    scopus 로고
    • Ribosome dysfunction is an early event in Alzheimer's disease
    • DOI 10.1523/JNEUROSCI.3040-05.2005
    • Ding Q, Markesbery WR, Chen Q, Li F, Keller JN. Ribosome dysfunction is an early event in Alzheimer ' s disease. J Neurosci 2005;25:9171-9175. (Pubitemid 41500825)
    • (2005) Journal of Neuroscience , vol.25 , Issue.40 , pp. 9171-9175
    • Ding, Q.1    Markesbery, W.R.2    Chen, Q.3    Li, F.4    Keller, J.N.5
  • 10
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • DOI 10.1002/ana.20629
    • Markesbery WR, Kryscio RJ, Lovell MA, Morrow JD. Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment. Ann Neurol 2005;58:730-735. (Pubitemid 41552548)
    • (2005) Annals of Neurology , vol.58 , Issue.5 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 11
    • 33645106680 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment
    • Wang J, Markesbery WR, Lovell MA. Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment. J Neurochem 2006;96:825-832.
    • (2006) J Neurochem , vol.96 , pp. 825-832
    • Wang, J.1    Markesbery, W.R.2    Lovell, M.A.3
  • 14
    • 80053110019 scopus 로고    scopus 로고
    • Oxidatively modifi ed nucleic acids in preclinical Alzheimer ' s disease (PCAD) brain
    • Lovell MA, Soman S, Bradley MA. Oxidatively modifi ed nucleic acids in preclinical Alzheimer ' s disease (PCAD) brain. Mech Ageing Dev 2011;132:443-448.
    • (2011) Mech Ageing Dev , vol.132 , pp. 443-448
    • Lovell, M.A.1    Soman, S.2    Bradley, M.A.3
  • 15
    • 84855801337 scopus 로고    scopus 로고
    • Modest amyloid deposition is associated with iron dysregulation, microglial activation, and oxidative stress
    • doi: 10.3233/JAD-2011-110614
    • Gallagher JJ, Finnegan ME, Grehan B, Dobson J, Collingwood JF, Lynch MA. Modest amyloid deposition is associated with iron dysregulation, microglial activation, and oxidative stress. J Alzheimers Dis 2011;doi: 10.3233/JAD-2011-110614.
    • (2011) J Alzheimers Dis
    • Gallagher, J.J.1    Finnegan, M.E.2    Grehan, B.3    Dobson, J.4    Collingwood, J.F.5    Lynch, M.A.6
  • 17
    • 67649687039 scopus 로고    scopus 로고
    • An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer ' s disease
    • Moreira PI, Duarte AI, Santos MS, Rego AC, Oliveira CR. An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer ' s disease. J Alzheimers Dis 2009;16:741-761.
    • (2009) J Alzheimers Dis , vol.16 , pp. 741-761
    • Moreira, P.I.1    Duarte, A.I.2    Santos, M.S.3    Rego, A.C.4    Oliveira, C.R.5
  • 18
    • 23844447372 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) and aging: Do we need them - Can we measure them - Should we block them?
    • DOI 10.1002/sita.200400053
    • Simm A, Brö m me H-J. Reactive oxygen species (ROS) and aging: do we need them-can we measure them-should we block them? Signal Transd 2005;5:115-125. (Pubitemid 41168380)
    • (2005) Signal Transduction , vol.5 , Issue.3 , pp. 115-125
    • Simm, A.1    Bromme, H.-J.2
  • 19
    • 75349112375 scopus 로고    scopus 로고
    • Mitochondrial turnover and aging of long-lived postmitotic cells: The mitochondrial-lysosomal axis theory of aging
    • Terman A, Kurz T, Navratil M, Arriaga EA, Brunk UT. Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging. Antioxid Redox Signal 2010;12:503-535.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 503-535
    • Terman, A.1    Kurz, T.2    Navratil, M.3    Arriaga, E.A.4    Brunk, U.T.5
  • 21
    • 0028587756 scopus 로고
    • Oxygen-derived species: Their relation to human disease and environmental stress
    • Halliwell B, Cross CE. Oxygen-derived species: their relation to human disease and environmental stress. Environ Health Perspect 1994;102(Suppl 10):5-12.
    • (1994) Environ Health Perspect , vol.102 , Issue.SUPPL. 10 , pp. 5-12
    • Halliwell, B.1    Cross, C.E.2
  • 24
    • 80052538857 scopus 로고    scopus 로고
    • Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer ' s disease: Implications for early intervention and therapeutics
    • Mao P, Reddy PH. Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer ' s disease: implications for early intervention and therapeutics. Biochim Biophys Acta 2011;1812:1359-1370.
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 1359-1370
    • Mao, P.1    Reddy, P.H.2
  • 25
    • 38049010515 scopus 로고    scopus 로고
    • Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer ' s disease
    • Lovell MA, Markesbery WR. Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer ' s disease. Nucleic Acids Res 2007;35:7497-7504.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7497-7504
    • Lovell, M.A.1    Markesbery, W.R.2
  • 27
    • 0004235430 scopus 로고    scopus 로고
    • Hoboken, NJ: John Wiley & Sons, Inc.
    • Scheffl er IE. Mitochondria. Hoboken, NJ: John Wiley & Sons, Inc.; 2008.
    • (2008) Mitochondria
    • Scheffler, I.E.1
  • 29
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979;59:527-605. (Pubitemid 9236599)
    • (1979) Physiological Reviews , vol.59 , Issue.3 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 31
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009;417:1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 32
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • DOI 10.1113/jphysiol.2003.049478
    • Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol 2003;552:335-344. (Pubitemid 37321833)
    • (2003) Journal of Physiology , vol.552 , Issue.2 , pp. 335-344
    • Turrens, J.F.1
  • 33
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • DOI 10.1074/jbc.M210269200
    • Han D, Antunes F, Canali R, Rettori D, Cadenas E. Voltagedependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J Biol Chem 2003;278:5557-5563. (Pubitemid 36800797)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 34
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • DOI 10.1074/jbc.M407715200
    • Muller FL, Liu Y, Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem 2004;279:49064-49073. (Pubitemid 39625788)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 35
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: A dawn for evolutionary medicine
    • DOI 10.1146/annurev.genet.39.110304.095751
    • Wallace DC. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu Rev Genet 2005;39:359-407. (Pubitemid 43011120)
    • (2005) Annual Review of Genetics , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 36
    • 0842328003 scopus 로고    scopus 로고
    • Prevention of Mitochondrial Oxidative Damage As A Therapeutic Strategy in Diabetes
    • Green K, Brand MD, Murphy MP. Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes. Diabetes 2004;53(Suppl 1):S110-S118. (Pubitemid 38168702)
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Green, K.1    Brand, M.D.2    Murphy, M.P.3
  • 37
    • 77956186783 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
    • Hamanaka RB, Chandel NS. Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes. Trends Biochem Sci 2010;35:505-513.
    • (2010) Trends Biochem Sci , vol.35 , pp. 505-513
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 38
    • 54049138387 scopus 로고    scopus 로고
    • Mechanisms of neuronal death in disease: Defi ning the models and the players
    • Ribe EM, Serrano-Saiz E, Akpan N, Troy CM. Mechanisms of neuronal death in disease: defi ning the models and the players. Biochem J 2008;415:165-182.
