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Volumn 1768, Issue 8, 2007, Pages 1976-1990

The redox chemistry of the Alzheimer's disease amyloid β peptide

Author keywords

Alzheimer's disease; Amyloid beta; Metal; Oxidative stress; Redox chemistry

Indexed keywords

1,1' XYLYL BIS 1,4,8,11 TETRAAZACYCLOTETRADECANE; ALPHA TOCOPHEROL; AMYLOID BETA PROTEIN; ANTIOXIDANT; ASCORBIC ACID; CLIOQUINOL; COPPER; CURCUMIN; DEFEROXAMINE; GINKGO BILOBA EXTRACT; GOSSYPINE; IRON; JKL 169; MELATONIN; METALLOPROTEIN; METHIONINE; OLIGOMER; REACTIVE OXYGEN METABOLITE; TRIENTINE; TYROSINE; UNCLASSIFIED DRUG; ZINC;

EID: 34547147090     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.02.002     Document Type: Review
Times cited : (557)

References (217)
  • 2
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G.G., and Wong C.W. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122 (1984) 1131-1135
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D., Lerman M.I., McBride O.W., Saffiotti U., and Gajdusek D.C. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235 (1987) 877-880
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 7
    • 0026442891 scopus 로고
    • Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid beta protein precursor
    • Wasco W., Bupp K., Magendantz M., Gusella J.F., Tanzi R.E., and Solomon F. Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid beta protein precursor. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 10758-10762
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10758-10762
    • Wasco, W.1    Bupp, K.2    Magendantz, M.3    Gusella, J.F.4    Tanzi, R.E.5    Solomon, F.6
  • 8
    • 0028059841 scopus 로고
    • Expression of a ubiquitous, cross-reactive homologue of the mouse beta-amyloid precursor protein (APP)
    • Slunt H.H., Thinakaran G., Von Koch C., Lo A.C., Tanzi R.E., and Sisodia S.S. Expression of a ubiquitous, cross-reactive homologue of the mouse beta-amyloid precursor protein (APP). J. Biol. Chem. 269 (1994) 2637-2644
    • (1994) J. Biol. Chem. , vol.269 , pp. 2637-2644
    • Slunt, H.H.1    Thinakaran, G.2    Von Koch, C.3    Lo, A.C.4    Tanzi, R.E.5    Sisodia, S.S.6
  • 9
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein
    • Mattson M.P., Cheng B., Culwell A.R., Esch F.S., Lieberburg I., and Rydel R.E. Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein. Neuron 10 (1993) 243-254
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 10
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • Milward E.A., Papadopoulos R., Fuller S.J., Moir R.D., Small D., Beyreuther K., and Masters C.L. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron 9 (1992) 129-137
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3    Moir, R.D.4    Small, D.5    Beyreuther, K.6    Masters, C.L.7
  • 12
    • 0024395366 scopus 로고
    • Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts
    • Saitoh T., Sundsmo M., Roch J.M., Kimura N., Cole G., Schubert D., Oltersdorf T., and Schenk D.B. Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts. Cell 58 (1989) 615-622
    • (1989) Cell , vol.58 , pp. 615-622
    • Saitoh, T.1    Sundsmo, M.2    Roch, J.M.3    Kimura, N.4    Cole, G.5    Schubert, D.6    Oltersdorf, T.7    Schenk, D.B.8
  • 13
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K., and Masters C.L. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J. Neurosci. 14 (1994) 2117-2127
    • (1994) J. Neurosci. , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 14
    • 0030727343 scopus 로고    scopus 로고
    • Down-regulation of the amyloid protein precursor of Alzheimer's disease by antisense oligonucleotides reduces neuronal adhesion to specific substrata
    • Coulson E.J., Barrett G.L., Storey E., Bartlett P.F., Beyreuther K., and Masters C.L. Down-regulation of the amyloid protein precursor of Alzheimer's disease by antisense oligonucleotides reduces neuronal adhesion to specific substrata. Brain Res. 770 (1997) 72-80
    • (1997) Brain Res. , vol.770 , pp. 72-80
    • Coulson, E.J.1    Barrett, G.L.2    Storey, E.3    Bartlett, P.F.4    Beyreuther, K.5    Masters, C.L.6
  • 15
    • 0030574061 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid precursor protein on the surface of cortical neurons in primary culture co-localizes with adhesion patch components
    • Storey E., Beyreuther K., and Masters C.L. Alzheimer's disease amyloid precursor protein on the surface of cortical neurons in primary culture co-localizes with adhesion patch components. Brain Res. 735 (1996) 217-231
    • (1996) Brain Res. , vol.735 , pp. 217-231
    • Storey, E.1    Beyreuther, K.2    Masters, C.L.3
  • 16
    • 0141462295 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease is found on the surface of static but not activity motile portions of neurites
    • Storey E., Spurck T., Pickett-Heaps J., Beyreuther K., and Masters C.L. The amyloid precursor protein of Alzheimer's disease is found on the surface of static but not activity motile portions of neurites. Brain Res. 735 (1996) 59-66
    • (1996) Brain Res. , vol.735 , pp. 59-66
    • Storey, E.1    Spurck, T.2    Pickett-Heaps, J.3    Beyreuther, K.4    Masters, C.L.5
  • 17
    • 0025965521 scopus 로고
    • Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion
    • Breen K.C., Bruce M., and Anderton B.H. Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J. Neurosci. Res. 28 (1991) 90-100
    • (1991) J. Neurosci. Res. , vol.28 , pp. 90-100
    • Breen, K.C.1    Bruce, M.2    Anderton, B.H.3
  • 18
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena S., and Goldstein L.S. Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 32 (2001) 389-401
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 19
    • 0028177269 scopus 로고
    • The beta A4 amyloid precursor protein binding to copper
    • Hesse L., Beher D., Masters C.L., and Multhaup G. The beta A4 amyloid precursor protein binding to copper. FEBS Lett. 349 (1994) 109-116
    • (1994) FEBS Lett. , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 20
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • Multhaup G., Schlicksupp A., Hesse L., Beher D., Ruppert T., Masters C.L., and Beyreuther K. The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I). Science 271 (1996) 1406-1409
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 22
    • 0032546577 scopus 로고    scopus 로고
    • Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide
    • Multhaup G., Ruppert T., Schlicksupp A., Hesse L., Bill E., Pipkorn R., Masters C.L., and Beyreuther K. Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide. Biochemistry 37 (1998) 7224-7230
    • (1998) Biochemistry , vol.37 , pp. 7224-7230
    • Multhaup, G.1    Ruppert, T.2    Schlicksupp, A.3    Hesse, L.4    Bill, E.5    Pipkorn, R.6    Masters, C.L.7    Beyreuther, K.8
  • 29
    • 34247553217 scopus 로고    scopus 로고
    • Amine Oxidases
    • Lennarz W.J., and Lane M.D. (Eds), Elsevier Inc.
