메뉴 건너뛰기




Volumn 14, Issue 11, 2010, Pages 1177-1197

Novel drug targets based on metallobiology of Alzheimer's disease

Author keywords

A ; APP; Iron responsive element; Metal chelators; Screening

Indexed keywords

1 (BENZIMIDAZOLE 2 YLMETHYL) 1,4,7 TRIAZACYCLONONANE; 1,4 BIS(BENZIMIDAZOLE 2 YLMETHYL) 1,4,7 TRIAZACYCLONONE); 2 METHYL 5 (3,4,5 TRIMETHOXYBENZAMIDO)DECAHYDROISOQUINOLINE; 5 (4 PROPARGYLPIPERAZIN 1 YLMETHYL) 8 HYDROXYQUINOLINE; 5 (N METHYL N PROPARGYLAMINOMETHYL) 8 HYDROXYQUINOLINE; 6 HYDROXYMELATONIN; ALPHA TOCOPHEROL; ALUMINUM; AMYLOID BETA PROTEIN; ASCORBIC ACID; CLIOQUINOL; COPPER; CURCUMIN; DEFEROXAMINE; DP 109; EPIGALLOCATECHIN GALLATE; GOSSYPINE; HLA 20; IRON; KAEMPFEROL; M 30A; NOOTROPIC AGENT; PBT 2; PENICILLAMINE; QUINOLINE DERIVATIVE; RASAGILINE; RESVERATROL; SELEGILINE; TACRINE; UNCLASSIFIED DRUG; VK 28; ZINC;

EID: 77958046282     PISSN: 14728222     EISSN: None     Source Type: Journal    
DOI: 10.1517/14728222.2010.525352     Document Type: Review
Times cited : (53)

References (228)
  • 1
    • 77951782384 scopus 로고    scopus 로고
    • Current therapeutic targets for the treatment of Alzheimer's disease
    • Grill JD, Cummings JL. Current therapeutic targets for the treatment of Alzheimer's disease. Expert Rev Neurother 2010;10:711-728
    • (2010) Expert Rev Neurother , vol.10 , pp. 711-728
    • Grill, J.D.1    Cummings, J.L.2
  • 2
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: A multifactorial view on the disease process
    • De Strooper B. Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process. Physiol Rev 2010;90:465-494
    • (2010) Physiol Rev , vol.90 , pp. 465-494
    • De Strooper, B.1
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002;297:353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 77953886784 scopus 로고    scopus 로고
    • Current status on Alzheimer disease molecular genetics: From past, to present, to future
    • Bettens K, Sleegers K, Van Broeckhoven C. Current status on Alzheimer disease molecular genetics: from past, to present, to future. Hum Mol Genet 2010;19(R1):R4-11
    • (2010) Hum Mol Genet , vol.19 , Issue.R1
    • Bettens, K.1    Sleegers, K.2    Vanbroeckhoven, C.3
  • 5
    • 46749100924 scopus 로고    scopus 로고
    • Therapeutics for Alzheimer's disease based on the metal hypothesis
    • Bush AI, Tanzi RE. Therapeutics for Alzheimer's disease based on the metal hypothesis. Neurotherapeutics 2008;5:421-432
    • (2008) Neurotherapeutics , vol.5 , pp. 421-432
    • Bush, A.I.1    Tanzi, R.E.2
  • 6
    • 0032507975 scopus 로고    scopus 로고
    • Copper, iron and zinc in Alzheimer's disease senile plaques
    • Lovell MA, Robertson JD, Teesdale WJ, et al. Copper, iron and zinc in Alzheimer's disease senile plaques. J Neurol Sci 1998;158:47-52
    • (1998) J Neurol Sci , vol.158 , pp. 47-52
    • Lovell, M.A.1    Robertson, J.D.2    Teesdale, W.J.3
  • 7
    • 33745112857 scopus 로고    scopus 로고
    • Metal exposure and Alzheimer's pathogenesis
    • Liu G, Huang W, Moir RD, et al. Metal exposure and Alzheimer's pathogenesis. J Struct Biol 2006;155:45-51
    • (2006) J Struct Biol , vol.155 , pp. 45-51
    • Liu, G.1    Huang, W.2    Moir, R.D.3
  • 8
    • 59149101704 scopus 로고    scopus 로고
    • Iron and the translation of the amyloid precursor protein (APP) and ferritin mRNAs: Riboregulation against neural oxidative damage in Alzheimer's disease
    • Rogers JT, Bush AI, Cho HH, et al. Iron and the translation of the amyloid precursor protein (APP) and ferritin mRNAs: riboregulation against neural oxidative damage in Alzheimer's disease. Biochem Soc Trans 2008;36:1282-1287
    • (2008) Biochem Soc Trans , vol.36 , pp. 1282-1287
    • Rogers, J.T.1    Bush, A.I.2    Cho, H.H.3
  • 9
    • 67651020783 scopus 로고    scopus 로고
    • Amyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease
    • Leskovjan AC, Lanzirotti A, Miller LM. Amyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease. Neuroimage 2009;47:1215-1220
    • (2009) Neuroimage , vol.47 , pp. 1215-1220
    • Leskovjan, A.C.1    Lanzirotti, A.2    Miller, L.M.3
  • 10
    • 23744431884 scopus 로고    scopus 로고
    • Immersion autometallographic tracing of zinc ions in Alzheimer beta-amyloid plaques
    • Stoltenberg M, Bruhn M, Sondergaard C, et al. Immersion autometallographic tracing of zinc ions in Alzheimer beta-amyloid plaques. Histochem Cell Biol 2005;123:605-611
    • (2005) Histochem Cell Biol , vol.123 , pp. 605-611
    • Stoltenberg, M.1    Bruhn, M.2    Sondergaard, C.3
  • 11
    • 0030804608 scopus 로고    scopus 로고
    • Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains: A proton-induced X-ray emission spectroscopic analysis of cryostat sections from autopsy material