    • (2008) Biochem J , vol.415 , pp. 165-182
    • Ribe, E.M.1    Serrano-Saiz, E.2    Akpan, N.3    Troy, C.M.4
  • 41
    • 69249211284 scopus 로고    scopus 로고
    • Mitochondrial dysfunction: An early event in Alzheimer pathology accumulates with age in AD transgenic mice
    • Hauptmann S, Scherping I, Drose S, Brandt U, Schulz KL, Jendrach M, et al. Mitochondrial dysfunction: an early event in Alzheimer pathology accumulates with age in AD transgenic mice. Neurobiol Aging 2009;30:1574-1586.
    • (2009) Neurobiol Aging , vol.30 , pp. 1574-1586
    • Hauptmann, S.1    Scherping, I.2    Drose, S.3    Brandt, U.4    Schulz, K.L.5    Jendrach, M.6
  • 42
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic defi cit precedes Alzheimer ' s pathology in female mouse model of Alzheimer ' s disease
    • Yao J, Irwin RW, Zhao L, Nilsen J, Hamilton RT, Brinton RD. Mitochondrial bioenergetic defi cit precedes Alzheimer ' s pathology in female mouse model of Alzheimer ' s disease. Proc Nat Acad Sci USA 2009;106:14670-14675.
    • (2009) Proc Nat Acad Sci USA , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 43
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006;443: 787-795. (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 45
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pathogenesis of Alzheimer's disease?
    • DOI 10.1016/j.brainresrev.2005.03.004, PII S0165017305000470
    • Reddy PH, Beal MF. Are mitochondria critical in the pathogenesis of Alzheimer ' s disease? Brain Res Brain Res Rev 2005;49:618-632. (Pubitemid 41546661)
    • (2005) Brain Research Reviews , vol.49 , Issue.3 , pp. 618-632
    • Reddy, P.H.1    Beal, M.F.2
  • 46
    • 71749121998 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a trigger of Alzheimer ' s disease pathophysiology
    • Moreira PI, Carvalho C, Zhu X, Smith MA, Perry G. Mitochondrial dysfunction is a trigger of Alzheimer ' s disease pathophysiology. Biochim Biophys Acta 2010;1802:2-10.
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 2-10
    • Moreira, P.I.1    Carvalho, C.2    Zhu, X.3    Smith, M.A.4    Perry, G.5
  • 47
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • DOI 10.1016/S0197-4580(00)00112-3, PII S0197458000001123
    • Maurer I, Zierz S, Moller HJ. A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol Aging 2000;21:455-462. (Pubitemid 30349116)
    • (2000) Neurobiology of Aging , vol.21 , Issue.3 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Moller, H.-J.3
  • 48
    • 0033569839 scopus 로고    scopus 로고
    • Increased neuronal glucose-6-phosphate dehydrogenase and sulfhydryl levels indicate reductive compensation to oxidative stress in Alzheimer disease
    • DOI 10.1006/abbi.1999.1404
    • Russell RL, Siedlak SL, Raina AK, Bautista JM, Smith MA, Perry G. Increased neuronal glucose-6-phosphate dehydrogenase and sulfhydryl levels indicate reductive compensation to oxidative stress in Alzheimer disease. Arch Biochem Biophys 1999;370:236-239. (Pubitemid 29491430)
    • (1999) Archives of Biochemistry and Biophysics , vol.370 , Issue.2 , pp. 236-239
    • Russell, R.L.1    Siedlak, S.L.2    Raina, A.K.3    Bautista, J.M.4    Smith, M.A.5    Perry, G.6
  • 49
    • 0026408619 scopus 로고
    • Cytochrome oxidase defi ciency in Alzheimer' s disease
    • Parker WD Jr. Cytochrome oxidase defi ciency in Alzheimer' s disease. Ann NY Acad Sci 1991;640:59-64.
    • (1991) Ann NY Acad Sci , vol.640 , pp. 59-64
    • Parker Jr., W.D.1
  • 50
    • 73949088883 scopus 로고    scopus 로고
    • RAGE-mediated signaling contributes to intraneuronal transport of amyloid-beta and neuronal dysfunction
    • T akuma K, Fang F, Zhang W, Yan S, Fukuzaki E, Du H, et al. RAGE-mediated signaling contributes to intraneuronal transport of amyloid-beta and neuronal dysfunction. Proc Natl Acad Sci USA 2009;106:20021-20026.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20021-20026
    • Takuma, K.1    Fang, F.2    Zhang, W.3    Yan, S.4    Fukuzaki, E.5    Du, H.6
  • 51
    • 24744449326 scopus 로고    scopus 로고
    • Cerebrovascular damage as a cause for Alzheimer's disease
    • DOI 10.2174/156720205774322610
    • Humpel C, Marksteiner J. Cerebrovascular damage as a cause for Alzheimer ' s disease. Curr Neurovasc Res 2005;2: 341-347. (Pubitemid 41297371)
    • (2005) Current Neurovascular Research , vol.2 , Issue.4 , pp. 341-347
    • Humpel, C.1    Marksteiner, J.2
  • 53
    • 33751103136 scopus 로고    scopus 로고
    • Heme binding to Amyloid-β peptide: Mechanistic role in Alzheimer's disease
    • Atamna H. Heme binding to Amyloid-beta peptide: mechanistic role in Alzheimer ' s disease. J Alzheimers Dis 2006;10: 255-266. (Pubitemid 44763996)
    • (2006) Journal of Alzheimer's Disease , vol.10 , Issue.2-3 , pp. 255-266
    • Atamna, H.1
  • 56
    • 69949108391 scopus 로고    scopus 로고
    • Amyloid precursor protein, heat-shock proteins, and Bcl-2 form a complex in mitochondria and modulate mitochondria function and apoptosis in N2a cells
    • Yang TT, Hsu CT, Kuo YM. Amyloid precursor protein, heat-shock proteins, and Bcl-2 form a complex in mitochondria and modulate mitochondria function and apoptosis in N2a cells. Mech Ageing Dev 2009;130:592-601.
    • (2009) Mech Ageing Dev , vol.130 , pp. 592-601
    • Yang, T.T.1    Hsu, C.T.2    Kuo, Y.M.3
  • 59
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fi ssion/fusion proteins
    • Wang X, Su B, Siedlak SL, Moreira PI, Fujioka H, Wang Y, Casadesus G, Zhu X. Amyloid-beta overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fi ssion/fusion proteins. Proc Natl Acad Sci USA 2008;105:19318-19323.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 60
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fi ssion and fusion in Alzheimer ' s disease
    • Wang X, Su B, Lee HG, Li X, Perry G, Smith MA, Zhu X. Impaired balance of mitochondrial fi ssion and fusion in Alzheimer ' s disease. J Neurosci 2009;29:9090-9103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 61
    • 79958721260 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer ' s disease: Implications for neuronal damage
    • Manczak M, Calkins MJ, Reddy PH. Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer ' s disease: implications for neuronal damage. Hum Mol Genet 2011;20:2495-2509.
    • (2011) Hum Mol Genet , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 62
    • 81255190781 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer ' s disease
    • Calkins MJ, Manczak M, Mao P, Shirendeb U, Reddy PH. Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer ' s disease. Hum Mol Genet 2011;20:4515-4529.
    • (2011) Hum Mol Genet , vol.20 , pp. 4515-4529
    • Calkins, M.J.1    Manczak, M.2    Mao, P.3    Shirendeb, U.4    Reddy, P.H.5
  • 63
    • 84855687153 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer ' s disease
    • doi: 10.1111/j.1471-4159.2011.07581.x
    • Sheng B, Wang X, Su B, Lee HG, Casadesus G, Perry G, Zhu X. Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer ' s disease. J Neurochem 2011; doi: 10.1111/j.1471-4159.2011.07581.x.