    • Floris G., and Agro A.F. Amine Oxidases. In: Lennarz W.J., and Lane M.D. (Eds). Encyclopedia of Biological Chemistry vol. 1 (2004), Elsevier Inc. 85-89
    • (2004) Encyclopedia of Biological Chemistry , vol.1 , pp. 85-89
    • Floris, G.1    Agro, A.F.2
  • 30
    • 0022480081 scopus 로고
    • Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress
    • Martins R.N., Harper C.G., Stokes G.B., and Masters C.L. Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress. J. Neurochem. 46 (1986) 1042-1045
    • (1986) J. Neurochem. , vol.46 , pp. 1042-1045
    • Martins, R.N.1    Harper, C.G.2    Stokes, G.B.3    Masters, C.L.4
  • 31
    • 0028129137 scopus 로고
    • Evidence of an oxidative challenge in the Alzheimer's brain
    • Balazs L., and Leon M. Evidence of an oxidative challenge in the Alzheimer's brain. Neurochem. Res. 19 (1994) 1131-1137
    • (1994) Neurochem. Res. , vol.19 , pp. 1131-1137
    • Balazs, L.1    Leon, M.2
  • 32
    • 8544257019 scopus 로고    scopus 로고
    • Heme oxygenase expression in human central nervous system disorders
    • Schipper H.M. Heme oxygenase expression in human central nervous system disorders. Free Radic. Biol. Med. 37 (2004) 1995-2011
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1995-2011
    • Schipper, H.M.1
  • 33
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery W.R., and Lovell M.A. Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol. Aging 19 (1998) 33-36
    • (1998) Neurobiol. Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 34
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • Sayre L.M., Zelasko D.A., Harris P.L., Perry G., Salomon R.G., and Smith M.A. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J. Neurochem. 68 (1997) 2092-2097
    • (1997) J. Neurochem. , vol.68 , pp. 2092-2097
    • Sayre, L.M.1    Zelasko, D.A.2    Harris, P.L.3    Perry, G.4    Salomon, R.G.5    Smith, M.A.6
  • 35
    • 33744935554 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease
    • Williams T.I., Lynn B.C., Markesbery W.R., and Lovell M.A. Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease. Neurobiol. Aging 27 (2006) 1094-1099
    • (2006) Neurobiol. Aging , vol.27 , pp. 1094-1099
    • Williams, T.I.1    Lynn, B.C.2    Markesbery, W.R.3    Lovell, M.A.4
  • 38
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., and Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10 (1997) 485-494
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 40
    • 20444373701 scopus 로고    scopus 로고
    • Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
    • Pamplona R., Dalfo E., Ayala V., Bellmunt M.J., Prat J., Ferrer I., and Portero-Otin M. Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. J. Biol. Chem. 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
  • 42
    • 0033401851 scopus 로고    scopus 로고
    • In vitro and in vivo protein oxidation induced by Alzheimer's disease amyloid beta-peptide (1-42)
    • Butterfield D.A., Yatin S.M., and Link C.D. In vitro and in vivo protein oxidation induced by Alzheimer's disease amyloid beta-peptide (1-42). Ann. N. Y. Acad. Sci. 893 (1999) 265-268
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 265-268
    • Butterfield, D.A.1    Yatin, S.M.2    Link, C.D.3
  • 45
    • 0030898724 scopus 로고    scopus 로고
    • An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease
    • Lyras L., Cairns N.J., Jenner A., Jenner P., and Halliwell B. An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease. J. Neurochem. 68 (1997) 2061-2069
    • (1997) J. Neurochem. , vol.68 , pp. 2061-2069
    • Lyras, L.1    Cairns, N.J.2    Jenner, A.3    Jenner, P.4    Halliwell, B.5
  • 46
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley K., Maidt M.L., Yu Z., Sang H., Markesbery W.R., and Floyd R.A. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 18 (1998) 8126-8132
    • (1998) J. Neurosci. , vol.18 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 49
    • 0032806289 scopus 로고    scopus 로고
    • Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine
    • Leeuwenburgh C., Hansen P.A., Holloszy J.O., and Heinecke J.W. Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine. Free Radic. Biol. Med. 27 (1999) 186-192
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 186-192
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 50
    • 0032891777 scopus 로고    scopus 로고
    • Oxidized amino acids in the urine of aging rats: potential markers for assessing oxidative stress in vivo
    • Leeuwenburgh C., Hansen P.A., Holloszy J.O., and Heinecke J.W. Oxidized amino acids in the urine of aging rats: potential markers for assessing oxidative stress in vivo. Am. J. Physiol. 276 (1999) R128-R135
    • (1999) Am. J. Physiol. , vol.276
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 51
    • 0037072542 scopus 로고    scopus 로고
    • Beta-amyloid deposition and neurofibrillary tangle association with caspase activation in Down syndrome
    • Head E., Lott I.T., Cribbs D.H., Cotman C.W., and Rohn T.T. Beta-amyloid deposition and neurofibrillary tangle association with caspase activation in Down syndrome. Neurosci. Lett. 330 (2002) 99-103
    • (2002) Neurosci. Lett. , vol.330 , pp. 99-103
    • Head, E.1    Lott, I.T.2    Cribbs, D.H.3    Cotman, C.W.4    Rohn, T.T.5
  • 52
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong J., Atwood C.S., Anderson V.E., Siedlak S.L., Smith M.A., Perry G., and Carey P.R. Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42 (2003) 2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 53
    • 0033969616 scopus 로고    scopus 로고
    • Decreased thioredoxin and increased thioredoxin reductase levels in Alzheimer's disease brain
    • Lovell M.A., Xie C., Gabbita S.P., and Markesbery W.R. Decreased thioredoxin and increased thioredoxin reductase levels in Alzheimer's disease brain. Free Radic. Biol. Med. 28 (2000) 418-427
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 418-427
    • Lovell, M.A.1    Xie, C.2    Gabbita, S.P.3    Markesbery, W.R.4
  • 54
    • 0031678044 scopus 로고    scopus 로고
    • Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease
    • Lovell M.A., Xie C., and Markesbery W.R. Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease. Neurology 51 (1998) 1562-1566
    • (1998) Neurology , vol.51 , pp. 1562-1566
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 56
    • 30944449237 scopus 로고    scopus 로고
    • Differential neuronal expression of manganese superoxide dismutase in Alzheimer's disease
    • Marcus D.L., Strafaci J.A., and Freedman M.L. Differential neuronal expression of manganese superoxide dismutase in Alzheimer's disease. Med. Sci. Monit. 12 (2006) BR8-BR14
    • (2006) Med. Sci. Monit. , vol.12
    • Marcus, D.L.1    Strafaci, J.A.2    Freedman, M.L.3
  • 59
    • 0024490143 scopus 로고
    • Superoxide dismutase activity in Alzheimer's disease: possible mechanism for paired helical filament formation
    • Zemlan F.P., Thienhaus O.J., and Bosmann H.B. Superoxide dismutase activity in Alzheimer's disease: possible mechanism for paired helical filament formation. Brain Res. 476 (1989) 160-162
    • (1989) Brain Res. , vol.476 , pp. 160-162
    • Zemlan, F.P.1    Thienhaus, O.J.2    Bosmann, H.B.3
  • 60
    • 0025670273 scopus 로고
    • Blood activity of Cu/Zn superoxide dismutase, glutathione peroxidase and catalase in Alzheimer's disease: a case-control study
    • Perrin R., Briancon S., Jeandel C., Artur Y., Minn A., Penin F., and Siest G. Blood activity of Cu/Zn superoxide dismutase, glutathione peroxidase and catalase in Alzheimer's disease: a case-control study. Gerontology 36 (1990) 306-313
    • (1990) Gerontology , vol.36 , pp. 306-313
    • Perrin, R.1    Briancon, S.2    Jeandel, C.3    Artur, Y.4    Minn, A.5    Penin, F.6    Siest, G.7
