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Volumn 56, Issue , 2013, Pages 184-192

Antioxidant role of amyloid β protein in cell-free and biological systems: Implication for the pathogenesis of Alzheimerdisease

Author keywords

Alzheimer disease; Amyloid peptide; Antioxidant; Free radicals; Mitochondria; Reactive oxygen species

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; ASCORBIC ACID; BENZOIC ACID; BRAIN PROTEIN; CARBOXYLIC ACID; COUMARIN; HYDROGEN PEROXIDE; HYDROXYL GROUP; IRON; RADICAL;

EID: 84874115680     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.09.036     Document Type: Article
Times cited : (36)

References (83)
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • D.J. Selkoe Alzheimer's disease: genes, proteins, and therapy Physiol. Rev. 81 2001 741 766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 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
    • R. Pamplona, E. Dalfo, V. Ayala, M.J. Bellmunt, J. Prat, I. Ferrer, and M. Portero-Otin Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation: effects of Alzheimer disease and identification of lipoxidation targets J. Biol. Chem. 280 2005 21522 21530
    • (2005) J. Biol. Chem. , vol.280 , pp. 21522-21530
    • Pamplona, R.1    Dalfo, E.2    Ayala, V.3    Bellmunt, M.J.4    Prat, J.5    Ferrer, I.6    Portero-Otin, M.7
  • 4
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 2 2007 101 112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 5
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: A multifactorial view on the disease process
    • B. De Strooper Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process Physiol. Rev 90 2010 465 494
    • (2010) Physiol. Rev , vol.90 , pp. 465-494
    • De Strooper, B.1
  • 9
    • 0033860372 scopus 로고    scopus 로고
    • Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity
    • S. Varadarajan, S. Yatin, M. Aksenova, and D.A. Butterfield Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity J. Struct. Biol. 130 2000 184 208
    • (2000) J. Struct. Biol. , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 10
    • 34248219460 scopus 로고    scopus 로고
    • Membrane mediated amyloidogenesis and the promotion of oxidative lipid damage by amyloid β proteins
    • I.V.J. Murray, L. Liu, H. Komatsu, K. Uryu, G. Xiao, J.A. Lawson, and P.A. Axelsen Membrane mediated amyloidogenesis and the promotion of oxidative lipid damage by amyloid β proteins J. Biol. Chem. 282 2007 9335 9345
    • (2007) J. Biol. Chem. , vol.282 , pp. 9335-9345
    • Murray, I.V.J.1    Liu, L.2    Komatsu, H.3    Uryu, K.4    Xiao, G.5    Lawson, J.A.6    Axelsen, P.A.7
  • 11
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • J.N. Keller, Z. Pang, J.W. Geddes, J.G. Begley, A. Germeyer, G. Waeg, and M.P. Mattson Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: role of the lipid peroxidation product 4-hydroxynonenal J. Neurochem. 69 1997 273 284
    • (1997) J. Neurochem. , vol.69 , pp. 273-284
    • Keller, J.N.1    Pang, Z.2    Geddes, J.W.3    Begley, J.G.4    Germeyer, A.5    Waeg, G.6    Mattson, M.P.7
  • 12
    • 0035667920 scopus 로고    scopus 로고
    • Differential efficacy of lipophilic and cytosolic antioxidants on generation of reactive oxygen species by amyloid-β
    • S. Dhitavat, E.R. Riverac, E. Rogers, and T.B. Shea Differential efficacy of lipophilic and cytosolic antioxidants on generation of reactive oxygen species by amyloid-β J. Alzheimers Dis. 3 2001 525 529
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 525-529
    • Dhitavat, S.1    Riverac, E.R.2    Rogers, E.3    Shea, T.B.4
  • 13
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide
    • R.J. Mark, M.A. Lovell, W.R. Markesbery, K. Uchida, and M.P. Mattson A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide J. Neurochem. 68 1997 255 264
    • (1997) J. Neurochem. , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 14
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid β peptide
    • D.G. Smith, R. Cappai, and K.J. Barnham The redox chemistry of the Alzheimer's disease amyloid β peptide Biochim. Biophys. Acta 1768 2007 1976 1990
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 17
    • 66149179229 scopus 로고    scopus 로고