    • Danscher G, Jensen KB, Frederickson CJ, et al. Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains: a proton-induced X-ray emission spectroscopic analysis of cryostat sections from autopsy material. J Neurosci Methods 1997;76:53-59
    • (1997) J Neurosci Methods , vol.76 , pp. 53-59
    • Danscher, G.1    Jensen, K.B.2    Frederickson, C.J.3
  • 12
    • 33745004381 scopus 로고    scopus 로고
    • Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease
    • Miller LM, Wang Q, Telivala TP, et al. Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease. J Struct Biol 2006;155:30-37
    • (2006) J Struct Biol , vol.155 , pp. 30-37
    • Miller, L.M.1    Wang, Q.2    Telivala, T.P.3
  • 13
    • 56549108452 scopus 로고    scopus 로고
    • A comparison of rapid-scanning X-ray fluorescence mapping and magnetic resonance imaging to localize brain iron distribution
    • McCrea RP, Harder SL, Martin M, et al. A comparison of rapid-scanning X-ray fluorescence mapping and magnetic resonance imaging to localize brain iron distribution. Eur J Radiol 2008;68:S109-13
    • (2008) Eur J Radiol , vol.68
    • McCrea, R.P.1    Harder, S.L.2    Martin, M.3
  • 14
    • 0028323318 scopus 로고
    • In vivo evaluation of brain iron in Alzheimer's disease and normal subjects using MRI
    • Bartzokis G, Sultzer D, Mintz J, et al. In vivo evaluation of brain iron in Alzheimer's disease and normal subjects using MRI. Biol Psychiatry 1994;35:480-487
    • (1994) Biol Psychiatry , vol.35 , pp. 480-487
    • Bartzokis, G.1    Sultzer, D.2    Mintz, J.3
  • 15
    • 0036724204 scopus 로고    scopus 로고
    • Iron (III) induces aggregation of hyperphosphorylated t and its reduction to iron (II) reverses the aggregation: Implications in the formation of neurofibrillary tangles of Alzheimer's disease
    • Yamamoto A, Shin RW, Hasegawa K, et al. Iron (III) induces aggregation of hyperphosphorylated t and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease. J Neurochem 2002;82:1137-1147
    • (2002) J Neurochem , vol.82 , pp. 1137-1147
    • Yamamoto, A.1    Shin, R.W.2    Hasegawa, K.3
  • 16
    • 61349110122 scopus 로고    scopus 로고
    • Chronic copper exposure exacerbates both amyloid and tau pathology and selectively dysregulates cdk5 in a mouse model of AD
    • Kitazawa M, Cheng D, Laferla FM. Chronic copper exposure exacerbates both amyloid and tau pathology and selectively dysregulates cdk5 in a mouse model of AD. J Neurochem 2009;108:1550-1560
    • (2009) J Neurochem , vol.108 , pp. 1550-1560
    • Kitazawa, M.1    Cheng, D.2    Laferla, F.M.3
  • 17
    • 16344379032 scopus 로고    scopus 로고
    • Characterization of the APP proximal promoter and 5¢-untranslated regions: Identification of cell type-specific domains and implications in APP gene expression and Alzheimer's disease
    • Lahiri DK, Ge YW, Maloney B. Characterization of the APP proximal promoter and 5¢-untranslated regions: identification of cell type-specific domains and implications in APP gene expression and Alzheimer's disease. FASEB J 2005;19:653-655
    • (2005) FASEB J , vol.19 , pp. 653-655
    • Lahiri, D.K.1    Ge, Y.W.2    Maloney, B.3
  • 18
    • 9444239191 scopus 로고    scopus 로고
    • Presence of a "cAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: Implications in Alzheimer's disease
    • Maloney B, Ge YW, Greig N, Lahiri DK. Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease. FASEB J 2004;18:1288-1290
    • (2004) FASEB J , vol.18 , pp. 1288-1290
    • Maloney, B.1    Ge, Y.W.2    Greig, N.3    Lahiri, D.K.4
  • 19
    • 34248577510 scopus 로고    scopus 로고
    • Metal specificity of an iron-responsive element in Alzheimer's APP mRNA 5¢untranslated region, tolerance of SH-SY5Y and H4 neural cells to desferrioxamine, clioquinol, VK-28, and a piperazine chelator
    • Bandyopadhyay S, Huang X, Cho H, et al. Metal specificity of an iron-responsive element in Alzheimer's APP mRNA 5¢untranslated region, tolerance of SH-SY5Y and H4 neural cells to desferrioxamine, clioquinol, VK-28, and a piperazine chelator. J Neural Transm Suppl 2006;71:237-247
    • (2006) J Neural Transm Suppl , vol.71 , pp. 237-247
    • Bandyopadhyay, S.1    Huang, X.2    Cho, H.3
  • 20
    • 54049133647 scopus 로고    scopus 로고
    • A potential pathogenetic role of iron in Alzheimer's disease
    • Silvestri L, Camaschella C. A potential pathogenetic role of iron in Alzheimer's disease. J Cell Mol Med 2008;12:1548-1550
    • (2008) J Cell Mol Med , vol.12 , pp. 1548-1550
    • Silvestri, L.1    Camaschella, C.2
  • 21
    • 0037474331 scopus 로고    scopus 로고
    • Cytosolic aconitase and ferritin are regulated by iron in Caenorhabditis elegans