  • 63
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush A.I. The metallobiology of Alzheimer's disease. Trends Neurosci. 26 (2003) 207-214
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 64
    • 0037174856 scopus 로고    scopus 로고
    • Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H(2)O(2)
    • Opazo C., Huang X., Cherny R.A., Moir R.D., Roher A.E., White A.R., Cappai R., Masters C.L., Tanzi R.E., Inestrosa N.C., and Bush A.I. Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H(2)O(2). J. Biol. Chem. 277 (2002) 40302-40308
    • (2002) J. Biol. Chem. , vol.277 , pp. 40302-40308
    • Opazo, C.1    Huang, X.2    Cherny, R.A.3    Moir, R.D.4    Roher, A.E.5    White, A.R.6    Cappai, R.7    Masters, C.L.8    Tanzi, R.E.9    Inestrosa, N.C.10    Bush, A.I.11
  • 65
    • 0023830814 scopus 로고
    • Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process
    • Hartter D.E., and Barnea A. Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process. J. Biol. Chem. 263 (1988) 799-805
    • (1988) J. Biol. Chem. , vol.263 , pp. 799-805
    • Hartter, D.E.1    Barnea, A.2
  • 67
    • 0021346169 scopus 로고
    • Copper-phenanthroline-induced site-specific oxygen-radical damage to DNA. Detection of loosely bound trace copper in biological fluids
    • Gutteridge J.M. Copper-phenanthroline-induced site-specific oxygen-radical damage to DNA. Detection of loosely bound trace copper in biological fluids. Biochem. J. 218 (1984) 983-985
    • (1984) Biochem. J. , vol.218 , pp. 983-985
    • Gutteridge, J.M.1
  • 68
    • 0024362166 scopus 로고
    • Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability
    • Kardos J., Kovacs I., Hajos F., Kalman M., and Simonyi M. Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability. Neurosci. Lett. 103 (1989) 139-144
    • (1989) Neurosci. Lett. , vol.103 , pp. 139-144
    • Kardos, J.1    Kovacs, I.2    Hajos, F.3    Kalman, M.4    Simonyi, M.5
  • 69
    • 0029883795 scopus 로고    scopus 로고
    • Copper biochemistry and molecular biology
    • Linder M.C., and Hazegh-Azam M. Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63 (1996) 797S-811S
    • (1996) Am. J. Clin. Nutr. , vol.63
    • Linder, M.C.1    Hazegh-Azam, M.2
  • 71
    • 0034105324 scopus 로고    scopus 로고
    • CSF copper concentrations, blood-brain barrier function, and coeruloplasmin synthesis during the treatment of Wilson's disease
    • Stuerenburg H.J. CSF copper concentrations, blood-brain barrier function, and coeruloplasmin synthesis during the treatment of Wilson's disease. J. Neural Transm. 107 (2000) 321-329
    • (2000) J. Neural Transm. , vol.107 , pp. 321-329
    • Stuerenburg, H.J.1
  • 73
    • 0028302302 scopus 로고
    • RNAA for arsenic, cadium, copper and molybdenum in CNS tissues from subjects with age-related neurodegenerative disease
    • Tandon L., Ni B.-F., Ding X.X., Ehmann W.D., Kasarskis E.J., and Markesbery W.R. RNAA for arsenic, cadium, copper and molybdenum in CNS tissues from subjects with age-related neurodegenerative disease. J. Radioanal. Nucl. Chem. 179 (1994) 331-339
    • (1994) J. Radioanal. Nucl. Chem. , vol.179 , pp. 331-339
    • Tandon, L.1    Ni, B.-F.2    Ding, X.X.3    Ehmann, W.D.4    Kasarskis, E.J.5    Markesbery, W.R.6
  • 74
    • 0023571213 scopus 로고
    • Neutron activation analysis techniques for identifying elemental status in Alzheimer's disease
    • Ward N.I., and Mason J.A. Neutron activation analysis techniques for identifying elemental status in Alzheimer's disease. J. Radioanal. Nucl. Chem. 113 (1987) 515-526
    • (1987) J. Radioanal. Nucl. Chem. , vol.113 , pp. 515-526
    • Ward, N.I.1    Mason, J.A.2
  • 75
    • 51249175720 scopus 로고
    • Trace elements in the human central nervous system studied with neutron activation analysis
    • Plantin L.-O., Lysing-Tunell U., and Kristensson K. Trace elements in the human central nervous system studied with neutron activation analysis. Biol. Trace Elem. Res. 1987 (1987) 69-75
    • (1987) Biol. Trace Elem. Res. , vol.1987 , pp. 69-75
    • Plantin, L.-O.1    Lysing-Tunell, U.2    Kristensson, K.3
  • 76
    • 0030297178 scopus 로고    scopus 로고
    • Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress
    • Deibel M.A., Ehmann W.D., and Markesbery W.R. Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress. J. Neurol. Sci. 143 (1996) 137-142
    • (1996) J. Neurol. Sci. , vol.143 , pp. 137-142
    • Deibel, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 77
    • 0033139740 scopus 로고    scopus 로고
    • Histochemically reactive zinc in plaques of the Swedish mutant beta-amyloid precursor protein transgenic mice
    • Lee J.Y., Mook-Jung I., and Koh J.Y. Histochemically reactive zinc in plaques of the Swedish mutant beta-amyloid precursor protein transgenic mice. J. Neurosci. 19 (1999) RC10
    • (1999) J. Neurosci. , vol.19
    • Lee, J.Y.1    Mook-Jung, I.2    Koh, J.Y.3
  • 78
    • 0020517761 scopus 로고
    • Cerebrospinal fluid trace element content in dementia: clinical, radiologic, and pathologic correlations
    • Hershey C.O., Hershey L.A., Varnes A., Vibhakar S.D., Lavin P., and Strain W.H. Cerebrospinal fluid trace element content in dementia: clinical, radiologic, and pathologic correlations. Neurology 33 (1983) 1350-1353
    • (1983) Neurology , vol.33 , pp. 1350-1353
    • Hershey, C.O.1    Hershey, L.A.2    Varnes, A.3    Vibhakar, S.D.4    Lavin, P.5    Strain, W.H.6
  • 79
    • 0027669512 scopus 로고
    • Hippocampal tin, aluminum and zinc in Alzheimer's disease
    • Corrigan F.M., Reynolds G.P., and Ward N.I. Hippocampal tin, aluminum and zinc in Alzheimer's disease. Biometals 6 (1993) 149-154
    • (1993) Biometals , vol.6 , pp. 149-154
    • Corrigan, F.M.1    Reynolds, G.P.2    Ward, N.I.3
  • 80
    • 0030297178 scopus 로고    scopus 로고
    • Copper, Iron and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress
    • Diebel M., Ehrmann W., and Markesbery W.R. Copper, Iron and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress. J. Neurol. Sci. 143 (1996) 137-142
    • (1996) J. Neurol. Sci. , vol.143 , pp. 137-142
    • Diebel, M.1    Ehrmann, W.2    Markesbery, W.R.3
  • 81
    • 0036860349 scopus 로고    scopus 로고
    • Metal complexing agents as therapies for Alzheimer's disease
    • Bush A.I. Metal complexing agents as therapies for Alzheimer's disease. Neurobiol. Aging 23 (2002) 1031-1038
    • (2002) Neurobiol. Aging , vol.23 , pp. 1031-1038
    • Bush, A.I.1
  • 82
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • Frederickson C.J. Neurobiology of zinc and zinc-containing neurons. Int. Rev. Neurobiol. 31 (1989) 145-238
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 83
    • 0021287299 scopus 로고
    • Release of endogenous Zn2+ from brain tissue during activity
    • Assaf S.Y., and Chung S.H. Release of endogenous Zn2+ from brain tissue during activity. Nature 308 (1984) 734-736
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 84
    • 0021220724 scopus 로고
    • Stimulation-induced uptake and release of zinc in hippocampal slices
    • Howell G.A., Welch M.G., and Frederickson C.J. Stimulation-induced uptake and release of zinc in hippocampal slices. Nature 308 (1984) 736-738
    • (1984) Nature , vol.308 , pp. 736-738
    • Howell, G.A.1    Welch, M.G.2    Frederickson, C.J.3
  • 86
    • 0033608740 scopus 로고    scopus 로고
    • Protection against amyloid beta peptide toxicity by zinc
    • Lovell M.A., Xie C., and Markesbery W.R. Protection against amyloid beta peptide toxicity by zinc. Brain Res. 823 (1999) 88-95
    • (1999) Brain Res. , vol.823 , pp. 88-95
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 87
    • 0000986581 scopus 로고    scopus 로고
    • Zonc promotes Abeta aggregation but attenuates Abeta neurotoxicity