    • Abeta 40, either soluble or aggregated, is a remarkably potent antioxidant in cell-free oxidative systems
    • R. Baruch-Suchodolsky, and B. Fischer Abeta 40, either soluble or aggregated, is a remarkably potent antioxidant in cell-free oxidative systems Biochemistry 48 2009 4354 4370
    • (2009) Biochemistry , vol.48 , pp. 4354-4370
    • Baruch-Suchodolsky, R.1    Fischer, B.2
  • 18
    • 0033794471 scopus 로고    scopus 로고
    • Factors affecting pro- and anti-oxidant properties of fragments of the b-protein precursor (bPP): Implication for Alzheimer's disease
    • A.C. Andorn, and R.N. Kalaria Factors affecting pro- and anti-oxidant properties of fragments of the b-protein precursor (bPP): implication for Alzheimer's disease J. Alzheimers Dis. 2 2000 69 78
    • (2000) J. Alzheimers Dis. , vol.2 , pp. 69-78
    • Andorn, A.C.1    Kalaria, R.N.2
  • 19
    • 0031589214 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions
    • M.F. Walter, P.E. Mason, and R.P. Mason Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions Biochem. Biophys. Res. Commun. 233 1997 760 764
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 760-764
    • Walter, M.F.1    Mason, P.E.2    Mason, R.P.3
  • 25
    • 0035194165 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling
    • J.R. Hoidal Reactive oxygen species and cell signaling Am. J. Respir. Cell. Mol. Biol. 25 2001 661 663
    • (2001) Am. J. Respir. Cell. Mol. Biol. , vol.25 , pp. 661-663
    • Hoidal, J.R.1
  • 28
    • 84455173852 scopus 로고    scopus 로고
    • Aging promotes amyloid beta peptide induced mitochondrial dysfunctions in rat brain: A molecular link between aging and Alzheimer's disease
    • M. Sinha, P. Behera, P. Bhowmick, K. Banerjee, S. Basu, and S. Chakrabarti Aging promotes amyloid beta peptide induced mitochondrial dysfunctions in rat brain: a molecular link between aging and Alzheimer's disease J. Alzheimers Dis. 27 2011 753 765
    • (2011) J. Alzheimers Dis. , vol.27 , pp. 753-765
    • Sinha, M.1    Behera, P.2    Bhowmick, P.3    Banerjee, K.4    Basu, S.5    Chakrabarti, S.6
  • 29
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • H 3rd. Levine Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution Protein Sci 2 1993 404 410
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • Levine III, H.1
  • 30
    • 0023338482 scopus 로고
    • Ferrous-salt-promoted damage to deoxyribose and benzoate: The increased effectiveness of hydroxyl-radical scavengers in the presence of EDTA
    • J.M. Gutteridge Ferrous-salt-promoted damage to deoxyribose and benzoate: the increased effectiveness of hydroxyl-radical scavengers in the presence of EDTA Biochem. J. 243 1987 709 714
    • (1987) Biochem. J. , vol.243 , pp. 709-714
    • Gutteridge, J.M.1
  • 31
    • 0030680226 scopus 로고    scopus 로고
    • Coumarin-3-carboxylic acid as a detector for hydroxyl radicals generated chemically and by γ radiation
    • Y. Manevich, K.D. Held, and J.E. Biaglow Coumarin-3-carboxylic acid as a detector for hydroxyl radicals generated chemically and by γ radiation Radiat. Res. 148 1997 580 591
    • (1997) Radiat. Res. , vol.148 , pp. 580-591
    • Manevich, Y.1    Held, K.D.2    Biaglow, J.E.3
  • 32
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • Q. Chen, E.J. Vazquez, S. Moghaddas, C.L. Hoppel, and E.J. Lesnefsky Production of reactive oxygen species by mitochondria: central role of complex III J. Biol. Chem. 38 2003 36027 36031
    • (2003) J. Biol. Chem. , vol.38 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 34
    • 79954581538 scopus 로고    scopus 로고
    • Mitochondrial dysfunction mediated by quinone oxidation products of dopamine: Implications in dopamine cytotoxicity and pathogenesis of Parkinson's disease
    • S. Jana, M. Sinha, D. Chanda, T. Roy, K. Banerjee, S. Munshi, B.S. Patro, and S. Chakrabart Mitochondrial dysfunction mediated by quinone oxidation products of dopamine: implications in dopamine cytotoxicity and pathogenesis of Parkinson's disease Biochim. Biophys. Acta 1812 2011 663 673
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 663-673
    • Jana, S.1    Sinha, M.2    Chanda, D.3    Roy, T.4    Banerjee, K.5    Munshi, S.6    Patro, B.S.7    Chakrabart, S.8