    • (2011) J Neurochem
    • Sheng, B.1    Wang, X.2    Su, B.3    Lee, H.G.4    Casadesus, G.5    Perry, G.6    Zhu, X.7
  • 64
    • 79952785327 scopus 로고    scopus 로고
    • Metal ions Alzheimer' s disease and chelation therapy
    • Budimir A. Metal ions, Alzheimer' s disease and chelation therapy. Acta Pharm 2011;61:1-14.
    • (2011) Acta Pharm , vol.61 , pp. 1-14
    • Budimir, A.1
  • 66
    • 75149152568 scopus 로고    scopus 로고
    • Increased iron and free radical generation in preclinical Alzheimer disease and mild cognitive impairment
    • Smith MA, Zhu X, Tabaton M, Liu G, McKeel DW Jr, Cohen ML, et al. Increased iron and free radical generation in preclinical Alzheimer disease and mild cognitive impairment. J Alzheimers Dis 2010;19:363-372.
    • (2010) J Alzheimers Dis , vol.19 , pp. 363-372
    • Smith, M.A.1    Zhu, X.2    Tabaton, M.3    Liu, G.4    McKeel Jr., D.W.5    Cohen, M.L.6
  • 70
    • 79952996094 scopus 로고    scopus 로고
    • Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation
    • Liu B, Moloney A, Meehan S, Morris K, Thomas SE, Serpell LC, et al. Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation. J Biol Chem 2011;286:4248-4256.
    • (2011) J Biol Chem , vol.286 , pp. 4248-4256
    • Liu, B.1    Moloney, A.2    Meehan, S.3    Morris, K.4    Thomas, S.E.5    Serpell, L.C.6
  • 71
    • 79955927181 scopus 로고    scopus 로고
    • Aluminum, copper, iron and zinc differentially alter amyloid-Abeta(1-42) aggregation and toxicity
    • Bolognin S, Messori L, Drago D, Gabbiani C, Cendron L, Zatta P. Aluminum, copper, iron and zinc differentially alter amyloid-Abeta(1-42) aggregation and toxicity. Int J Biochem Cell Biol 2011;43:877-885.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 877-885
    • Bolognin, S.1    Messori, L.2    Drago, D.3    Gabbiani, C.4    Cendron, L.5    Zatta, P.6
  • 72
    • 79953225854 scopus 로고    scopus 로고
    • Distinct effects of Zn2, Cu2, Fe3, and Al3on amyloid-beta stability, oligomerization, and aggregation: Amyloid-beta destabilization promotes annular protofi bril formation
    • Chen WT, Liao YH, Yu HM, Cheng IH, Chen YR. Distinct effects of Zn2, Cu2, Fe3, and Al3on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofi bril formation. J Biol Chem 2011;286:9646-9656.
    • (2011) J Biol Chem , vol.286 , pp. 9646-9656
    • Chen, W.T.1    Liao, Y.H.2    Yu, H.M.3    Cheng, I.H.4    Chen, Y.R.5
  • 73
    • 79954642381 scopus 로고    scopus 로고
    • Advances in metal-induced oxidative stress and human disease
    • Jomova K, Valko M. Advances in metal-induced oxidative stress and human disease. Toxicology 2011;283:65-87.
    • (2011) Toxicology , vol.283 , pp. 65-87
    • Jomova, K.1    Valko, M.2
  • 74
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • DOI 10.1046/j.1471-4159.2000.0740270.x
    • Sayre LM, Perry G, Harris PL, Liu Y, Schubert KA, Smith MA. In situ oxidative catalysis by neurofi brillary tangles and senile plaques in Alzheimer ' s disease: a central role for bound transition metals. J Neurochem 2000;74:270-279. (Pubitemid 30012778)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.1 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.R.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 76
  • 77
    • 57449110125 scopus 로고    scopus 로고
    • NADPH oxidase as a therapeutic target in Alzheimer ' s disease
    • Block ML. NADPH oxidase as a therapeutic target in Alzheimer ' s disease. BMC Neurosci 2008;9(Suppl 2):S8.
    • (2008) BMC Neurosci , vol.9 , Issue.SUPPL. 2
    • Block, M.L.1
  • 79
    • 1042278903 scopus 로고    scopus 로고
    • NADPH oxidase
    • DOI 10.1016/j.coi.2003.12.001
    • Babior BM. NADPH oxidase. Curr Opin Immunol 2004;16:42-47. (Pubitemid 38198116)
    • (2004) Current Opinion in Immunology , vol.16 , Issue.1 , pp. 42-47
    • Babior, B.M.1
  • 81
    • 67651184281 scopus 로고    scopus 로고
    • NOX enzymes in the central nervous system: From signaling to disease
    • Sorce S, Krause KH. NOX enzymes in the central nervous system: from signaling to disease. Antioxid Redox Signal 2009;11:2481-2504.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2481-2504
    • Sorce, S.1    Krause, K.H.2
  • 82
    • 0030795049 scopus 로고    scopus 로고
    • β-amyloid protein enhances macrophage production of oxygen free radicals and glutamate
    • DOI 10.1002/(SICI)1097-4547(19970715)49:2<229::AID-JNR11>3.0.CO;2-W
    • Klegeris A, McGeer PL. Beta-amyloid protein enhances macrophage production of oxygen free radicals and glutamate. J Neurosci Res 1997;49:229-235. (Pubitemid 27332721)
    • (1997) Journal of Neuroscience Research , vol.49 , Issue.2 , pp. 229-235
    • Klegeris, A.1    McGeer, P.L.2
  • 84
    • 0029971210 scopus 로고    scopus 로고
    • Amyloid β protein primes cultured rat microglial cells for an enhanced phorbol 12-myristate 13-acetate-induced respiratory burst activity
    • Van Muiswinkel FL, Veerhuis R, Eikelenboom P. Amyloid beta protein primes cultured rat microglial cells for an enhanced phorbol 12-myristate 13-acetate-induced respiratory burst activity. J Neurochem 1996;66:2468-2476. (Pubitemid 26159083)
    • (1996) Journal of Neurochemistry , vol.66 , Issue.6 , pp. 2468-2476
    • Van Muiswinkel, F.L.1    Veerhuis, R.2    Eikelenboom, P.3
  • 87
    • 79957935719 scopus 로고    scopus 로고
    • NADPH-oxidase activation and cognition in Alzheimer disease progression
    • Ansari MA, Scheff SW. NADPH-oxidase activation and cognition in Alzheimer disease progression. Free Radic Biol Med 2011;51:171-178.
    • (2011) Free Radic Biol Med , vol.51 , pp. 171-178
    • Ansari, M.A.1    Scheff, S.W.2
  • 88
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer's disease
    • Iadecola C. Neurovascular regulation in the normal brain and in Alzheimer ' s disease. Nat Rev Neurosci 2004;5: 347-360. (Pubitemid 38568496)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.5 , pp. 347-360
    • Iadecola, C.1
  • 90
    • 14044258771 scopus 로고    scopus 로고
    • NADPH oxidase-derived reactive oxygen species mediate the cerebrovascular dysfunction induced by the amyloid β peptide
    • DOI 10.1523/JNEUROSCI.5207-04.2005
    • Park L, Anrather J, Zhou P, Frys K, Pitstick R, Younkin S, Carlson GA, Iadecola C. NADPH-oxidase-derived reactive oxygen species mediate the cerebrovascular dysfunction induced by the amyloid beta peptide. J Neurosci 2005;25: 1769-1777. (Pubitemid 40279282)
    • (2005) Journal of Neuroscience , vol.25 , Issue.7 , pp. 1769-1777
    • Park, L.1    Anrather, J.2    Zhou, P.3    Frys, K.4    Pitstick, R.5    Younkin, S.6    Carlson, G.A.7    Iadecola, C.8
  • 91
    • 77956207871 scopus 로고    scopus 로고
    • Mitochondria and antioxidant targeted therapeutic strategies for Alzheimer ' s disease
    • Dumont M, Lin MT, Beal MF. Mitochondria and antioxidant targeted therapeutic strategies for Alzheimer ' s disease. J Alzheimers Dis 2010;20(Suppl 2):S633-S643.