    • Fuson K.S., Boggs L.N., and May P.C. Zonc promotes Abeta aggregation but attenuates Abeta neurotoxicity. Neurobiol. Aging 17 (1996) 431
    • (1996) Neurobiol. Aging , vol.17 , pp. 431
    • Fuson, K.S.1    Boggs, L.N.2    May, P.C.3
  • 89
    • 27744456147 scopus 로고    scopus 로고
    • Protective effect of zinc on amyloid?-beta ?25-35 and 1-40? mediated toxicity
    • Cardoso S.M., Rego A.C., Pereira C., and Oliveira C.R. Protective effect of zinc on amyloid?-beta ?25-35 and 1-40? mediated toxicity. Neurotox. Res. 7 (2005) 273-282
    • (2005) Neurotox. Res. , vol.7 , pp. 273-282
    • Cardoso, S.M.1    Rego, A.C.2    Pereira, C.3    Oliveira, C.R.4
  • 90
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity
    • Bhatia R., Lin H., and Lal R. Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity. FASEB J. 14 (2000) 1233-1243
    • (2000) FASEB J. , vol.14 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 91
    • 0033808530 scopus 로고    scopus 로고
    • Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block)
    • Hirakura Y., Yiu W.W., Yamamoto A., and Kagan B.L. Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block). Amyloid 7 (2000) 194-199
    • (2000) Amyloid , vol.7 , pp. 194-199
    • Hirakura, Y.1    Yiu, W.W.2    Yamamoto, A.3    Kagan, B.L.4
  • 92
    • 0033600590 scopus 로고    scopus 로고
    • Amyloid beta protein (1-40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles
    • Lin H., Zhu Y.J., and Lal R. Amyloid beta protein (1-40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles. Biochemistry 38 (1999) 11189-11196
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3
  • 93
    • 0001282871 scopus 로고    scopus 로고
    • Amyloid beta protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel
    • Rhee S.K., Quist A.P., and Lal R. Amyloid beta protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel. J. Biol. Chem. 273 (1998) 13379-13382
    • (1998) J. Biol. Chem. , vol.273 , pp. 13379-13382
    • Rhee, S.K.1    Quist, A.P.2    Lal, R.3
  • 94
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid beta protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity
    • Zhu Y.J., Lin H., and Lal R. Fresh and nonfibrillar amyloid beta protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity. FASEB J. 14 (2000) 1244-1254
    • (2000) FASEB J. , vol.14 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3
  • 95
    • 0029670048 scopus 로고    scopus 로고
    • Zn2+ interaction with Alzheimer amyloid beta protein calcium channels
    • Arispe N., Pollard H.B., and Rojas E. Zn2+ interaction with Alzheimer amyloid beta protein calcium channels. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 1710-1715
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1710-1715
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 96
    • 0030966536 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons
    • Kawahara M., Arispe N., Kuroda Y., and Rojas E. Alzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons. Biophys. J. 73 (1997) 67-75
    • (1997) Biophys. J. , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 100
    • 0030662586 scopus 로고    scopus 로고
    • Zinc and platelet membrane microviscosity in Alzheimer's disease. The in vivo effect of zinc on platelet membranes and cognition
    • Potocnik F.C., van Rensburg S.J., Park C., Taljaard J.J., and Emsley R.A. Zinc and platelet membrane microviscosity in Alzheimer's disease. The in vivo effect of zinc on platelet membranes and cognition. S. Afr. Med. J. 87 (1997) 1116-1119
    • (1997) S. Afr. Med. J. , vol.87 , pp. 1116-1119
    • Potocnik, F.C.1    van Rensburg, S.J.2    Park, C.3    Taljaard, J.J.4    Emsley, R.A.5
  • 101
    • 84961432203 scopus 로고
    • Dietary Supplementation with zinc sulphate, sodium selenite and fatty acids in early dementia of Alzheimer's type
    • Van Rhijin A.G., Prior C.A., and Corrigan F.M. Dietary Supplementation with zinc sulphate, sodium selenite and fatty acids in early dementia of Alzheimer's type. J. Nutr. Med. 1 (1990) 259-266
    • (1990) J. Nutr. Med. , vol.1 , pp. 259-266
    • Van Rhijin, A.G.1    Prior, C.A.2    Corrigan, F.M.3
  • 106
    • 33744510885 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing
    • Hu W.P., Chang G.L., Chen S.J., and Kuo Y.M. Kinetic analysis of beta-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing. J. Neurosci. Methods 154 (2006) 190-197
    • (2006) J. Neurosci. Methods , vol.154 , pp. 190-197
    • Hu, W.P.1    Chang, G.L.2    Chen, S.J.3    Kuo, Y.M.4
  • 109
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • Connor J.R., Snyder B.S., Beard J.L., Fine R.E., and Mufson E.J. Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease. J. Neurosci. Res. 31 (1992) 327-335
    • (1992) J. Neurosci. Res. , vol.31 , pp. 327-335
    • Connor, J.R.1    Snyder, B.S.2    Beard, J.L.3    Fine, R.E.4    Mufson, E.J.5
  • 110
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
    • Connor J.R., Menzies S.L., St Martin S.M., and Mufson E.J. A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains. J. Neurosci. Res. 31 (1992) 75-83
    • (1992) J. Neurosci. Res. , vol.31 , pp. 75-83
    • Connor, J.R.1    Menzies, S.L.2    St Martin, S.M.3    Mufson, E.J.4
  • 111
    • 0029433318 scopus 로고
    • Cellular management of iron in the brain
    • (Suppl.)
    • Connor J.R., and Menzies S.L. Cellular management of iron in the brain. J. Neurol. Sci. 134 (1995) 33-44 (Suppl.)
    • (1995) J. Neurol. Sci. , vol.134 , pp. 33-44
    • Connor, J.R.1    Menzies, S.L.2
  • 112
    • 3342880690 scopus 로고    scopus 로고
    • A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism
    • Atamna H., and Frey II W.H. A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 11153-11158
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11153-11158
    • Atamna, H.1    Frey II, W.H.2
  • 114
  • 115
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee J.Y., Cole T.B., Palmiter R.D., Suh S.W., and Koh J.Y. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 7705-7710
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 116
    • 0027476481 scopus 로고
    • Age-related changes in footshock avoidance acquisition and retention in senescence accelerated mouse (SAM)
    • Flood J.F., and Morley J.E. Age-related changes in footshock avoidance acquisition and retention in senescence accelerated mouse (SAM). Neurobiol. Aging 14 (1993) 153-157
    • (1993) Neurobiol. Aging , vol.14 , pp. 153-157
    • Flood, J.F.1    Morley, J.E.2
  • 117
    • 3242715959 scopus 로고    scopus 로고
    • Antisense directed at the Abeta region of APP decreases brain oxidative markers in aged senescence accelerated mice
    • Poon H.F., Joshi G., Sultana R., Farr S.A., Banks W.A., Morley J.E., Calabrese V., and Butterfield D.A. Antisense directed at the Abeta region of APP decreases brain oxidative markers in aged senescence accelerated mice. Brain Res. 1018 (2004) 86-96
    • (2004) Brain Res. , vol.1018 , pp. 86-96
    • Poon, H.F.1    Joshi, G.2    Sultana, R.3    Farr, S.A.4    Banks, W.A.5    Morley, J.E.6    Calabrese, V.7    Butterfield, D.A.8
  • 118
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • Atwood C.S., Scarpa R.C., Huang X., Moir R.D., Jones W.D., Fairlie D.P., Tanzi R.E., and Bush A.I. Characterization of copper interactions with Alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42. J. Neurochem. 75 (2000) 1219-1233
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 119
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S., Beyreuther K., Barrow C.J., Masters C.L., Bush A.I., and Barnham K.J. Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276 (2001) 20466-20473
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 120
    • 16844373633 scopus 로고    scopus 로고