    • Gourley BL, Parker SB, Jones BJ, et al. Cytosolic aconitase and ferritin are regulated by iron in Caenorhabditis elegans. J Biol Chem 2003;278:3227-3234
    • (2003) J Biol Chem , vol.278 , pp. 3227-3234
    • Gourley, B.L.1    Parker, S.B.2    Jones, B.J.3
  • 22
    • 0032579795 scopus 로고    scopus 로고
    • Abnormal localization of iron regulatory protein in Alzheimer's disease
    • Smith MA, Wehr K, Harris PL, et al. Abnormal localization of iron regulatory protein in Alzheimer's disease. Brain Res 1998;788:232-236
    • (1998) Brain Res , vol.788 , pp. 232-236
    • Smith, M.A.1    Wehr, K.2    Harris, P.L.3
  • 23
    • 0033525735 scopus 로고    scopus 로고
    • Translation of the alzheimer amyloid precursor protein mRNA is up-regulated by interleukin-1 through 5¢-untranslated region sequences
    • Rogers JT, Leiter LM, McPhee J, et al. Translation of the alzheimer amyloid precursor protein mRNA is up-regulated by interleukin-1 through 5¢-untranslated region sequences. J Biol Chem 1999;274:6421-6431
    • (1999) J Biol Chem , vol.274 , pp. 6421-6431
    • Rogers, J.T.1    Leiter, L.M.2    McPhee, J.3
  • 24
    • 0347928847 scopus 로고    scopus 로고
    • An iron-responsive element type II in the 5¢-untranslated region of the Alzheimer's amyloid precursor protein transcript
    • Rogers JT, Randall JD, Cahill CM, et al. An iron-responsive element type II in the 5¢-untranslated region of the Alzheimer's amyloid precursor protein transcript. J Biol Chem 2002;277:45518-45528
    • (2002) J Biol Chem , vol.277 , pp. 45518-45528
    • Rogers, J.T.1    Randall, J.D.2    Cahill, C.M.3
  • 25
    • 0036845563 scopus 로고    scopus 로고
    • Polymorphisms in the promoter of the human APP gene: Functional evaluation and allele frequencies in Alzheimer disease
    • Athan ES, Lee JH, Arriaga A, et al. Polymorphisms in the promoter of the human APP gene: functional evaluation and allele frequencies in Alzheimer disease. Arch Neurol 2002;59:1793-1799
    • (2002) Arch Neurol , vol.59 , pp. 1793-1799
    • Athan, E.S.1    Lee, J.H.2    Arriaga, A.3
  • 26
    • 0029935613 scopus 로고    scopus 로고
    • Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin
    • Jefferies WA, Food MR, Gabathuler R, et al. Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin. Brain Res 1996;712:122-126
    • (1996) Brain Res , vol.712 , pp. 122-126
    • Jefferies, W.A.1    Food, M.R.2    Gabathuler, R.3
  • 27
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
    • Connor JR, Menzies SL, St Martin SM, Mufson EJ. A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains. J Neurosci Res 1992;31:75-83
    • (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
  • 28
    • 0025648873 scopus 로고
    • Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia
    • Grundke-Iqbal I, Fleming J, Tung YC, et al. Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia. Acta Neuropathol 1990;81:105-110
    • (1990) Acta Neuropathol , vol.81 , pp. 105-110
    • Grundke-Iqbal, I.1    Fleming, J.2    Tung, Y.C.3
  • 29
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • Sayre LM, Perry G, Harris PL, et al. In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J Neurochem 2000;74:270-279
    • (2000) J Neurochem , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.3
  • 30
    • 2142828035 scopus 로고    scopus 로고
    • Alterations in the interaction between iron regulatory proteins and their iron responsive element in normal and Alzheimer's diseased brains
    • Pinero DJ, Hu J, Connor JR. Alterations in the interaction between iron regulatory proteins and their iron responsive element in normal and Alzheimer's diseased brains. Cell Mol Biol (Noisy-le-grand) 2000;46:761-776
    • (2000) Cell Mol Biol (Noisy-le-grand) , vol.46 , pp. 761-776
    • Pinero, D.J.1    Hu, J.2    Connor, J.R.3
  • 31
    • 1942469548 scopus 로고    scopus 로고
    • Synergy between the C2 allele of transferrin and the C282Y allele of the haemochromatosis gene (HFE) as risk factors for developing Alzheimer's disease
    • Robson KJ, Lehmann DJ, Wimhurst VL, et al. Synergy between the C2 allele of transferrin and the C282Y allele of the haemochromatosis gene (HFE) as risk factors for developing Alzheimer's disease. J Med Genet 2004;41:261-265
    • (2004) J Med Genet , vol.41 , pp. 261-265
    • Robson, K.J.1    Lehmann, D.J.2    Wimhurst, V.L.3
  • 32
    • 38349131338 scopus 로고    scopus 로고
    • Iron genes, iron load and risk of Alzheimer's disease
    • Lehmann DJ, Worwood M, Ellis R, et al. Iron genes, iron load and risk of Alzheimer's disease. J Med Genet 2006;43(10):e52
    • (2006) J Med Genet , vol.43 , Issue.10
    • Lehmann, D.J.1    Worwood, M.2    Ellis, R.3