    • (2010) J Alzheimers Dis , vol.20 , Issue.SUPPL. 2
    • Dumont, M.1    Lin, M.T.2    Beal, M.F.3
  • 94
    • 33646922865 scopus 로고    scopus 로고
    • Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
    • DOI 10.1523/JNEUROSCI.0482-06.2006
    • Esposito L, Raber J, Kekonius L, Yan F, Yu GQ, Bien-Ly N, et al. Reduction in mitochondrial superoxide dismutase modulates Alzheimer ' s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice. J Neurosci 2006;26: 5167-5179. (Pubitemid 44315298)
    • (2006) Journal of Neuroscience , vol.26 , Issue.19 , pp. 5167-5179
    • Esposito, L.1    Raber, J.2    Kekonius, L.3    Yan, F.4    Yu, G.-Q.5    Bien-Ly, N.6    Puolivali, J.7    Scearce-Levie, K.8    Masliah, E.9    Mucke, L.10
  • 95
    • 68849110235 scopus 로고    scopus 로고
    • Reduction of oxidative stress, amyloid deposition, and memory defi cit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer ' s disease
    • Dumont M, Wille E, Stack C, Calingasan NY, Beal MF, Lin MT. Reduction of oxidative stress, amyloid deposition, and memory defi cit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer ' s disease. FASEB J 2009;23:2459-2466.
    • (2009) FASEB J , vol.23 , pp. 2459-2466
    • Dumont, M.1    Wille, E.2    Stack, C.3    Calingasan, N.Y.4    Beal, M.F.5    Lin, M.T.6
  • 96
    • 69449096141 scopus 로고    scopus 로고
    • Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory defi cits in a mouse model of Alzheimer ' s disease
    • Massaad CA, Washington TM, Pautler RG, Klann E. Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory defi cits in a mouse model of Alzheimer ' s disease. Proc Natl Acad Sci USA 2009;106:13576-13581.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13576-13581
    • Massaad, C.A.1    Washington, T.M.2    Pautler, R.G.3    Klann, E.4
  • 98
    • 19444377184 scopus 로고    scopus 로고
    • Oxidative imbalance and cathepsin D changes as peripheral blood biomarkers of Alzheimer disease: A pilot study
    • DOI 10.1016/j.febslet.2005.03.094, PII S0014579305004655
    • Straface E, Matarrese P, Gambardella L, Vona R, Sgadari A, Silveri MC, Malorni W. Oxidative imbalance and cathepsin D changes as peripheral blood biomarkers of Alzheimer disease: a pilot study. FEBS Lett 2005;579:2759-2766. (Pubitemid 40725242)
    • (2005) FEBS Letters , vol.579 , Issue.13 , pp. 2759-2766
    • Straface, E.1    Matarrese, P.2    Gambardella, L.3    Vona, R.4    Sgadari, A.5    Silveri, M.C.6    Malorni, W.7
  • 100
    • 78649820608 scopus 로고    scopus 로고
    • Inhibitors of catalase-amyloid interactions protect cells from beta-amyloid-induced oxidative stress and toxicity
    • Habib LK, Lee MT, Yang J. Inhibitors of catalase-amyloid interactions protect cells from beta-amyloid-induced oxidative stress and toxicity. J Biol Chem 2010;285: 38933-38943.
    • (2010) J Biol Chem , vol.285 , pp. 38933-38943
    • Habib, L.K.1    Lee, M.T.2    Yang, J.3
  • 101
  • 102
    • 33846995116 scopus 로고    scopus 로고
    • Up-regulation of plasma membraneassociated redox activities in neuronal cells lacking functional mitochondria
    • Hyun DH, Hunt ND, Emerson SS, Hernandez JO, Mattson MP, de Cabo R. Up-regulation of plasma membraneassociated redox activities in neuronal cells lacking functional mitochondria. J Neurochem 2007;100:1364-1374.
    • (2007) J Neurochem , vol.100 , pp. 1364-1374
    • Hyun, D.H.1    Hunt, N.D.2    Emerson, S.S.3    Hernandez, J.O.4    Mattson, M.P.5    De Cabo, R.6
  • 103
    • 34248195909 scopus 로고    scopus 로고
    • The importance of plasma membrane coenzyme Q in aging and stress responses
    • DOI 10.1016/j.mito.2007.02.010, PII S1567724907000554, The Roled of Coenzyme Q in Cellular Metabolism: Current Biological and Clinical Aspects
    • Navas P, Villalba JM, de Cabo R. The importance of plasma membrane coenzyme Q in aging and stress responses. Mitochondrion 2007;7(Suppl):S34-40. (Pubitemid 46722290)
    • (2007) Mitochondrion , vol.7 , Issue.SUPPL.
    • Navas, P.1    Villalba, J.M.2    De Cabo, R.3
  • 105
    • 0033920064 scopus 로고    scopus 로고
    • Plasma membrane redox system in the control of stress-induced apoptosis
    • Villalba JM, Navas P. Plasma membrane redox system in the control of stress-induced apoptosis. Antioxid Redox Signal 2000;2:213-230. (Pubitemid 30445934)
    • (2000) Antioxidants and Redox Signaling , vol.2 , Issue.2 , pp. 213-230
    • Villalba, J.M.1    Navas, P.2
  • 106
    • 77956430510 scopus 로고    scopus 로고
    • The plasma membrane redox system is impaired by amyloid beta-peptide and in the hippocampus and cerebral cortex of 3xTgAD mice
    • Hyun DH, Mughal MR, Yang H, Lee JH, Ko EJ, Hunt ND, de Cabo R, Mattson MP. The plasma membrane redox system is impaired by amyloid beta-peptide and in the hippocampus and cerebral cortex of 3xTgAD mice. Exp Neurol 2010;225:423-429.
    • (2010) Exp Neurol , vol.225 , pp. 423-429
    • Hyun, D.H.1    Mughal, M.R.2    Yang, H.3    Lee, J.H.4    Ko, E.J.5    Hunt, N.D.6    De Cabo, R.7    Mattson, M.P.8
  • 108
    • 70450246963 scopus 로고    scopus 로고
    • Depletion of vitamin e increases amyloid beta accumulation by decreasing its clearances from brain and blood in a mouse model of Alzheimer disease
    • Nishida Y, Ito S, Ohtsuki S, Yamamoto N, Takahashi T, Iwata N, et al. Depletion of vitamin E increases amyloid beta accumulation by decreasing its clearances from brain and blood in a mouse model of Alzheimer disease. J Biol Chem 2009; 284:33400-33408.