    • N-terminal deletions modify the Cu2+ binding site in amyloid-beta
    • Karr J.W., Akintoye H., Kaupp L.J., and Szalai V.A. N-terminal deletions modify the Cu2+ binding site in amyloid-beta. Biochemistry 44 (2005) 5478-5487
    • (2005) Biochemistry , vol.44 , pp. 5478-5487
    • Karr, J.W.1    Akintoye, H.2    Kaupp, L.J.3    Szalai, V.A.4
  • 121
    • 2442461177 scopus 로고    scopus 로고
    • Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques
    • Syme C.D., Nadal R.C., Rigby S.E., and Viles J.H. Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques. J. Biol. Chem. 279 (2004) 18169-18177
    • (2004) J. Biol. Chem. , vol.279 , pp. 18169-18177
    • Syme, C.D.1    Nadal, R.C.2    Rigby, S.E.3    Viles, J.H.4
  • 122
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes
    • Miura T., Suzuki K., Kohata N., and Takeuchi H. Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes. Biochemistry 39 (2000) 7024-7031
    • (2000) Biochemistry , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 123
    • 12844276303 scopus 로고    scopus 로고
    • Rodent Abeta(1-42) exhibits oxidative stress properties similar to those of human Abeta(1-42): Implications for proposed mechanisms of toxicity
    • Boyd-Kimball D., Sultana R., Mohmmad-Abdul H., and Butterfield D.A. Rodent Abeta(1-42) exhibits oxidative stress properties similar to those of human Abeta(1-42): Implications for proposed mechanisms of toxicity. J. Alzheimer's Dis. 6 (2004) 515-525
    • (2004) J. Alzheimer's Dis. , vol.6 , pp. 515-525
    • Boyd-Kimball, D.1    Sultana, R.2    Mohmmad-Abdul, H.3    Butterfield, D.A.4
  • 124
    • 0036591863 scopus 로고    scopus 로고
    • Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide
    • Kanski J., Aksenova M., Schoneich C., and Butterfield D.A. Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide. Free Radic. Biol. Med. 32 (2002) 1205-1211
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1205-1211
    • Kanski, J.1    Aksenova, M.2    Schoneich, C.3    Butterfield, D.A.4
  • 125
    • 0035997233 scopus 로고    scopus 로고
    • Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide 1-42
    • Butterfield D.A., and Kanski J. Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide 1-42. Peptides 23 (2002) 1299-1309
    • (2002) Peptides , vol.23 , pp. 1299-1309
    • Butterfield, D.A.1    Kanski, J.2
  • 126
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42)
    • discussion 339-342
    • Yatin S.M., Varadarajan S., Link C.D., and Butterfield D.A. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42). Neurobiol. Aging 20 (1999) 325-330 discussion 339-342
    • (1999) Neurobiol. Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4
  • 127
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield D.A. Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radical Res. 36 (2002) 1307-1313
    • (2002) Free Radical Res. , vol.36 , pp. 1307-1313
    • Butterfield, D.A.1
  • 128
    • 1842519391 scopus 로고    scopus 로고
    • Alzheimer's amyloid beta-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide
    • Butterfield D.A., and Bush A.I. Alzheimer's amyloid beta-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol. Aging 25 (2004) 563-568
    • (2004) Neurobiol. Aging , vol.25 , pp. 563-568
    • Butterfield, D.A.1    Bush, A.I.2
  • 129
    • 0036592636 scopus 로고    scopus 로고
    • Amyloid beta-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists
    • Butterfield D.A., Griffin S., Munch G., and Pasinetti G.M. Amyloid beta-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists. J. Alzheimers Dis. 4 (2002) 193-201
    • (2002) J. Alzheimers Dis. , vol.4 , pp. 193-201
    • Butterfield, D.A.1    Griffin, S.2    Munch, G.3    Pasinetti, G.M.4
  • 130
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35)
    • Varadarajan S., Kanski J., Aksenova M., Lauderback C., and Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35). J. Am. Chem. Soc. 123 (2001) 5625-5631
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 133
    • 0035874024 scopus 로고    scopus 로고
    • New evidence that the Alzheimer beta-amyloid peptide does not spontaneously form free radicals: an ESR study using a series of spin-traps
    • Turnbull S., Tabner B.J., El-Agnaf O.M., Twyman L.J., and Allsop D. New evidence that the Alzheimer beta-amyloid peptide does not spontaneously form free radicals: an ESR study using a series of spin-traps. Free Radic. Biol. Med. 30 (2001) 1154-1162
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1154-1162
    • Turnbull, S.1    Tabner, B.J.2    El-Agnaf, O.M.3    Twyman, L.J.4    Allsop, D.5
  • 136
    • 0029866991 scopus 로고    scopus 로고
    • beta-Amyloid toxicity in organotypic hippocampal cultures: protection by EUK-8, a synthetic catalytic free radical scavenger
    • Bruce A.J., Malfroy B., and Baudry M. beta-Amyloid toxicity in organotypic hippocampal cultures: protection by EUK-8, a synthetic catalytic free radical scavenger. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 2312-2316
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 2312-2316
    • Bruce, A.J.1    Malfroy, B.2    Baudry, M.3
  • 137
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J.B., Lesley R., and Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77 (1994) 817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 138
    • 0033430085 scopus 로고    scopus 로고
    • Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown
    • Milton N.G. Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Biochem. J. 344 Pt 2 (1999) 293-296
    • (1999) Biochem. J. , vol.344 , Issue.PART 2 , pp. 293-296
    • Milton, N.G.1
  • 140
    • 0036591852 scopus 로고    scopus 로고
    • Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease
    • Tabner B.J., Turnbull S., El-Agnaf O.M., and Allsop D. Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease. Free Radic. Biol. Med. 32 (2002) 1076-1083
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1076-1083
    • Tabner, B.J.1    Turnbull, S.2    El-Agnaf, O.M.3    Allsop, D.4
  • 141
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W.R. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 23 (1997) 134-147
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 142
    • 0032619789 scopus 로고    scopus 로고
    • The mechanism of "Fenton-like" reactions and their importance for biological systems. A biologist's view
    • Liochev S.I. The mechanism of "Fenton-like" reactions and their importance for biological systems. A biologist's view. Met. Ions Biol. Syst. 36 (1999) 1-39
    • (1999) Met. Ions Biol. Syst. , vol.36 , pp. 1-39
    • Liochev, S.I.1
  • 144
    • 3242715131 scopus 로고    scopus 로고
    • Rapid characterization of amyloid-beta side-chain oxidation by tandem mass spectrometry and the scoring algorithm for spectral analysis
    • Schiewe A.J., Margol L., Soreghan B.A., Thomas S.N., and Yang A.J. Rapid characterization of amyloid-beta side-chain oxidation by tandem mass spectrometry and the scoring algorithm for spectral analysis. Pharm. Res. 21 (2004) 1094-1102
    • (2004) Pharm. Res. , vol.21 , pp. 1094-1102
    • Schiewe, A.J.1    Margol, L.2    Soreghan, B.A.3    Thomas, S.N.4    Yang, A.J.5
  • 145
    • 19444383084 scopus 로고    scopus 로고
    • Abeta(31-35) and Abeta(25-35) fragments of amyloid beta-protein induce cellular death through apoptotic signals: Role of the redox state of methionine-35
    • Clementi M.E., Marini S., Coletta M., Orsini F., Giardina B., and Misiti F. Abeta(31-35) and Abeta(25-35) fragments of amyloid beta-protein induce cellular death through apoptotic signals: Role of the redox state of methionine-35. FEBS Lett. 579 (2005) 2913-2918
    • (2005) FEBS Lett. , vol.579 , pp. 2913-2918