  • 33
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith MA, Harris PL, Sayre LM, Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci USA 1997;94:9866-9868
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 34
    • 0031981072 scopus 로고    scopus 로고
    • Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress
    • Smith MA, Hirai K, Hsiao K, et al. Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress. J Neurochem 1998;70:2212-2215
    • (1998) J Neurochem , vol.70 , pp. 2212-2215
    • Smith, M.A.1    Hirai, K.2    Hsiao, K.3
  • 35
    • 69049113059 scopus 로고    scopus 로고
    • Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: Binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease
    • Jiang D, Li X, Williams R, et al. Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease. Biochemistry 2009;48:7939-7947
    • (2009) Biochemistry , vol.48 , pp. 7939-7947
    • Jiang, D.1    Li, X.2    Williams, R.3
  • 37
    • 33751107948 scopus 로고    scopus 로고
    • Aluminium and iron, but neither copper nor zinc, are key to the precipitation of beta-sheets of Abeta42. in senile plaque cores in Alzheimer's disease
    • Exley C. Aluminium and iron, but neither copper nor zinc, are key to the precipitation of beta-sheets of Abeta42. in senile plaque cores in Alzheimer's disease. J Alzheimers Dis 2006;10:173-177
    • (2006) J Alzheimers Dis , vol.10 , pp. 173-177
    • Exley, C.1
  • 38
    • 47849086918 scopus 로고    scopus 로고
    • Three-dimensional tomographic imaging and characterization of iron compounds within Alzheimer's plaque core material
    • Collingwood JF, Chong RK, Kasama T, et al. Three-dimensional tomographic imaging and characterization of iron compounds within Alzheimer's plaque core material. J Alzheimers Dis 2008;14:235-245
    • (2008) J Alzheimers Dis , vol.14 , pp. 235-245
    • Collingwood, J.F.1    Chong, R.K.2    Kasama, T.3
  • 39
    • 0037216723 scopus 로고    scopus 로고
    • Mouse brains deficient in H-ferritin have normal iron concentration but a protein profile of iron deficiency and increased evidence of oxidative stress
    • Thompson K, Menzies S, Muckenthaler M, et al. Mouse brains deficient in H-ferritin have normal iron concentration but a protein profile of iron deficiency and increased evidence of oxidative stress. J Neurosci Res 2003;71:46-63
    • (2003) J Neurosci Res , vol.71 , pp. 46-63
    • Thompson, K.1    Menzies, S.2    Muckenthaler, M.3
  • 40
    • 33644778691 scopus 로고    scopus 로고
    • Amyloid-beta peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer's disease
    • Atamna H, Boyle K. Amyloid-beta peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease. Proc Natl Acad Sci USA 2006;103:3381-3386
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3381-3386
    • Atamna, H.1    Boyle, K.2
  • 41
    • 67349213608 scopus 로고    scopus 로고
    • Down-regulation of aminolevulinate synthase, the rate-limiting enzyme for heme biosynthesis in Alzheimer's disease
    • Dwyer BE, Smith MA, Richardson SL, et al. Down-regulation of aminolevulinate synthase, the rate-limiting enzyme for heme biosynthesis in Alzheimer's disease. Neurosci Lett 2009;460:180-184
    • (2009) Neurosci Lett , vol.460 , pp. 180-184
    • Dwyer, B.E.1    Smith, M.A.2    Richardson, S.L.3
  • 42
    • 34247120546 scopus 로고    scopus 로고
    • Iron, copper, and iron regulatory protein 2 in Alzheimer's disease and related dementias
    • Magaki S, Raghavan R, Mueller C, et al. Iron, copper, and iron regulatory protein 2 in Alzheimer's disease and related dementias. Neurosci Lett 2007;418:72-76
    • (2007) Neurosci Lett , vol.418 , pp. 72-76
    • Magaki, S.1    Raghavan, R.2    Mueller, C.3
  • 43
    • 3342880690 scopus 로고    scopus 로고
    • A role for heme in Alzheimer's disease: Heme binds amyloid beta and has altered metabolism
    • Atamna H, Frey WH II. A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism. Proc Natl Acad Sci USA 2004;101:11153-11158
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11153-11158
    • Atamna, H.1    Frey Ii, W.H.2
  • 44
    • 67649617842 scopus 로고    scopus 로고
    • Suppression of Glial HO-1 activitiy as a potential neurotherapeutic intervention in AD
    • published online Oct 1 2009. doi: 10.2174/156720509789207985
    • Schipper HM, Gupta A, Szarek WA. Suppression of Glial HO-1 activitiy as a potential neurotherapeutic intervention in AD. Curr Alzheimer Res 2009 published online Oct 1 2009. doi: 10.2174/ 156720509789207985
    • (2009) Curr Alzheimer Res
    • Schipper, H.M.1    Gupta, A.2    Szarek, W.A.3
  • 45
    • 0037355733 scopus 로고    scopus 로고