    • (2009) J Biol Chem , vol.284 , pp. 33400-33408
    • Nishida, Y.1    Ito, S.2    Ohtsuki, S.3    Yamamoto, N.4    Takahashi, T.5    Iwata, N.6
  • 110
    • 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
    • DOI 10.1080/10715760701861373, PII 790807039
    • Bermejo P, Martin-Aragon S, Benedi J, Susin C, Felici E, Gil P, Ribera JM, Villar AM. Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer ' s disease from mild cognitive impairment. Free Radic Res 2008;42:162-170. (Pubitemid 351298365)
    • (2008) Free Radical Research , vol.42 , Issue.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.Ma.8
  • 112
    • 0037361527 scopus 로고    scopus 로고
    • Glutathione cycle impairment mediates Aβ-induced cell toxicity
    • DOI 10.1080/1071576021000041023
    • Cardoso SM, Oliveira CR. Glutathione cycle impairment mediates A beta-induced cell toxicity. Free Radic Res 2003;37:241-250. (Pubitemid 36181880)
    • (2003) Free Radical Research , vol.37 , Issue.3 , pp. 241-250
    • Cardoso, S.M.1    Oliveira, C.R.2
  • 113
    • 79957456954 scopus 로고    scopus 로고
    • Base excision repair and lesion-dependent subpathways for repair of oxidative DNA damage
    • Svilar D, Goellner EM, Almeida KH, Sobol RW. Base excision repair and lesion-dependent subpathways for repair of oxidative DNA damage. Antioxid Redox Signal 2011;14: 2491-2507.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2491-2507
    • Svilar, D.1    Goellner, E.M.2    Almeida, K.H.3    Sobol, R.W.4
  • 114
    • 0025098737 scopus 로고
    • A cysteine-specifi c lysosomal transport system provides a major route for the delivery of thiol to human fi broblast lysosomes: Possible role in supporting lysosomal proteolysis
    • Pisoni RL, Acker TL, Lisowski KM, Lemons RM, Thoene JG. A cysteine-specifi c lysosomal transport system provides a major route for the delivery of thiol to human fi broblast lysosomes: possible role in supporting lysosomal proteolysis. J Cell Biol 1990;110:327-335.
    • (1990) J Cell Biol , vol.110 , pp. 327-335
    • Pisoni, R.L.1    Acker, T.L.2    Lisowski, K.M.3    Lemons, R.M.4    Thoene, J.G.5
  • 115
    • 0014878377 scopus 로고
    • Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver
    • Brun A, Brunk U. Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver. J Histochem Cytochem 1970;18:820-827.
    • (1970) J Histochem Cytochem , vol.18 , pp. 820-827
    • Brun, A.1    Brunk, U.2
  • 116
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cells
    • DOI 10.1042/0264-6021:3560061
    • Petrat F, de Groot H, Rauen U. Subcellular distribution of chelatable iron: a laser scanning microscopic study in isolated hepatocytes and liver endothelial cells. Biochem J 2001;356:61-69. (Pubitemid 34275706)
    • (2001) Biochemical Journal , vol.356 , Issue.1 , pp. 61-69
    • Petrat, F.1    De Groot, H.2    Rauen, U.3
  • 117
    • 0034656371 scopus 로고    scopus 로고
    • Acidic pH amplifies iron-mediated lipid peroxidation in cells
    • DOI 10.1016/S0891-5849(00)00319-1, PII S0891584900003191
    • Schafer FQ, Buettner GR. Acidic pH amplifi es ironmediated lipid peroxidation in cells. Free Radic Biol Med 2000;28:1175-1181. (Pubitemid 30417459)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.8 , pp. 1175-1181
    • Schafer, F.Q.1    Buettner, G.R.2
  • 118
    • 18844425714 scopus 로고    scopus 로고
    • Role of compartmentalized redox-active iron in hydrogen peroxide-induced DNA damage and apoptosis
    • DOI 10.1042/BJ20041650
    • Tenopoulou M, Doulias PT, Barbouti A, Brunk U, Galaris D. Role of compartmentalized redox-active iron in hydrogen peroxide-induced DNA damage and apoptosis. Biochem J 2005;387:703-710. (Pubitemid 40685704)
    • (2005) Biochemical Journal , vol.387 , Issue.3 , pp. 703-710
    • Tenopoulou, M.1    Doulias, P.-T.2    Barbouti, A.3    Brunk, U.4    Galaris, D.5
  • 119
    • 1642463971 scopus 로고    scopus 로고
    • Relocalized redox-active lysosomal iron is an important mediator of oxidative-stress-induced DNA damage
    • DOI 10.1042/BJ20031029
    • Kurz T, Leake A, Von Zglinicki T, Brunk UT. Relocalized redox-active lysosomal iron is an important mediator of oxidative-stress-induced DNA damage. Biochem J 2004;378: 1039-1045. (Pubitemid 38406883)
    • (2004) Biochemical Journal , vol.378 , Issue.3 , pp. 1039-1045
    • Kurz, T.1    Leake, A.2    Von Zglinicki, T.3    Brunk, U.T.4
  • 120
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Aβ-mediated cell death in Alzheimer's disease
    • DOI 10.1006/nbdi.2000.0364
    • Ditaranto K, Tekirian TL, Yang AJ. Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer ' s disease. Neurobiol Dis 2001;8:19-31. (Pubitemid 32171815)
    • (2001) Neurobiology of Disease , vol.8 , Issue.1 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 121
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Aβ1-42 pathogenesis
    • DOI 10.1002/(SICI)1097-4547(19980615)52:6<691::AID-JNR8>3.0.CO;2-3
    • Yang AJ, Chandswangbhuvana D, Margol L, Glabe CG. Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta1-42 pathogenesis. J Neurosci Res 1998;52:691-698. (Pubitemid 28300049)
    • (1998) Journal of Neuroscience Research , vol.52 , Issue.6 , pp. 691-698
    • Yang, A.J.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.G.4
  • 123
    • 56349129570 scopus 로고    scopus 로고
    • Formamidopyrimidines in DNA: Mechanisms of formation, repair, and biological effects
    • Dizdaroglu M, Kirkali G, Jaruga P. Formamidopyrimidines in DNA: mechanisms of formation, repair, and biological effects. Free Radic Biol Med 2008;45:1610-1621.
    • (2008) Free Radic Biol Med , vol.45 , pp. 1610-1621
    • Dizdaroglu, M.1    Kirkali, G.2    Jaruga, P.3
  • 124
    • 0021769722 scopus 로고
    • Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents
    • Kasai H, Nishimura S. Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents. Nucleic Acids Res 1984;12:2137-2145.
    • (1984) Nucleic Acids Res , vol.12 , pp. 2137-2145
    • Kasai, H.1    Nishimura, S.2
  • 125
    • 0036948404 scopus 로고    scopus 로고
    • Origins of spontaneous mutations: Specifi city and directionality of base-substitution, frameshift, and sequencesubstitution mutageneses
    • Maki H. Origins of spontaneous mutations: specifi city and directionality of base-substitution, frameshift, and sequencesubstitution mutageneses. Annu Rev Genet 2002;36: 279-303.
    • (2002) Annu Rev Genet , vol.36 , pp. 279-303
    • Maki, H.1
  • 126
    • 0023898319 scopus 로고
    • Ring-opened 7-methylguanine residues in DNA are a block to in vitro DNA synthesis
    • O' C onnor TR, Boiteux S, Laval J. Ring-opened 7-methylguanine residues in DNA are a block to in vitro DNA synthesis. Nucleic Acids Res 1988;16:5879-5894.