  • 35
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • H. Ohkawa, N. Ohishi, and K. Yagi Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction Anal. Biochem. 95 1979 351 358
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 36
    • 0034868796 scopus 로고    scopus 로고
    • Lipid peroxidation associated protein damage in rat brain crude synaptosomal fraction mediated by iron and ascorbate
    • H. Chakraborty, S.N. Ray, and S. Chakrabarti Lipid peroxidation associated protein damage in rat brain crude synaptosomal fraction mediated by iron and ascorbate Neurochem. Int. 39 2001 311 317
    • (2001) Neurochem. Int. , vol.39 , pp. 311-317
    • Chakraborty, H.1    Ray, S.N.2    Chakrabarti, S.3
  • 37
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • R.L. Levine, J.A. Williams, E.R. Stadtman, and E. Shacter Carbonyl assays for determination of oxidatively modified proteins Methods Enzymol. 233 1994 346 357
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 38
    • 0036712473 scopus 로고    scopus 로고
    • The carbonyl content of specific plasma proteins is decreased by dietary copper deficiency in rats
    • K.A. Cockell, and B. Belonje The carbonyl content of specific plasma proteins is decreased by dietary copper deficiency in rats J. Nutr. 132 2002 2514 2518
    • (2002) J. Nutr. , vol.132 , pp. 2514-2518
    • Cockell, K.A.1    Belonje, B.2
  • 39
    • 62349088898 scopus 로고    scopus 로고
    • Mitochondrial decay in the brains of old rats: Ameliorating effect of alpha-lipoic acid and acetyl-L-carnitine
    • J. Long, F. Gao, L. Tong, C.W. Cotman, B.N. Ames, and J. Liu Mitochondrial decay in the brains of old rats: ameliorating effect of alpha-lipoic acid and acetyl-L-carnitine Neurochem. Res. 34 2009 755 763
    • (2009) Neurochem. Res. , vol.34 , pp. 755-763
    • Long, J.1    Gao, F.2    Tong, L.3    Cotman, C.W.4    Ames, B.N.5    Liu, J.6
  • 40
    • 0036790590 scopus 로고    scopus 로고
    • Mouse heat shock transcription factor 1deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage
    • L.J. Yan, E.S. Christians, L. Liu, X. Xiao, R.S Sohal, and I.J Benjamin Mouse heat shock transcription factor 1deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage EMBO J. 21 2002 5164 5172
    • (2002) EMBO J. , vol.21 , pp. 5164-5172
    • Yan, L.J.1    Christians, E.S.2    Liu, L.3    Xiao, X.4    Sohal, R.S.5    Benjamin, I.J.6
  • 41
    • 0002276871 scopus 로고
    • Oxygen proton and phosphate fluxes and stoichiometries
    • G.C. Brown, C.E. Cooper, IRL Press Oxford
    • P.C. Hinkle Oxygen proton and phosphate fluxes and stoichiometries G.C. Brown, C.E. Cooper, Bioenergetics: a Practical Approach 1995 IRL Press Oxford 1 15
    • (1995) Bioenergetics: A Practical Approach , pp. 1-15
    • Hinkle, P.C.1
  • 43
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • B. Halliwell, and J.M. Gutteridge Oxygen toxicity, oxygen radicals, transition metals and disease Biochem. J. 219 1984 1 14
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 44
    • 48249117506 scopus 로고    scopus 로고
    • Soluble amyloid beta(1-28)-(I)/copper(II)/iron(II) complexes are potent antioxidants in cell-free copper systems
    • R. Baruch-Suchodolsky, and B. Fischer Soluble amyloid beta(1-28)-(I)/copper(II)/iron(II) complexes are potent antioxidants in cell-free copper systems Biochemistry 47 2008 7796 7806
    • (2008) Biochemistry , vol.47 , pp. 7796-7806
    • Baruch-Suchodolsky, R.1    Fischer, B.2
  • 50
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • M. Manczak, T.S. Anekonda, E. Henson, B.S. Park, J. Quinn, and P.H. Reddy Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression Hum. Mol. Genet. 15 2006 1437 1449
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 51
    • 77956201762 scopus 로고    scopus 로고
    • Role of mitochondrial amyloid-β in Alzheimer's disease
    • J.X. Chen, and S.S. Yan Role of mitochondrial amyloid-β in Alzheimer's disease J. Alzheimers Dis. 20 2010 S569 S578
    • (2010) J. Alzheimers Dis. , vol.20
    • Chen, J.X.1    Yan, S.S.2
  • 52
    • 79951761390 scopus 로고    scopus 로고
    • The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: Oligomer size or conformation?