    • Adventiously-bound redox active iron and copper are at the center of oxidative damage in Alzheimer disease
    • Perry G, Taddeo MA, Petersen RB, et al. Adventiously-bound redox active iron and copper are at the center of oxidative damage in Alzheimer disease. Biometals 2003;16:77-81
    • (2003) Biometals , vol.16 , pp. 77-81
    • Perry, G.1    Taddeo, M.A.2    Petersen, R.B.3
  • 47
    • 3442888291 scopus 로고    scopus 로고
    • Metal and inflammatory targets for Alzheimer's disease
    • Rogers JT, Lahiri DK. Metal and inflammatory targets for Alzheimer's disease. Curr Drug Targets 2004;5:535-551
    • (2004) Curr Drug Targets , vol.5 , pp. 535-551
    • Rogers, J.T.1    Lahiri, D.K.2
  • 48
    • 0036728812 scopus 로고    scopus 로고
    • Abeta[25-35] peptide and iron promote apoptosis in lymphocytes by an oxidative stress mechanism: Involvement of H2O2, caspase-3, NF-kappaB, p53 and c-Jun
    • Velez-Pardo C, Ospina GG, Jimenez del Rio M. Abeta[25-35] peptide and iron promote apoptosis in lymphocytes by an oxidative stress mechanism: involvement of H2O2, caspase-3, NF-kappaB, p53 and c-Jun. Neurotoxicology 2002;23:351-365
    • (2002) Neurotoxicology , vol.23 , pp. 351-365
    • Velez-Pardo, C.1    Ospina, G.G.2    Jimenez Del Rio, M.3
  • 49
    • 33749161414 scopus 로고    scopus 로고
    • Deposition of iron and beta-amyloid plaques is associated with cortical cellular damage in rabbits fed with long-term cholesterol-enriched diets
    • Ghribi O, Golovko MY, Larsen B, et al. Deposition of iron and beta-amyloid plaques is associated with cortical cellular damage in rabbits fed with long-term cholesterol-enriched diets. J Neurochem 2006;99:438-449
    • (2006) J Neurochem , vol.99 , pp. 438-449
    • Ghribi, O.1    Golovko, M.Y.2    Larsen, B.3
  • 50
    • 29844456397 scopus 로고    scopus 로고
    • Study of the localization of iron, ferritin, and hemosiderin in Alzheimer's disease hippocampus by analytical microscopy at the subcellular level
    • Quintana C, Bellefqih S, Laval JY, et al. Study of the localization of iron, ferritin, and hemosiderin in Alzheimer's disease hippocampus by analytical microscopy at the subcellular level. J Struct Biol 2006;153:42-54
    • (2006) J Struct Biol , vol.153 , pp. 42-54
    • Quintana, C.1    Bellefqih, S.2    Laval, J.Y.3
  • 51
    • 0346770038 scopus 로고    scopus 로고
    • Age-related myelin breakdown: A developmental model of cognitive decline and Alzheimer's disease
    • author reply 49-62
    • Bartzokis G. Age-related myelin breakdown: a developmental model of cognitive decline and Alzheimer's disease. Neurobiol Aging 2004;25:5-18; author reply 49-62
    • (2004) Neurobiol Aging , vol.25 , pp. 5-18
    • Bartzokis, G.1
  • 52
    • 0035865905 scopus 로고    scopus 로고
    • Redox-active iron mediates amyloid-beta toxicity
    • Rottkamp CA, Raina AK, Zhu X, et al. Redox-active iron mediates amyloid-beta toxicity. Free Radic Biol Med 2001;30:447-450
    • (2001) Free Radic Biol Med , vol.30 , pp. 447-450
    • Rottkamp, C.A.1    Raina, A.K.2    Zhu, X.3
  • 53
    • 0033986037 scopus 로고    scopus 로고
    • Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains
    • Suh SW, Jensen KB, Jensen MS, et al. Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Res 2000;852:274-278
    • (2000) Brain Res , vol.852 , pp. 274-278
    • Suh, S.W.1    Jensen, K.B.2    Jensen, M.S.3
  • 54
    • 32444440545 scopus 로고    scopus 로고
    • Is zinc the link between compromises of brain perfusion (excitotoxicity) and Alzheimer's disease?
    • discussion 209-215
    • Frederickson CJ, Cuajungco MP. Is zinc the link between compromises of brain perfusion (excitotoxicity) and Alzheimer's disease? J Alzheimers Dis 2005;8:155-60; discussion 209-215
    • (2005) J Alzheimers Dis , vol.8 , pp. 155-60
    • Frederickson, C.J.1    Cuajungco, M.P.2
  • 55
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida Y, Takio K, Titani K, et al. The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron 1991;7:337-347
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3
  • 56
    • 0026597204 scopus 로고
    • Characterization of neutral proteinases from Alzheimer-affected and control brain specimens: Identification of calcium-dependent metalloproteinases from the hippocampus
    • Backstrom JR, Miller CA, Tokes ZA. Characterization of neutral proteinases from Alzheimer-affected and control brain specimens: identification of calcium-dependent metalloproteinases from the hippocampus. J Neurochem 1992;58:983-992
    • (1992) J Neurochem , vol.58 , pp. 983-992
    • Backstrom, J.R.1    Miller, C.A.2    Tokes, Z.A.3
  • 57
    • 0021358519 scopus 로고
    • Cholinergic denervation-induced increase of chelatable zinc in mossy-fiber region of the hippocampal formation