    • Clementi, M.E.1    Marini, S.2    Coletta, M.3    Orsini, F.4    Giardina, B.5    Misiti, F.6
  • 146
    • 2942631225 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces toxic and pro-apoptotic effects of the amyloid beta-protein fragment (31-35) on isolated brain mitochondria
    • Misiti F., Martorana G.E., Nocca G., Di Stasio E., Giardina B., and Clementi M.E. Methionine 35 oxidation reduces toxic and pro-apoptotic effects of the amyloid beta-protein fragment (31-35) on isolated brain mitochondria. Neuroscience 126 (2004) 297-303
    • (2004) Neuroscience , vol.126 , pp. 297-303
    • Misiti, F.1    Martorana, G.E.2    Nocca, G.3    Di Stasio, E.4    Giardina, B.5    Clementi, M.E.6
  • 147
    • 0037117310 scopus 로고    scopus 로고
    • Role of glycine-33 and methionine-35 in Alzheimer's amyloid beta-peptide 1-42-associated oxidative stress and neurotoxicity
    • Kanski J., Varadarajan S., Aksenova M., and Butterfield D.A. Role of glycine-33 and methionine-35 in Alzheimer's amyloid beta-peptide 1-42-associated oxidative stress and neurotoxicity. Biochim. Biophys. Acta 1586 (2002) 190-198
    • (2002) Biochim. Biophys. Acta , vol.1586 , pp. 190-198
    • Kanski, J.1    Varadarajan, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 148
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modelling study
    • Pogocki D., and Schoneich C. Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modelling study. Chem. Res. Toxicol. 15 (2002) 408-418
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 408-418
    • Pogocki, D.1    Schoneich, C.2
  • 151
    • 0027932162 scopus 로고
    • Effect of substance P and protein kinase inhibitors on beta-amyloid peptide-induced proliferation of cultured brain cells
    • Singh V.K., Cheng J.F., and Leu S.J. Effect of substance P and protein kinase inhibitors on beta-amyloid peptide-induced proliferation of cultured brain cells. Brain Res. 660 (1994) 353-356
    • (1994) Brain Res. , vol.660 , pp. 353-356
    • Singh, V.K.1    Cheng, J.F.2    Leu, S.J.3
  • 152
    • 0026783914 scopus 로고
    • In vivo effects of beta-amyloid implants in rodents: lack of potentiation of damage associated with transient global forebrain ischemia
    • Stephenson D.T., and Clemens J.A. In vivo effects of beta-amyloid implants in rodents: lack of potentiation of damage associated with transient global forebrain ischemia. Brain Res. 586 (1992) 235-246
    • (1992) Brain Res. , vol.586 , pp. 235-246
    • Stephenson, D.T.1    Clemens, J.A.2
  • 153
    • 0029144218 scopus 로고
    • beta-Amyloid peptide, substance P, and SEC receptor ligand activate cytoplasmic Ca2+ in neutrophil-like HL-60 cells: effect of chemotactic peptide antagonist BocMLF
    • Takenouchi T., and Munekata E. beta-Amyloid peptide, substance P, and SEC receptor ligand activate cytoplasmic Ca2+ in neutrophil-like HL-60 cells: effect of chemotactic peptide antagonist BocMLF. Peptides 16 (1995) 1019-1024
    • (1995) Peptides , vol.16 , pp. 1019-1024
    • Takenouchi, T.1    Munekata, E.2
  • 154
    • 0025095256 scopus 로고
    • Beta-amyloid protein promotes neuritic branching in hippocampal cultures
    • Whitson J.S., Glabe C.G., Shintani E., Abcar A., and Cotman C.W. Beta-amyloid protein promotes neuritic branching in hippocampal cultures. Neurosci. Lett. 110 (1990) 319-324
    • (1990) Neurosci. Lett. , vol.110 , pp. 319-324
    • Whitson, J.S.1    Glabe, C.G.2    Shintani, E.3    Abcar, A.4    Cotman, C.W.5
  • 155
    • 0024543836 scopus 로고
    • Amyloid beta protein enhances the survival of hippocampal neurons in vitro
    • Whitson J.S., Selkoe D.J., and Cotman C.W. Amyloid beta protein enhances the survival of hippocampal neurons in vitro. Science 243 (1989) 1488-1490
    • (1989) Science , vol.243 , pp. 1488-1490
    • Whitson, J.S.1    Selkoe, D.J.2    Cotman, C.W.3
  • 156
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., and Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science 250 (1990) 279-282
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 157
    • 0027166738 scopus 로고
    • Amyloid beta peptides act directly on single neurons
    • Simmons M.A., and Schneider C.R. Amyloid beta peptides act directly on single neurons. Neurosci. Lett. 150 (1993) 133-136
    • (1993) Neurosci. Lett. , vol.150 , pp. 133-136
    • Simmons, M.A.1    Schneider, C.R.2
  • 158
    • 0028331604 scopus 로고
    • Amyloid beta protein-induced neuronal cell death: neurotoxic properties of aggregated amyloid beta protein
    • Ueda K., Fukui Y., and Kageyama H. Amyloid beta protein-induced neuronal cell death: neurotoxic properties of aggregated amyloid beta protein. Brain Res. 639 (1994) 240-244
    • (1994) Brain Res. , vol.639 , pp. 240-244
    • Ueda, K.1    Fukui, Y.2    Kageyama, H.3
  • 160
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • Pike C.J., Walencewicz A.J., Glabe C.G., and Cotman C.W. Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures. Eur. J. Pharmacol. 207 (1991) 367-368
    • (1991) Eur. J. Pharmacol. , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 161
    • 0028207907 scopus 로고
    • Amyloid beta peptide induces necrosis rather than apoptosis
    • Behl C., Davis J.B., Klier F.G., and Schubert D. Amyloid beta peptide induces necrosis rather than apoptosis. Brain Res. 645 (1994) 253-264
    • (1994) Brain Res. , vol.645 , pp. 253-264
    • Behl, C.1    Davis, J.B.2    Klier, F.G.3    Schubert, D.4
  • 162
    • 20444479483 scopus 로고    scopus 로고
    • Amyloid-beta in Alzheimer's disease: the horse or the cart? Pathogenic or protective?
    • Lee H.G., Castellani R.J., Zhu X., Perry G., and Smith M.A. Amyloid-beta in Alzheimer's disease: the horse or the cart? Pathogenic or protective?. Int. J. Exp. Pathol. 86 (2005) 133-138
    • (2005) Int. J. Exp. Pathol. , vol.86 , pp. 133-138
    • Lee, H.G.1    Castellani, R.J.2    Zhu, X.3    Perry, G.4    Smith, M.A.5
  • 165
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging
    • Wang J., Dickson D.W., Trojanowski J.Q., and Lee V.M. The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging. Exp. Neurol. 158 (1999) 328-337
    • (1999) Exp. Neurol. , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 166
    • 0032498829 scopus 로고    scopus 로고
    • Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition
    • Koppal T., Subramaniam R., Drake J., Prasad M.R., Dhillon H., and Butterfield D.A. Vitamin E protects against Alzheimer's amyloid peptide (25-35)-induced changes in neocortical synaptosomal membrane lipid structure and composition. Brain Res. 786 (1998) 270-273
    • (1998) Brain Res. , vol.786 , pp. 270-273
    • Koppal, T.1    Subramaniam, R.2    Drake, J.3    Prasad, M.R.4    Dhillon, H.5    Butterfield, D.A.6
  • 167
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: tools, targets, and reversal
    • Vogt W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic. Biol. Med. 18 (1995) 93-105
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 169
    • 0032880901 scopus 로고    scopus 로고
    • Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress
    • Varadarajan S., Yatin S., Kanski J., Jahanshahi F., and Butterfield D.A. Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress. Brain Res. Bull. 50 (1999) 133-141
    • (1999) Brain Res. Bull. , vol.50 , pp. 133-141
    • Varadarajan, S.1    Yatin, S.2    Kanski, J.3    Jahanshahi, F.4    Butterfield, D.A.5
  • 170
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X., and Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402 (1999) 47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 171
    • 0034638379 scopus 로고    scopus 로고
    • Is oxidative damage mediated by amyoid beta and prion peptide mediated by hydrogen atom transfer from glycine alpha-carbon to methionine sulfur within beta-sheets?