    • K. Broersen, F. Rousseau, and J. Schymkowitz The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? Alzheimers Res. Ther. 2 2010 1 12
    • (2010) Alzheimers Res. Ther. , vol.2 , pp. 1-12
    • Broersen, K.1    Rousseau, F.2    Schymkowitz, J.3
  • 53
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • X. Hu, S.L. Crick, G. Bu, C. Frieden, R.V. Pappu, and J.M. Lee Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Proc. Natl. Acad. Sci. USA 106 2009 20324 20329
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 54
    • 0042387935 scopus 로고    scopus 로고
    • 1-42 reduces iron-induced toxicity in rat cerebral cortex
    • 1-42 reduces iron-induced toxicity in rat cerebral cortex J. Neurosci. Res. 73 2003 316 323
    • (2003) J. Neurosci. Res. , vol.73 , pp. 316-323
    • Bishop, G.M.1    Robinson, S.R.2
  • 55
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 1 2009 1 13
    • (2009) Biochem. J. , vol.417 , Issue.1 , pp. 1-13
    • Murphy, M.P.1
  • 56
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state J. Neurochem. 86 2003 1101 1107
    • (2003) J. Neurochem. , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 57
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • L. Kussmaul, and J. Hirst The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria Proc. Natl. Acad. Sci. USA 103 2006 7607 7612
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 58
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species mitochondrial electron transport complex i activity through oxidative cardiolipin damage
    • G. Paradies, G. Petrosillo, M. Pistolese, and F.M. Ruggiero Reactive oxygen species mitochondrial electron transport complex I activity through oxidative cardiolipin damage Gene 286 2002 135 141
    • (2002) Gene , vol.286 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 60
    • 33748201552 scopus 로고    scopus 로고
    • Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents
    • H.H. Szeto Mitochondria-targeted peptide antioxidants: novel neuroprotective agents AAPS J. 8 2006 619 642
    • (2006) AAPS J. , vol.8 , pp. 619-642
    • Szeto, H.H.1
  • 61
    • 0037096251 scopus 로고    scopus 로고
    • A novel function of monomeric amyloid β protein serving as an antioxidant molecule against metal-induced oxidative damage
    • K. Zou, J.S. Gong, K. Yanagisawa, and M. Michikawa A novel function of monomeric amyloid β protein serving as an antioxidant molecule against metal-induced oxidative damage J. Neurosci. 22 2002 4833 4841
    • (2002) J. Neurosci. , vol.22 , pp. 4833-4841
    • Zou, K.1    Gong, J.S.2    Yanagisawa, K.3    Michikawa, M.4
  • 62
    • 0031741578 scopus 로고    scopus 로고
    • The free radical antioxidant vitamin e protects cortical synaptosomal membranes from amyloid β-peptide (25-35) toxicity but not from hydroxynonenal toxicity: Relevance to the free radical hypothesis of Alzheimer's disease
    • R. Subramaniam, T. Koppal, M. Green, S. Yatin, B. Jordan, J. Drake, and D.A. Butterfield The free radical antioxidant vitamin E protects cortical synaptosomal membranes from amyloid β-peptide (25-35) toxicity but not from hydroxynonenal toxicity: relevance to the free radical hypothesis of Alzheimer's disease Neurochem. Res. 23 1998 1403 1410
    • (1998) Neurochem. Res. , vol.23 , pp. 1403-1410
    • Subramaniam, R.1    Koppal, T.2    Green, M.3    Yatin, S.4    Jordan, B.5    Drake, J.6    Butterfield, D.A.7
  • 63
    • 1542377619 scopus 로고    scopus 로고
    • Toxicity of amyloid β peptide: Tales of calcium, mitochondria, and oxidative stress
    • L. Canevari, A.Y. Abramov, and M.R. Duchen Toxicity of amyloid β peptide: tales of calcium, mitochondria, and oxidative stress Neurochem. Res. 29 2004 637 650
    • (2004) Neurochem. Res. , vol.29 , pp. 637-650