    • (1988) Nucleic Acids Res , vol.16 , pp. 5879-5894
    • O'Connor, T.R.1    Boiteux, S.2    Laval, J.3
  • 128
    • 33646080824 scopus 로고    scopus 로고
    • Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products
    • Neeley WL, Essigmann JM. Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products. Chem Res Toxicol 2006;19:491-505.
    • (2006) Chem Res Toxicol , vol.19 , pp. 491-505
    • Neeley, W.L.1    Essigmann, J.M.2
  • 129
    • 7944222565 scopus 로고    scopus 로고
    • Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2
    • DOI 10.1016/j.dnarep.2004.07.006, PII S1568786404002186
    • Hailer MK, Slade PG, Martin BD, Rosenquist TA, Sugden KD. Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2. DNA Repair (Amst) 2005;4:41-50. (Pubitemid 39469081)
    • (2005) DNA Repair , vol.4 , Issue.1 , pp. 41-50
    • Hailer, M.K.1    Slade, P.G.2    Martin, B.D.3    Rosenquist, T.A.4    Sugden, K.D.5
  • 130
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • DOI 10.1096/fj.02-0752rev
    • Cooke MS, Evans MD, Dizdaroglu M, Lunec J. Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 2003;17:1195-1214. (Pubitemid 36775767)
    • (2003) FASEB Journal , vol.17 , Issue.10 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 131
    • 33748366270 scopus 로고
    • Purine bases, nucleosides, and nucleotides: Aqueous solution redox chemistry and transformation reactions of their radical cations and e-and OH adducts
    • Steenken S. Purine bases, nucleosides, and nucleotides: aqueous solution redox chemistry and transformation reactions of their radical cations and e-and OH adducts. Chem Rev 1989;89:503-520.
    • (1989) Chem Rev , vol.89 , pp. 503-520
    • Steenken, S.1
  • 132
    • 27844495699 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage by DNA glycosylases
    • DOI 10.1016/j.mrfmmm.2005.01.033, PII S0027510705002782, Mechanistic Approaches to Chemoprevention of Mutation and Cancer
    • Dizdaroglu M. Base-excision repair of oxidative DNA damage by DNA glycosylases. Mutat Res 2005;591:45-59. (Pubitemid 41654839)
    • (2005) Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis , vol.591 , Issue.1-2 , pp. 45-59
    • Dizdaroglu, M.1
  • 133
    • 34247156564 scopus 로고    scopus 로고
    • DNA repair, mitochondria, and neurodegeneration
    • DOI 10.1016/j.neuroscience.2006.08.061, PII S0306452206011730, Genome Dynamics and DNA Repair in the CNS
    • Weissman L, de Souza-Pinto NC, Stevnsner T, Bohr VA. DNA repair, mitochondria, and neurodegeneration. Neuroscience 2007;145:1318-1329. (Pubitemid 46602727)
    • (2007) Neuroscience , vol.145 , Issue.4 , pp. 1318-1329
    • Weissman, L.1    De Souza-Pinto, N.C.2    Stevnsner, T.3    Bohr, V.A.4
  • 135
    • 0042342532 scopus 로고    scopus 로고
    • A mechanistic perspective on the chemistry of DNA repair glycosylases
    • Stivers JT, Jiang YL. A mechanistic perspective on the chemistry of DNA repair glycosylases. Chem Rev 2003;103: 2729-2759.
    • (2003) Chem Rev , vol.103 , pp. 2729-2759
    • Stivers, J.T.1    Jiang, Y.L.2
  • 136
    • 0037112668 scopus 로고    scopus 로고
    • Human DNA glycosylases of the bacterial Fpg/MutM superfamily: An alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA
    • Morland I, Rolseth V, Luna L, Rognes T, Bjoras M, Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res 2002;30:4926-4936. (Pubitemid 35414653)
    • (2002) Nucleic Acids Research , vol.30 , Issue.22 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjoras, M.5    Seeberg, E.6
  • 138
    • 7444266619 scopus 로고    scopus 로고
    • Human DNA glycosylases involved in the repair of oxidatively damaged DNA
    • DOI 10.1248/bpb.27.480
    • Ide H, Kotera M. Human DNA glycosylases involved in the repair of oxidatively damaged DNA. Biol Pharm Bull 2004;27:480-485. (Pubitemid 41701830)
    • (2004) Biological and Pharmaceutical Bulletin , vol.27 , Issue.4 , pp. 480-485
    • Ide, H.1    Kotera, M.2
  • 139
    • 0033539610 scopus 로고    scopus 로고
    • Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage
    • Klungland A, Rosewell I, Hollenbach S, Larsen E, Daly G, Epe B, et al. Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage. Proc Natl Acad Sci USA 1999;96:13300-13305.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13300-13305
    • Klungland, A.1    Rosewell, I.2    Hollenbach, S.3    Larsen, E.4    Daly, G.5    Epe, B.6
  • 140
    • 0035878869 scopus 로고    scopus 로고
    • Repair of 8-oxodeoxyguanosine lesions in mitochondrial DNA depends on the oxoguanine DNA glycosylase (OGG1) gene and 8-oxoguanine accumulates in the mitochondrial DNA of OGG1-defective mice
    • de Souza-Pinto NC, Eide L, Hogue BA, Thybo T, Stevnsner T, Seeberg E, Klungland A, Bohr VA. Repair of 8-oxodeoxyguanosine lesions in mitochondrial dna depends on the oxoguanine dna glycosylase (OGG1) gene and 8-oxoguanine accumulates in the mitochondrial dna of OGG1-defective mice. Cancer Res 2001;61:5378-5381. (Pubitemid 32694914)
    • (2001) Cancer Research , vol.61 , Issue.14 , pp. 5378-5381
    • De Souza-Pinto, N.C.1    Eide, L.2    Hogue, B.A.3    Thybo, T.4    Stevnsner, T.5    Seeberg, E.6    Klungland, A.7    Bohr, V.A.8
  • 141
    • 27844501168 scopus 로고    scopus 로고
    • Molecular and biological roles of Ape1 protein in mammalian base excision repair
    • DOI 10.1016/j.dnarep.2005.09.004, PII S1568786405002557
    • Demple B, Sung JS. Molecular and biological roles of Ape1 protein in mammalian base excision repair. DNA Repair (Amst) 2005;4:1442-1449. (Pubitemid 41653305)
    • (2005) DNA Repair , vol.4 , Issue.12 , pp. 1442-1449
    • Demple, B.1    Sung, J.-S.2
  • 142
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA
    • DOI 10.1016/S0921-8777(01)00063-5, PII S0921877701000635
    • Wilson DM 3rd, Barsky D. The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA. Mutat Res 2001;485:283-307. (Pubitemid 32406284)
    • (2001) Mutation Research - DNA Repair , vol.485 , Issue.4 , pp. 283-307
    • Wilson III, D.M.1    Barsky, D.2
  • 143
    • 0036570012 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells
    • DOI 10.1016/S0891-5849(02)00787-6, PII S0891584902007876
    • Bohr VA. Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells. Free Radic Biol Med 2002;32:804-812. (Pubitemid 34439251)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 804-812
    • Bohr, V.A.1
  • 144
    • 0019423856 scopus 로고
    • Sequence and organization of the human mitochondrial genome
    • DOI 10.1038/290457a0
    • Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, et al. Sequence and organization of the human mitochondrial genome. Nature 1981;290:457-465. (Pubitemid 11159074)
    • (1981) Nature , vol.290 , Issue.5806 , pp. 457-465