    • Stewart GR, Frederickson CJ, Howell GA, Gage FH. Cholinergic denervation-induced increase of chelatable zinc in mossy-fiber region of the hippocampal formation. Brain Res 1984;290:43-51
    • (1984) Brain Res , vol.290 , pp. 43-51
    • Stewart, G.R.1    Frederickson, C.J.2    Howell, G.A.3    Gage, F.H.4
  • 59
    • 70449709313 scopus 로고    scopus 로고
    • Altered expression and distribution of zinc transporters in APP/PS1 transgenic mouse brain
    • Zhang LH, Wang X, Zheng ZH, et al. Altered expression and distribution of zinc transporters in APP/PS1 transgenic mouse brain. Neurobiol Aging 2010;31:74-87
    • (2010) Neurobiol Aging , vol.31 , pp. 74-87
    • Zhang, L.H.1    Wang, X.2    Zheng, Z.H.3
  • 60
    • 51749106579 scopus 로고    scopus 로고
    • Abundant expression of zinc transporters in the amyloid plaques of Alzheimer's disease brain
    • Zhang LH, Wang X, Stoltenberg M, et al. Abundant expression of zinc transporters in the amyloid plaques of Alzheimer's disease brain. Brain Res Bull 2008;77:55-60
    • (2008) Brain Res Bull , vol.77 , pp. 55-60
    • Zhang, L.H.1    Wang, X.2    Stoltenberg, M.3
  • 61
    • 0027980901 scopus 로고
    • Rapid induction of Alzheimer A beta amyloid formation by zinc
    • Bush AI, Pettingell WH, Multhaup G, et al. Rapid induction of Alzheimer A beta amyloid formation by zinc. Science 1994;265:1464-1467
    • (1994) Science , vol.265 , pp. 1464-1467
    • Bush, A.I.1    Pettingell, W.H.2    Multhaup, G.3
  • 62
    • 33744965484 scopus 로고    scopus 로고
    • Zinc homeostasis in aging: Two elusive faces of the same "metal"
    • Mocchegiani E, Costarelli L, Giacconi R, et al. Zinc homeostasis in aging: two elusive faces of the same "metal". Rejuvenation Res 2006;9:351-354
    • (2006) Rejuvenation Res , vol.9 , pp. 351-354
    • Mocchegiani, E.1    Costarelli, L.2    Giacconi, R.3
  • 64
    • 1842506368 scopus 로고    scopus 로고
    • Neuronal zinc exchange with the blood vessel wall promotes cerebral amyloid angiopathy in an animal model of Alzheimer's disease
    • Friedlich AL, Lee JY, van Groen T, et al. Neuronal zinc exchange with the blood vessel wall promotes cerebral amyloid angiopathy in an animal model of Alzheimer's disease. J Neurosci 2004;24:3453-3459
    • (2004) J Neurosci , vol.24 , pp. 3453-3459
    • Friedlich, A.L.1    Lee, J.Y.2    Vangroen, T.3
  • 65
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee JY, Cole TB, Palmiter RD, et al. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc Natl Acad Sci USA 2002;99:7705-7710
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3
  • 66
    • 0027220686 scopus 로고
    • A novel zinc(II) binding site modulates the function of the betaA4 amyloid protein precursor of Alzheimer's disease
    • Bush AI, Multhaup G, Moir RD, et al. A novel zinc(II) binding site modulates the function of the betaA4 amyloid protein precursor of Alzheimer's disease. J Biol Chem 1993;268:16109-16112
    • (1993) J Biol Chem , vol.268 , pp. 16109-16112
    • Bush, A.I.1    Multhaup, G.2    Moir, R.D.3
  • 67
    • 0028171064 scopus 로고
    • The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily
    • Bush AI, Pettingell WH Jr, de Paradis M, et al. The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. J Biol Chem 1994;269:26618-26621
    • (1994) J Biol Chem , vol.269 , pp. 26618-26621
    • Bush, A.I.1    Pettingell Jr., W.H.2    De Paradis, M.3
  • 68
    • 0029331504 scopus 로고
    • Characterization of the high affinity heparin binding site of the Alzheimer's disease betaA4 amyloid precursor protein (APP) and its enhancement by zinc(II)
    • Multhaup G, Mechler H, Masters CL. Characterization of the high affinity heparin binding site of the Alzheimer's disease betaA4 amyloid precursor protein (APP) and its enhancement by zinc(II). J Mol Recognit 1995;8:247-257
    • (1995) J Mol Recognit , vol.8 , pp. 247-257
    • Multhaup, G.1    Mechler, H.2    Masters, C.L.3
  • 69
    • 0026474527 scopus 로고
    • Characterization of high affinity binding between laminin and Alzheimer's disease amyloid precursor proteins
    • Narindrasorasak S, Lowery DE, Altman RA, et al. Characterization of high affinity binding between laminin and Alzheimer's disease amyloid precursor proteins. Lab Invest 1992;67:643-652
    • (1992) Lab Invest , vol.67 , pp. 643-652
    • Narindrasorasak, S.1    Lowery, D.E.2    Altman, R.A.3
  • 70
    • 0034054929 scopus 로고    scopus 로고
    • Alzheimer's disease, beta-amyloid protein and zinc
    • Huang X, Cuajungco MP, Atwood CS, et al. Alzheimer's disease, beta-amyloid protein and zinc. J Nutr 2000;130(5S Suppl):1488S-1492S
    • (2000) J Nutr , vol.130 , Issue.5 SUPPL.