    • Canevari, L.1    Abramov, A.Y.2    Duchen, M.R.3
  • 64
    • 0032891616 scopus 로고    scopus 로고
    • Gearing, A. J.; Miller, K. M. A central role for astrocytes in the inflammatory response to beta-amyloid; Chemokines, cytokines and reactive oxygen species are produced
    • M. Johnstone Gearing, A. J.; Miller, K. M. A central role for astrocytes in the inflammatory response to beta-amyloid; chemokines, cytokines and reactive oxygen species are produced J. Neuroimmunol. 93 1999 182 193
    • (1999) J. Neuroimmunol. , vol.93 , pp. 182-193
    • Johnstone, M.1
  • 65
    • 0035500510 scopus 로고    scopus 로고
    • Amyloid-β: An antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer's disease
    • A. Kontush Amyloid-β: an antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer's disease Free Radic. Biol. Med. 31 2001 1120 1131
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1120-1131
    • Kontush, A.1
  • 67
    • 0034981701 scopus 로고    scopus 로고
    • Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation
    • J. Xu, S. Chen, G. Ku, S.H. Ahmed, J. Xu, H. Chen, and C.Y. Hsu Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation J. Cereb. Blood Flow Metab. 21 2001 702 710
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 702-710
    • Xu, J.1    Chen, S.2    Ku, G.3    Ahmed, S.H.4    Xu, J.5    Chen, H.6    Hsu, C.Y.7
  • 68
    • 68149148549 scopus 로고    scopus 로고
    • Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells
    • V. Rhein, G. Baysang, S. Rao, F. Meier, A. Bonert, F. Müller-Spahn, and A. Eckert Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells Cell. Mol. Neurobiol. 29 2009 1063 1071
    • (2009) Cell. Mol. Neurobiol. , vol.29 , pp. 1063-1071
    • Rhein, V.1    Baysang, G.2    Rao, S.3    Meier, F.4    Bonert, A.5    Müller-Spahn, F.6    Eckert, A.7
  • 69
    • 79955454688 scopus 로고    scopus 로고
    • Amyloid-beta interaction with mitochondria
    • L. Pagani, and A. Eckert Amyloid-beta interaction with mitochondria Int. J. Alzheimers Dis. 2011 925050
    • (2011) Int. J. Alzheimers Dis. , pp. 925050
    • Pagani, L.1    Eckert, A.2
  • 70
    • 0034812181 scopus 로고    scopus 로고
    • Amyloid β-peptide disrupts mitochondrial membrane lipid and protein structure: Protective role of tauroursodeoxycholate
    • C.M. Rodrigues, S. Sola, M.A. Brito, C.D. Brondino, D. Brites, and J.J. Moura Amyloid β-peptide disrupts mitochondrial membrane lipid and protein structure: protective role of tauroursodeoxycholate Biochem. Biophys. Res. Commun. 281 2001 468 474
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 468-474
    • Rodrigues, C.M.1    Sola, S.2    Brito, M.A.3    Brondino, C.D.4    Brites, D.5    Moura, J.J.6
  • 71
    • 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
    • M.J. Calkins, M. Manczak, P. Mao, U. Shirendeb, and P.H. Reddy 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. 20 2011 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
  • 72
    • 57049099718 scopus 로고    scopus 로고
    • N-acetylcysteine prevents beta-amyloid toxicity by a stimulatory effect on p35/cyclin-dependent kinase 5activity in cultured cortical neurons
    • Y.H. Hsiao, P.S. Chen, S.H. Yeh, C.H. Lin, and P.W. Gean N-acetylcysteine prevents beta-amyloid toxicity by a stimulatory effect on p35/cyclin-dependent kinase 5activity in cultured cortical neurons J. Neurosci. Res. 86 2008 2685 2695
    • (2008) J. Neurosci. Res. , vol.86 , pp. 2685-2695
    • Hsiao, Y.H.1    Chen, P.S.2    Yeh, S.H.3    Lin, C.H.4    Gean, P.W.5
  • 73
    • 78651074924 scopus 로고    scopus 로고
    • Protects human neuroblastoma SH-SY5Y cells against β-amyloid-induced cell toxicity
    • P. Chonpathompikunlert, J. Han, K. Toh, H. Isoda, and Y.TEMPOL Nagasaki protects human neuroblastoma SH-SY5Y cells against β-amyloid-induced cell toxicity Eur. J. Pharmacol. 650 2011 544 549