    • Anderson, S.1    Bankier, A.T.2    Barrell, B.G.3
  • 145
    • 65349123514 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
    • Stowe DF, Camara AK. Mitochondrial reactive oxygen species production in excitable cells: modulators of mitochondrial and cell function. Antioxid Redox Signal 2009;11: 1373-1414.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1373-1414
    • Stowe, D.F.1    Camara, A.K.2
  • 146
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • DOI 10.1073/pnas.94.2.514
    • Yakes FM, Van Houten B. Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc Natl Acad Sci USA 1997;94:514-519. (Pubitemid 27053665)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.2 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2
  • 147
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • DOI 10.1093/nar/25.4.750
    • Nilsen H, Otterlei M, Haug T, Solum K, Nagelhus TA, Skorpen F, Krokan HE. Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res 1997;25:750-755. (Pubitemid 27299828)
    • (1997) Nucleic Acids Research , vol.25 , Issue.4 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 148
    • 0032945268 scopus 로고    scopus 로고
    • Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs
    • Nishioka K, Ohtsubo T, Oda H, Fujiwara T, Kang D, Sugimachi K, Nakabeppu Y. Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs. Mol Biol Cell 1999;10:1637-1652. (Pubitemid 29230914)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.5 , pp. 1637-1652
    • Nishioka, K.1    Ohtsubo, T.2    Oda, H.3    Fujiwara, T.4    Kang, D.5    Sugimachi, K.6    Nakabeppu, Y.7
  • 151
    • 0028007266 scopus 로고
    • Expression of a multifunctional DNA repair enzyme gene, apurinic/apyrimidinic endonuclease (APE; Ref-1) in the suprachiasmatic, supraoptic and paraventricular nuclei
    • DOI 10.1016/0006-8993(94)90296-8
    • Rivkees SA, Kelley MR. Expression of a multifunctional DNA repair enzyme gene, apurinic/apyrimidinic endonuclease (APE; Ref-1) in the suprachiasmatic, supraoptic and paraventricular nuclei. Brain Res 1994;666:137-142. (Pubitemid 24359666)
    • (1994) Brain Research , vol.666 , Issue.1 , pp. 137-142
    • Rivkees, S.A.1    Kelley, M.R.2
  • 152
    • 0030004546 scopus 로고    scopus 로고
    • Differential expression of the apurinic/apyrimidinic endonuclease (APE/ref-1) multifunctional DNA base excision repair gene during fetal development and in adult rat brain and testis
    • DOI 10.1016/0921-8777(95)00053-4
    • Wilson TM, Rivkees SA, Deutsch WA, Kelley MR. Differential expression of the apurinic/apyrimidinic endonuclease (APE/ref-1) multifunctional DNA base excision repair gene during fetal development and in adult rat brain and testis. Mutat Res 1996;362:237-248. (Pubitemid 26102977)
    • (1996) Mutation Research - DNA Repair , vol.362 , Issue.3 , pp. 237-248
    • Wilson, T.M.1    Rivkees, S.A.2    Deutsch, W.A.3    Kelley, M.R.4
  • 153
    • 0034667766 scopus 로고    scopus 로고
    • Mitochondrial DNA ligase III function is independent of Xrcc1
    • Lakshmipathy U, Campbell C. Mitochondrial DNA ligase III function is independent of Xrcc1. Nucleic Acids Res 2000;28:3880-3886.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3880-3886
    • Lakshmipathy, U.1    Campbell, C.2
  • 154
    • 0032960864 scopus 로고    scopus 로고
    • The human DNA ligase III gene encodes nuclear and mitochondrial proteins
    • Lakshmipathy U, Campbell C. The human DNA ligase III gene encodes nuclear and mitochondrial proteins. Mol Cell Biol 1999;19:3869-3876. (Pubitemid 29193846)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.5 , pp. 3869-3876
    • Lakshmipathy, U.1    Campbell, C.2
  • 155
    • 29244433031 scopus 로고    scopus 로고
    • Mitochondrial DNA integrity is not dependent on DNA polymerase-β activity
    • DOI 10.1016/j.dnarep.2005.07.009, PII S1568786405002004
    • Hansen AB, Griner NB, Anderson JP, Kujoth GC, Prolla TA, Loeb LA, Glick E. Mitochondrial DNA integrity is not dependent on DNA polymerase-beta activity. DNA Repair (Amst) 2006;5:71-79. (Pubitemid 41832513)
    • (2006) DNA Repair , vol.5 , Issue.1 , pp. 71-79
    • Hansen, A.B.1    Griner, N.B.2    Anderson, J.P.3    Kujoth, G.C.4    Prolla, T.A.5    Loeb, L.A.6    Glick, E.7
  • 156
    • 2342429459 scopus 로고    scopus 로고
    • DNA polymerase γ, the mitochondrial replicase
    • DOI 10.1146/annurev.biochem.72.121801.161455
    • Kaguni LS. DNA polymerase gamma, the mitochondrial replicase. Annu Rev Biochem 2004;73:293-320. (Pubitemid 39050371)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 293-320
    • Kaguni, L.S.1
  • 159
    • 33744912521 scopus 로고    scopus 로고
    • Mitochondrial and nuclear DNA-repair capacity of various brain regions in mouse is altered in an age-dependent manner
    • DOI 10.1016/j.neurobiolaging.2005.06.002, PII S0197458005001739
    • Imam SZ, Karahalil B, Hogue BA, Souza-Pinto NC, Bohr VA. Mitochondrial and nuclear DNA-repair capacity of various brain regions in mouse is altered in an agedependent manner. Neurobiol Aging 2006;27:1129-1136. (Pubitemid 43850641)
    • (2006) Neurobiology of Aging , vol.27 , Issue.8 , pp. 1129-1136
    • Imam, S.Z.1    Karahalil, B.2    Hogue, B.A.3    Souza-Pinto, N.C.4    Bohr, V.A.5
  • 160
    • 0036316413 scopus 로고    scopus 로고
    • Age-dependent decline of DNA repair activity for oxidative lesions in rat brain mitochondria
    • DOI 10.1046/j.1471-4159.2002.00916.x
    • Chen D, Cao G, Hastings T, Feng Y, Pei W, O' H oro C, Chen J. Age-dependent decline of DNA repair activity for oxidative lesions in rat brain mitochondria. J Neurochem 2002;81: 1273-1284. (Pubitemid 34809261)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.6 , pp. 1273-1284
    • Chen, D.1    Cao, G.2    Hastings, T.3    Feng, Y.4    Pei, W.5    O'Horo, C.6    Chen, J.7
  • 161
    • 8344257204 scopus 로고    scopus 로고
    • Age-dependent modulation of DNA repair enzymes by covalent modification and subcellular distribution
    • DOI 10.1016/j.mad.2004.07.005, PII S0047637404001666
    • Szczesny B, Bhakat KK, Mitra S, Boldogh I. Age-dependent modulation of DNA repair enzymes by covalent modifi cation and subcellular distribution. Mech Ageing Dev 2004;125:755-765. (Pubitemid 39482404)
    • (2004) Mechanisms of Ageing and Development , vol.125 , Issue.SPEC. ISS. , pp. 755-765
    • Szczesny, B.1    Bhakat, K.K.2    Mitra, S.3    Boldogh, I.4
  • 162
    • 77956545422 scopus 로고    scopus 로고
    • Specifi c Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: Potential etiological linkage to neurodegenerative diseases
    • Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S. Specifi c Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem 2010;285:28812-28825.