    • Huang, X.1    Cuajungco, M.P.2    Atwood, C.S.3
  • 71
    • 0028169266 scopus 로고
    • Non-amyloidogenic cleavage of the beta-amyloid precursor protein by an integral membrane metalloendopeptidase
    • Roberts SB, Ripellino JA, Ingalls KM, et al. Non-amyloidogenic cleavage of the beta-amyloid precursor protein by an integral membrane metalloendopeptidase. J Biol Chem 1994;269:3111-3116
    • (1994) J Biol Chem , vol.269 , pp. 3111-3116
    • Roberts, S.B.1    Ripellino, J.A.2    Ingalls, K.M.3
  • 72
    • 0034811346 scopus 로고    scopus 로고
    • Zinc enhances synthesis of presenilin 1 in mouse primary cortical culture
    • Park IH, Jung MW, Mori H, Mook-Jung I. Zinc enhances synthesis of presenilin 1 in mouse primary cortical culture. Biochem Biophys Res Commun 2001;285:680-688
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 680-688
    • Park, I.H.1    Jung, M.W.2    Mori, H.3    Mook-Jung, I.4
  • 73
    • 0030725838 scopus 로고    scopus 로고
    • Zinc metabolism in the brain: Relevance to human neurodegenerative disorders
    • Cuajungco MP, Lees GJ. Zinc metabolism in the brain: relevance to human neurodegenerative disorders. Neurobiol Dis 1997;4:137-169
    • (1997) Neurobiol Dis , vol.4 , pp. 137-169
    • Cuajungco, M.P.1    Lees, G.J.2
  • 74
    • 0027301434 scopus 로고
    • Drastic reduction of the zinc- and magnesium-stimulated protein tyrosine kinase activities in Alzheimer's disease hippocampus
    • Vener AV, Aksenova MV, Burbaeva G. Drastic reduction of the zinc- and magnesium-stimulated protein tyrosine kinase activities in Alzheimer's disease hippocampus. FEBS Lett 1993;328:6-8
    • (1993) FEBS Lett , vol.328 , pp. 6-8
    • Vener, A.V.1    Aksenova, M.V.2    Burbaeva, G.3
  • 75
    • 0028180196 scopus 로고
    • Modulation of Abeta adhesiveness and secretase site cleavage by zinc
    • Bush AI, Pettingell WH Jr, Paradis MD, Tanzi RE. Modulation of Abeta adhesiveness and secretase site cleavage by zinc. J Biol Chem 1994;269:12152-12158
    • (1994) J Biol Chem , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell Jr., W.H.2    Paradis, M.D.3    Tanzi, R.E.4
  • 76
    • 38649112930 scopus 로고    scopus 로고
    • Zinc-amyloid beta interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species
    • Noy D, Solomonov I, Sinkevich O, et al. Zinc-amyloid beta interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species. J Am Chem Soc 2008;130:1376-1383
    • (2008) J Am Chem Soc , vol.130 , pp. 1376-1383
    • Noy, D.1    Solomonov, I.2    Sinkevich, O.3
  • 77
    • 0034806472 scopus 로고    scopus 로고
    • Zinc binding to Alzheimer's Abeta(1-16) peptide results in stable soluble complex
    • Kozin SA, Zirah S, Rebuffat S, et al. Zinc binding to Alzheimer's Abeta(1-16) peptide results in stable soluble complex. Biochem Biophys Res Commun 2001;285:959-964
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 959-964
    • Kozin, S.A.1    Zirah, S.2    Rebuffat, S.3
  • 78
    • 33744956272 scopus 로고    scopus 로고
    • Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge
    • Smith DP, Smith DG, Curtain CC, et al. Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge. J Biol Chem 2006;281:15145-15154
    • (2006) J Biol Chem , vol.281 , pp. 15145-15154
    • Smith, D.P.1    Smith, D.G.2    Curtain, C.C.3
  • 79
    • 33845665797 scopus 로고    scopus 로고
    • High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide
    • Danielsson J, Pierattelli R, Banci L, Graslund A. High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide. FEBS J 2007;274:46-59
    • (2007) FEBS J , vol.274 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 80
    • 59449097016 scopus 로고    scopus 로고
    • Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide
    • Faller P, Hureau C. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide. Dalton Trans 2009;(7):1080-1094
    • (2009) Dalton Trans , Issue.7 , pp. 1080-1094
    • Faller, P.1    Hureau, C.2
  • 81
    • 38649116906 scopus 로고    scopus 로고
    • NMR studies of the Zn2+ interactions with rat and human beta-amyloid (1-28) peptides in water-micelle environment
    • Gaggelli E, Janicka-Klos A, Jankowska E, et al. NMR studies of the Zn2+ interactions with rat and human beta-amyloid (1-28) peptides in water-micelle environment. J Phys Chem B 2008;112:100-109
    • (2008) J Phys Chem B , vol.112 , pp. 100-109
    • Gaggelli, E.1    Janicka-Klos, A.2    Jankowska, E.3
  • 82
    • 33644867988 scopus 로고    scopus 로고
    • Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging
    • Zirah S, Kozin SA, Mazur AK, et al. Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging. J Biol Chem 2006;281:2151-2161
    • (2006) J Biol Chem , vol.281 , pp. 2151-2161
    • Zirah, S.1    Kozin, S.A.2    Mazur, A.K.3
  • 83
    • 36749044742 scopus 로고    scopus 로고
    • Zinc binding to amyloid-beta: Isothermal titration calorimetry and Zn competition experiments with Zn sensors
    • Talmard C, Bouzan A, Faller P. Zinc binding to amyloid-beta: isothermal titration calorimetry and Zn competition experiments with Zn sensors. Biochemistry 2007;46:13658-13666
    • (2007) Biochemistry , vol.46 , pp. 13658-13666