    • (2011) Eur. J. Pharmacol. , vol.650 , pp. 544-549
    • Chonpathompikunlert, P.1    Han, J.2    Toh, K.3    Isoda, H.4    Nagasaki, Y.T.5
  • 74
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides
    • X. Huang, C.S. Atwood, R.D. Moir, M.A. Hartshorn, R.E. Tanzi, and A.I. Bush Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides J. Biol. Inorg. Chem. 9 2004 954 960
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 954-960
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Tanzi, R.E.5    Bush, A.I.6
  • 75
    • 70350348150 scopus 로고    scopus 로고
    • Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots
    • L. Xiao, D. Zhao, W.H. Chan, M.M. Choi, and H.W. Li Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots Biomaterials 31 2010 91 98
    • (2010) Biomaterials , vol.31 , pp. 91-98
    • Xiao, L.1    Zhao, D.2    Chan, W.H.3    Choi, M.M.4    Li, H.W.5
  • 77
    • 27144513779 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • M. Hirohata, K. Ono, H. Naiki, and M. Yamada Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro Neuropharmacology 49 2005 1088 1099
    • (2005) Neuropharmacology , vol.49 , pp. 1088-1099
    • Hirohata, M.1    Ono, K.2    Naiki, H.3    Yamada, M.4
  • 79
    • 0029985732 scopus 로고    scopus 로고
    • Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (Aβ) in mammalian lenses, and Aβ has toxic effects on lens epithelial cells
    • P.H. Frederikse, D. Garland, J.S. Zigler Jr, and J. Piatigorsky Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (Aβ) in mammalian lenses, and Aβ has toxic effects on lens epithelial cells J. Biol. Chem. 271 1996 10169 10174
    • (1996) J. Biol. Chem. , vol.271 , pp. 10169-10174
    • Frederikse, P.H.1    Garland, D.2    Zigler, Jr.J.S.3    Piatigorsky, J.4
  • 80
    • 52649131924 scopus 로고    scopus 로고
    • Oxidative stress increases levels of endogenous amyloid-beta peptides secreted from primary chick brain neurons
    • C. Goldsbury, I.T. Whiteman, E.V. Jeong, and Y.A. Lim Oxidative stress increases levels of endogenous amyloid-beta peptides secreted from primary chick brain neurons Aging Cell 7 2008 771 775
    • (2008) Aging Cell , vol.7 , pp. 771-775
    • Goldsbury, C.1    Whiteman, I.T.2    Jeong, E.V.3    Lim, Y.A.4
  • 81
    • 34249337528 scopus 로고    scopus 로고
    • Iron dysregulation in Alzheimer's disease: Multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents
    • S. Mandel, T. Amit, O. Bar-Am, and M.B. Youdim Iron dysregulation in Alzheimer's disease: multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents Prog. Neurobiol. 82 2007 348 360
    • (2007) Prog. Neurobiol. , vol.82 , pp. 348-360
    • Mandel, S.1    Amit, T.2    Bar-Am, O.3    Youdim, M.B.4
  • 82
    • 77950189704 scopus 로고    scopus 로고
    • Copper enhances amyloid-β peptide neurotoxicity and non β-aggregation: A series of experiments conducted upon copper-bound and copper-free amyloid-β peptide
    • X. Dai, Y. Sun, Z. Gao, and Z. Jiang Copper enhances amyloid-β peptide neurotoxicity and non β-aggregation: a series of experiments conducted upon copper-bound and copper-free amyloid-β peptide J. Mol. Neurosci. 41 2010 66 73
    • (2010) J. Mol. Neurosci. , vol.41 , pp. 66-73
    • Dai, X.1    Sun, Y.2    Gao, Z.3    Jiang, Z.4
  • 83
    • 58049203021 scopus 로고    scopus 로고
    • Is covalently crosslinked Aβ responsible for synaptotoxicity in Alzheimer's disease?
    • R. Naylor, A.F. Hill, and K.J. Barnham Is covalently crosslinked Aβ responsible for synaptotoxicity in Alzheimer's disease? Curr. Alzheimers Res. 5 2008 533 539
    • (2008) Curr. Alzheimers Res. , vol.5 , pp. 533-539
    • Naylor, R.1    Hill, A.F.2    Barnham, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.