    • (2010) J Biol Chem , vol.285 , pp. 28812-28825
    • Hegde, M.L.1    Hegde, P.M.2    Holthauzen, L.M.3    Hazra, T.K.4    Rao, K.S.5    Mitra, S.6
  • 165
    • 58649099395 scopus 로고    scopus 로고
    • Age-associated oxidative damage to the p62 promoter: Implications for Alzheimer disease
    • Du Y, Wooten MC, Gearing M, Wooten MW. Age-associated oxidative damage to the p62 promoter: implications for Alzheimer disease. Free Radic Biol Med 2009;46:492-501.
    • (2009) Free Radic Biol Med , vol.46 , pp. 492-501
    • Du, Y.1    Wooten, M.C.2    Gearing, M.3    Wooten, M.W.4
  • 166
    • 2442585133 scopus 로고    scopus 로고
    • Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: Possible mechanisms and the role in Lewy body formation in Parkinson's disease
    • DOI 10.1016/j.brainres.2004.03.029, PII S0006899304004743
    • Nakaso K, Yoshimoto Y, Nakano T, Takeshima T, Fukuhara Y, Yasui K, et al. Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson ' s disease. Brain Res 2004;1012:42-51. (Pubitemid 38648897)
    • (2004) Brain Research , vol.1012 , Issue.1-2 , pp. 42-51
    • Nakaso, K.1    Yoshimoto, Y.2    Nakano, T.3    Takeshima, T.4    Fukuhara, Y.5    Yasui, K.6    Araga, S.7    Yanagawa, T.8    Ishii, T.9    Nakashima, K.10
  • 168
    • 34548802393 scopus 로고    scopus 로고
    • Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment
    • DOI 10.1093/nar/gkm605
    • Weissman L, Jo DG, Sorensen MM, de Souza-Pinto NC, Markesbery WR, Mattson MP, Bohr VA. Defective DNA base excision repair in brain from individuals with Alzheimer ' s disease and amnestic mild cognitive impairment. Nucleic Acids Res 2007;35:5545-5555. (Pubitemid 47423927)
    • (2007) Nucleic Acids Research , vol.35 , Issue.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
  • 169
    • 79960452243 scopus 로고    scopus 로고
    • Expression of 8-oxoguanine DNA glycosylase 1 (OGG1) and the level of p53 and TNFalphalpha proteins in peripheral lymphocytes of patients with Alzheimer ' s disease
    • Dezor M, Dorszewska J, Florczak J, Kempisty B, Jaroszewska-Kolecka J, Rozycka A, et al. Expression of 8-oxoguanine DNA glycosylase 1 (OGG1) and the level of p53 and TNFalphalpha proteins in peripheral lymphocytes of patients with Alzheimer ' s disease. Folia Neuropathol 2011;49: 123-131.
    • (2011) Folia Neuropathol , vol.49 , pp. 123-131
    • Dezor, M.1    Dorszewska, J.2    Florczak, J.3    Kempisty, B.4    Jaroszewska-Kolecka, J.5    Rozycka, A.6
  • 170
    • 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 GM, Gu L, Mao G, Markesbery WR, Lovell MA. Altered 8-oxoguanine glycosylase in mild cognitive impairment and late-stage Alzheimer ' s disease brain. Free Radic Biol Med 2008;45:813-819.
    • (2008) Free Radic Biol Med , vol.45 , 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
  • 171
    • 70349852936 scopus 로고    scopus 로고
    • DNA base excision repair activities in mouse models of Alzheimer ' s disease
    • Weissman L, de Souza-Pinto NC, Mattson MP, Bohr VA. DNA base excision repair activities in mouse models of Alzheimer ' s disease. Neurobiol Aging 2009;30:2080-2081.
    • (2009) Neurobiol Aging , vol.30 , pp. 2080-2081
    • Weissman, L.1    De Souza-Pinto, N.C.2    Mattson, M.P.3    Bohr, V.A.4
  • 172
    • 79551536942 scopus 로고    scopus 로고
    • Mitochondrial base excision repair in mouse synaptosomes during normal aging and in a model of Alzheimer ' s disease
    • doi:10.1016/j.neurobiolaging.2010. 1006.1019
    • Gredilla R, Weissman L, Yang JL, Bohr VA, Stevnsner T. Mitochondrial base excision repair in mouse synaptosomes during normal aging and in a model of Alzheimer ' s disease. Neurobiol Aging 2010; doi:10.1016/j.neurobiolaging.2010. 1006.1019.
    • (2010) Neurobiol Aging
    • Gredilla, R.1    Weissman, L.2    Yang, J.L.3    Bohr, V.A.4    Stevnsner, T.5
  • 173
    • 4544225426 scopus 로고    scopus 로고
    • Detection of oxidative DNA damage in lymphocytes of patients with Alzheimer's disease
    • DOI 10.1080/13547500410001728390
    • Kadioglu E, Sardas S, Aslan S, Isik E, Esat Karakaya A. Detection of oxidative DNA damage in lymphocytes of patients with Alzheimer ' s disease. Biomarkers 2004;9: 203-209. (Pubitemid 39255641)
    • (2004) Biomarkers , vol.9 , Issue.2 , pp. 203-209
    • Kadioglu, E.1    Sardas, S.2    Aslan, S.3    Isik, E.4    Karakaya, A.E.5
  • 175
    • 0036141861 scopus 로고    scopus 로고
    • Elevated levels of oxidative DNA damage in lymphocytes from patients with Alzheimer's disease
    • DOI 10.1016/S0197-4580(01)00257-3, PII S0197458001002573
    • Morocz M, Kalman J, Juhasz A, Sinko I, McGlynn AP, Downes CS, Janka Z, Rasko I. Elevated levels of oxidative DNA damage in lymphocytes from patients with Alzheimer ' s disease. Neurobiol Aging 2002;23:47-53. (Pubitemid 34070637)
    • (2002) Neurobiology of Aging , vol.23 , Issue.1 , pp. 47-53
    • Morocz, M.1    Kalman, J.2    Juhasz, A.3    Sinko, I.4    McGlynn, A.P.5    Downes C.Stephen6    Janka, Z.7    Rasko, I.8
  • 176
    • 0032933750 scopus 로고    scopus 로고
    • Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF
    • DOI 10.1046/j.1471-4159.1999.0720771.x
    • Lovell MA, Gabbita SP, Markesbery WR. Increased DNA oxidation and decreased levels of repair products in Alzheimer ' s disease ventricular CSF. J Neurochem 1999;72: 771-776. (Pubitemid 29055242)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.2 , pp. 771-776
    • Lovell, M.A.1    Gabbita, S.P.2    Markesbery, W.R.3
  • 177
    • 18844462415 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2005.03053.x
    • Wang J, Xiong S, Xie C, Markesbery WR, Lovell MA. Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer ' s disease. J Neurochem 2005;93:953-962. (Pubitemid 40695754)
    • (2005) Journal of Neurochemistry , vol.93 , Issue.4 , pp. 953-962
    • Wang, J.1    Xiong, S.2    Xie, C.3    Markesbery, W.R.4    Lovell, M.A.5
  • 178
    • 42749087763 scopus 로고    scopus 로고
    • The mitochondrial impairment oxidative stress and neurodegeneration connection: Reality or just an attractive hypothesis?
    • Fukui H, Moraes CT. The mitochondrial impairment, oxidative stress and neurodegeneration connection: reality or just an attractive hypothesis? Trends Neurosci 2008;31: 251-256.
    • (2008) Trends Neurosci , vol.31 , pp. 251-256
    • Fukui, H.1    Moraes, C.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.