    • Rauk A., Armstrong D.A., and Fairlie D.P. Is oxidative damage mediated by amyoid beta and prion peptide mediated by hydrogen atom transfer from glycine alpha-carbon to methionine sulfur within beta-sheets?. J. Am. Chem. Soc. 122 (2000) 9761-9767
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9761-9767
    • Rauk, A.1    Armstrong, D.A.2    Fairlie, D.P.3
  • 172
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease
    • Lovell M.A., Ehmann W.D., Mattson M.P., and Markesbery W.R. Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease. Neurobiol. Aging 18 (1997) 457-461
    • (1997) Neurobiol. Aging , vol.18 , pp. 457-461
    • Lovell, M.A.1    Ehmann, W.D.2    Mattson, M.P.3    Markesbery, W.R.4
  • 173
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11 (1991) 81-128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 174
    • 33745850084 scopus 로고    scopus 로고
    • Peroxyl radicals: inductors of neurodegenerative and other inflammatory diseases. Their origin and how they transform cholesterol, phospholipids, plasmalogens, polyunsaturated fatty acids, sugars, and proteins into deleterious products
    • Spiteller G. Peroxyl radicals: inductors of neurodegenerative and other inflammatory diseases. Their origin and how they transform cholesterol, phospholipids, plasmalogens, polyunsaturated fatty acids, sugars, and proteins into deleterious products. Free Radic. Biol. Med. 41 (2006) 362-387
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 362-387
    • Spiteller, G.1
  • 175
    • 0037205434 scopus 로고    scopus 로고
    • Oxidation of methionine 35 attenuates formation of amyloid beta -peptide 1-40 oligomers
    • Palmblad M., Westlind-Danielsson A., and Bergquist J. Oxidation of methionine 35 attenuates formation of amyloid beta -peptide 1-40 oligomers. J. Biol. Chem. 277 (2002) 19506-19510
    • (2002) J. Biol. Chem. , vol.277 , pp. 19506-19510
    • Palmblad, M.1    Westlind-Danielsson, A.2    Bergquist, J.3
  • 176
    • 0344687267 scopus 로고    scopus 로고
    • Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide
    • Ali F.E., Barnham K.J., Barrow C.J., and Separovic F. Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide. J. Inorg. Biochem. 98 (2004) 173-184
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 173-184
    • Ali, F.E.1    Barnham, K.J.2    Barrow, C.J.3    Separovic, F.4
  • 178
    • 0032422401 scopus 로고    scopus 로고
    • Immunohistochemical and ELISA assays for biomarkers of oxidative stress in aging and disease
    • Onorato J.M., Thorpe S.R., and Baynes J.W. Immunohistochemical and ELISA assays for biomarkers of oxidative stress in aging and disease. Ann. N. Y. Acad. Sci. 854 (1998) 277-290
    • (1998) Ann. N. Y. Acad. Sci. , vol.854 , pp. 277-290
    • Onorato, J.M.1    Thorpe, S.R.2    Baynes, J.W.3
  • 180
    • 0031985973 scopus 로고    scopus 로고
    • Molecular mechanisms of cellular injury produced by neurotoxic amino acids that generate reactive oxygen species
    • Metodiewa D. Molecular mechanisms of cellular injury produced by neurotoxic amino acids that generate reactive oxygen species. Amino Acids 14 (1998) 181-187
    • (1998) Amino Acids , vol.14 , pp. 181-187
    • Metodiewa, D.1
  • 181
    • 0033521095 scopus 로고    scopus 로고
    • Mass spectrometric quantification of 3-nitrotyrosine, ortho-tyrosine, and o,o′-dityrosine in brain tissue of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine-treated mice, a model of oxidative stress in Parkinson's disease
    • Pennathur S., Jackson-Lewis V., Przedborski S., and Heinecke J.W. Mass spectrometric quantification of 3-nitrotyrosine, ortho-tyrosine, and o,o′-dityrosine in brain tissue of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine-treated mice, a model of oxidative stress in Parkinson's disease. J. Biol. Chem. 274 (1999) 34621-34628
    • (1999) J. Biol. Chem. , vol.274 , pp. 34621-34628
    • Pennathur, S.1    Jackson-Lewis, V.2    Przedborski, S.3    Heinecke, J.W.4
  • 182
    • 0346100519 scopus 로고    scopus 로고
    • Dityrosine as a product of oxidative stress and fluorescent probe
    • Malencik D.A., and Anderson S.R. Dityrosine as a product of oxidative stress and fluorescent probe. Amino Acids 25 (2003) 233-247
    • (2003) Amino Acids , vol.25 , pp. 233-247
    • Malencik, D.A.1    Anderson, S.R.2
  • 185
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 186
    • 16544373763 scopus 로고    scopus 로고
    • Gossypin protects primary cultured rat cortical cells from oxidative stress- and beta-amyloid-induced toxicity
    • Yoon I., Lee K.H., and Cho J. Gossypin protects primary cultured rat cortical cells from oxidative stress- and beta-amyloid-induced toxicity. Arch. Pharm. Res. 27 (2004) 454-459
    • (2004) Arch. Pharm. Res. , vol.27 , pp. 454-459
    • Yoon, I.1    Lee, K.H.2    Cho, J.3
  • 187
    • 0041589063 scopus 로고    scopus 로고
    • Melatonin prevents free radical formation due to the interaction between beta-amyloid peptides and metal ions [Al(III), Zn(II), Cu(II), Mn(II), Fe(II)]
    • Zatta P., Tognon G., and Carampin P. Melatonin prevents free radical formation due to the interaction between beta-amyloid peptides and metal ions [Al(III), Zn(II), Cu(II), Mn(II), Fe(II)]. J. Pineal. Res. 35 (2003) 98-103
    • (2003) J. Pineal. Res. , vol.35 , pp. 98-103
    • Zatta, P.1    Tognon, G.2    Carampin, P.3
  • 188
    • 4344568620 scopus 로고    scopus 로고
    • Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease
    • Feng Z., Chang Y., Cheng Y., Zhang B.L., Qu Z.W., Qin C., and Zhang J.T. Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease. J. Pineal. Res. 37 (2004) 129-136
    • (2004) J. Pineal. Res. , vol.37 , pp. 129-136
    • Feng, Z.1    Chang, Y.2    Cheng, Y.3    Zhang, B.L.4    Qu, Z.W.5    Qin, C.6    Zhang, J.T.7
  • 190
    • 31644432763 scopus 로고    scopus 로고
    • Beneficial effects of melatonin in experimental models of Alzheimer disease
    • Cheng Y., Feng Z., Zhang Q.Z., and Zhang J.T. Beneficial effects of melatonin in experimental models of Alzheimer disease. Acta Pharmacol. Sin. 27 (2006) 129-139
    • (2006) Acta Pharmacol. Sin. , vol.27 , pp. 129-139
    • Cheng, Y.1    Feng, Z.2    Zhang, Q.Z.3    Zhang, J.T.4
  • 191
    • 0036451982 scopus 로고    scopus 로고
    • Bilobalide and neuroprotection
    • Defeudis F.V. Bilobalide and neuroprotection. Pharmacol. Res. 46 (2002) 565-568
    • (2002) Pharmacol. Res. , vol.46 , pp. 565-568
    • Defeudis, F.V.1
  • 192
    • 0031788259 scopus 로고    scopus 로고
    • The efficacy of Ginkgo biloba on cognitive function in Alzheimer disease
    • Oken B.S., Storzbach D.M., and Kaye J.A. The efficacy of Ginkgo biloba on cognitive function in Alzheimer disease. Arch. Neurol. 55 (1998) 1409-1415
    • (1998) Arch. Neurol. , vol.55 , pp. 1409-1415
    • Oken, B.S.1    Storzbach, D.M.2    Kaye, J.A.3
  • 193
    • 0041825230 scopus 로고    scopus 로고
    • Response patterns of EGb 761 in Alzheimer's disease: influence of neuropsychological profiles
    • Le Bars P.L. Response patterns of EGb 761 in Alzheimer's disease: influence of neuropsychological profiles. Pharmacopsychiatry 36 Suppl. 1 (2003) S50-S55
    • (2003) Pharmacopsychiatry , vol.36 , Issue.SUPPL. 1
    • Le Bars, P.L.1
  • 194
    • 28244446721 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled trial of two doses of Ginkgo biloba extract in dementia of the Alzheimer's type
    • Schneider L.S., DeKosky S.T., Farlow M.R., Tariot P.N., Hoerr R., and Kieser M. A randomized, double-blind, placebo-controlled trial of two doses of Ginkgo biloba extract in dementia of the Alzheimer's type. Curr. Alzheimer Res. 2 (2005) 541-551
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 541-551
    • Schneider, L.S.1    DeKosky, S.T.2    Farlow, M.R.3    Tariot, P.N.4    Hoerr, R.5    Kieser, M.6
  • 195
    • 0035910374 scopus 로고    scopus 로고
    • The Ginkgo biloba extract EGb 761 rescues the PC12 neuronal cells from beta-amyloid-induced cell death by inhibiting the formation of beta-amyloid-derived diffusible neurotoxic ligands
    • Yao Z., and Papadopoulos Drieu.V. The Ginkgo biloba extract EGb 761 rescues the PC12 neuronal cells from beta-amyloid-induced cell death by inhibiting the formation of beta-amyloid-derived diffusible neurotoxic ligands. Brain Res. 889 (2001) 181-190
    • (2001) Brain Res. , vol.889 , pp. 181-190
    • Yao, Z.1    Papadopoulos, Drieu.V.2
  • 199
    • 0035917819 scopus 로고    scopus 로고
    • Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease
    • Aksenov M.Y., and Markesbery W.R. Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease. Neurosci. Lett. 302 (2001) 141-145
    • (2001) Neurosci. Lett. , vol.302 , pp. 141-145
    • Aksenov, M.Y.1    Markesbery, W.R.2
  • 202
    • 4644275696 scopus 로고    scopus 로고
    • Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models
    • (discussion 443-369)
    • Baum L., and Ng A. Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models. J. Alzheimers Dis. 6 (2004) 367-377 (discussion 443-369)
    • (2004) J. Alzheimers Dis. , vol.6 , pp. 367-377
    • Baum, L.1    Ng, A.2
  • 203
    • 7444249085 scopus 로고
    • The biochemistry of desferrioxamine and its relation to iron metabolism
    • Keberle H. The biochemistry of desferrioxamine and its relation to iron metabolism. Ann. N. Y. Acad. Sci. 119 (1964) 758-768
    • (1964) Ann. N. Y. Acad. Sci. , vol.119 , pp. 758-768
    • Keberle, H.1
  • 205
    • 33646180185 scopus 로고    scopus 로고
    • Aluminum in hippocampal neurons from humans with Alzheimer's disease
    • Walton J.R. Aluminum in hippocampal neurons from humans with Alzheimer's disease. Neurotoxicology 27 (2006) 385-394
    • (2006) Neurotoxicology , vol.27 , pp. 385-394
    • Walton, J.R.1
  • 206
    • 0022363156 scopus 로고
    • New insights into the nature of senile (Alzheimer-type) plaques
    • Perry E.K., and Perry R.H. New insights into the nature of senile (Alzheimer-type) plaques. Trends Neurosci. 8 (1985) 301-303
    • (1985) Trends Neurosci. , vol.8 , pp. 301-303
    • Perry, E.K.1    Perry, R.H.2
  • 207
    • 0018827099 scopus 로고
    • Alzheimer's disease: X-ray spectrometric evidence of aluminum accumulation in neurofibrillary tangle-bearing neurons
    • Perl D.P., and Brody A.R. Alzheimer's disease: X-ray spectrometric evidence of aluminum accumulation in neurofibrillary tangle-bearing neurons. Science 208 (1980) 297-299
    • (1980) Science , vol.208 , pp. 297-299
    • Perl, D.P.1    Brody, A.R.2
  • 208
    • 0027518294 scopus 로고
    • Laser microprobe analysis of brain aluminum in Alzheimer's disease
    • Lovell M.A., Ehmann W.D., and Markesbery W.R. Laser microprobe analysis of brain aluminum in Alzheimer's disease. Ann. Neurol. 33 (1993) 36-42
    • (1993) Ann. Neurol. , vol.33 , pp. 36-42
    • Lovell, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 209
    • 32444450650 scopus 로고    scopus 로고
    • Effects of aluminum on the nervous system and its possible link with neurodegenerative diseases
    • (discussion 209-115)
    • Kawahara M. Effects of aluminum on the nervous system and its possible link with neurodegenerative diseases. J. Alzheimers Dis. 8 (2005) 171-182 (discussion 209-115)
    • (2005) J. Alzheimers Dis. , vol.8 , pp. 171-182
    • Kawahara, M.1
  • 210
    • 33646490404 scopus 로고    scopus 로고
    • 1,1′-Xylyl bis-1,4,8,11-tetraaza cyclotetradecane: a new potential copper chelator agent for neuroprotection in Alzheimer's disease. Its comparative effects with clioquinol on rat brain copper distribution
    • Moret V., Laras Y., Pietrancosta N., Garino C., Quelever G., Rolland A., Mallet B., Norreel J.C., and Kraus J.L. 1,1′-Xylyl bis-1,4,8,11-tetraaza cyclotetradecane: a new potential copper chelator agent for neuroprotection in Alzheimer's disease. Its comparative effects with clioquinol on rat brain copper distribution. Bioorg. Med. Chem. Lett. 16 (2006) 3298-3301
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 3298-3301
    • Moret, V.1    Laras, Y.2    Pietrancosta, N.3    Garino, C.4    Quelever, G.5    Rolland, A.6    Mallet, B.7    Norreel, J.C.8    Kraus, J.L.9
  • 211
    • 4644238758 scopus 로고    scopus 로고
    • The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice
    • Lee J.Y., Friedman J.E., Angel I., Kozak A., and Koh J.Y. The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice. Neurobiol. Aging 25 (2004) 1315-1321
    • (2004) Neurobiol. Aging , vol.25 , pp. 1315-1321
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3    Kozak, A.4    Koh, J.Y.5
  • 213
    • 33644843098 scopus 로고    scopus 로고
    • In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid beta-peptide (1-42)-induced oxidative stress
    • Perluigi M., Joshi G., Sultana R., Calabrese V., De Marco C., Coccia R., and Butterfield D.A. In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid beta-peptide (1-42)-induced oxidative stress. Neuroscience 138 (2006) 1161-1170
    • (2006) Neuroscience , vol.138 , pp. 1161-1170
    • Perluigi, M.1    Joshi, G.2    Sultana, R.3    Calabrese, V.4    De Marco, C.5    Coccia, R.6    Butterfield, D.A.7
  • 214
    • 0015907827 scopus 로고
    • [Long-term follow-up following anastomosis of the superior vena cava and pulmonary artery]
    • Nakae S., Iwa T., Asai Y., Anjiki H., and Kameta Y. [Long-term follow-up following anastomosis of the superior vena cava and pulmonary artery]. Nippon Kyobu Geka Gakkai Zasshi 21 (1973) 530-537
    • (1973) Nippon Kyobu Geka Gakkai Zasshi , vol.21 , pp. 530-537
    • Nakae, S.1    Iwa, T.2    Asai, Y.3    Anjiki, H.4    Kameta, Y.5
  • 215
    • 0033974529 scopus 로고    scopus 로고
    • Changes in uptake of vitamin B(12) and trace metals in brains of mice treated with clioquinol
    • Yassin M.S., Ekblom J., Xilinas M., Gottfries C.G., and Oreland L. Changes in uptake of vitamin B(12) and trace metals in brains of mice treated with clioquinol. J. Neurol. Sci. 173 (2000) 40-44
    • (2000) J. Neurol. Sci. , vol.173 , pp. 40-44
    • Yassin, M.S.1    Ekblom, J.2    Xilinas, M.3    Gottfries, C.G.4    Oreland, L.5
  • 217
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-beta precursor protein: integrating structure with biological function
    • Reinhard C., Hebert S.S., and De Strooper B. The amyloid-beta precursor protein: integrating structure with biological function. EMBO J. 24 (2005) 3996-4006
    • (2005) EMBO J. , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.