    • Talmard, C.1    Bouzan, A.2    Faller, P.3
  • 84
    • 48649105912 scopus 로고    scopus 로고
    • Isomerization of the Asp7 residue results in zinc-induced oligomerization of Alzheimer's disease amyloid beta(1-16) peptide
    • Tsvetkov PO, Popov IA, Nikolaev EN, et al. Isomerization of the Asp7 residue results in zinc-induced oligomerization of Alzheimer's disease amyloid beta(1-16) peptide. Chembiochem 2008;9:1564-1567
    • (2008) Chembiochem , vol.9 , pp. 1564-1567
    • Tsvetkov, P.O.1    Popov, I.A.2    Nikolaev, E.N.3
  • 85
    • 69949167074 scopus 로고    scopus 로고
    • Zn(II)- and Cu(II)-induced nonfibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
    • Tougu V, Karafin A, Zovo K, et al. Zn(II)- and Cu(II)-induced nonfibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators. J Neurochem 2009;110:1784-1795
    • (2009) J Neurochem , vol.110 , pp. 1784-1795
    • Tougu, V.1    Karafin, A.2    Zovo, K.3
  • 86
    • 61849148857 scopus 로고    scopus 로고
    • Mechanism of zinc(II)-promoted amyloid formation: Zinc(II) binding facilitates the transition from the partially alpha-helical conformer to aggregates of amyloid beta protein(1-28)
    • Talmard C, Leuma Yona R, Faller P. Mechanism of zinc(II)-promoted amyloid formation: zinc(II) binding facilitates the transition from the partially alpha-helical conformer to aggregates of amyloid beta protein(1-28). J Biol Inorg Chem 2009;14:449-455
    • (2009) J Biol Inorg Chem , vol.14 , pp. 449-455
    • Talmard, C.1    Leuma Yona, R.2    Faller, P.3
  • 87
    • 0035297710 scopus 로고    scopus 로고
    • S100beta interaction with tau is promoted by zinc and inhibited by hyperphosphorylation in Alzheimer's disease
    • Yu WH, Fraser PE. S100beta interaction with tau is promoted by zinc and inhibited by hyperphosphorylation in Alzheimer's disease. J Neurosci 2001;21:2240-2246
    • (2001) J Neurosci , vol.21 , pp. 2240-2246
    • Yu, W.H.1    Fraser, P.E.2
  • 88
    • 62449128087 scopus 로고    scopus 로고
    • Ceruloplasmin fragmentation is implicated in 'free' copper deregulation of Alzheimer's disease
    • Squitti R, Quattrocchi CC, Salustri C, Rossini PM. Ceruloplasmin fragmentation is implicated in 'free' copper deregulation of Alzheimer's disease. Prion 2008;2:23-27
    • (2008) Prion , vol.2 , pp. 23-27
    • Squitti, R.1    Quattrocchi, C.C.2    Salustri, C.3    Rossini, P.M.4
  • 89
    • 20444440369 scopus 로고    scopus 로고
    • Metals and amyloid-beta in Alzheimer's disease
    • Maynard CJ, Bush AI, Masters CL, et al. Metals and amyloid-beta in Alzheimer's disease. Int J Exp Pathol 2005;86:147-159
    • (2005) Int J Exp Pathol , vol.86 , pp. 147-159
    • Maynard, C.J.1    Bush, A.I.2    Masters, C.L.3
  • 90
    • 58549113169 scopus 로고    scopus 로고
    • Metallo-complex activation of neuroprotective signalling pathways as a therapeutic treatment for Alzheimer's disease
    • Bica L, Crouch PJ, Cappai R, White AR. Metallo-complex activation of neuroprotective signalling pathways as a therapeutic treatment for Alzheimer's disease. Mol Biosyst 2009;5:134-142
    • (2009) Mol Biosyst , vol.5 , pp. 134-142
    • Bica, L.1    Crouch, P.J.2    Cappai, R.3    White, A.R.4
  • 91
    • 69749106568 scopus 로고    scopus 로고
    • Abeta-mediated ROS production by Cu ions: Structural insights, mechanisms and relevance to Alzheimer's disease
    • Hureau C, Faller P. Abeta-mediated ROS production by Cu ions: structural insights, mechanisms and relevance to Alzheimer's disease. Biochimie 2009;91:1212-1217
    • (2009) Biochimie , vol.91 , pp. 1212-1217
    • Hureau, C.1    Faller, P.2
  • 93
    • 42049116923 scopus 로고    scopus 로고
    • Alzheimer disease and the role of free radicals in the pathogenesis of the disease
    • Moreira PI, Santos MS, Oliveira CR, et al. Alzheimer disease and the role of free radicals in the pathogenesis of the disease. CNS Neurol Disord Drug Targets 2008;7:3-10
    • (2008) CNS Neurol Disord Drug Targets , vol.7 , pp. 3-10
    • Moreira, P.I.1    Santos, M.S.2    Oliveira, C.R.3
  • 94
    • 63849241137 scopus 로고    scopus 로고
    • Longitudinal prognostic value of serum "free" copper in patients with Alzheimer disease
    • Squitti R, Bressi F, Pasqualetti P, et al. Longitudinal prognostic value of serum "free" copper in patients with Alzheimer disease. Neurology 2009;72:50-55
    • (2009) Neurology , vol.72 , pp. 50-55
    • Squitti, R.1    Bressi, F.2    Pasqualetti, P.3
  • 95
    • 34547102265 scopus 로고    scopus 로고
    • Roles of amyloid beta-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment
    • Butterfield DA, Reed T, Newman SF, Sultana R. Roles of amyloid beta-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment. Free Radic Biol Med 2007;43:658-677
    • (2007) Free Radic Biol Med , vol.43 , pp. 658-677
    • Butterfield, D.A.1    Reed, T.2    Newman, S.F.3    Sultana, R.4
  • 96
    • 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 H2O2
    • Opazo C, Huang X, Cherny RA, et al. Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H2O2. J Biol Chem 2002;277:40302-40308
    • (2002) J Biol Chem , vol.277 , pp. 40302-40308
    • Opazo, C.1    Huang, X.2    Cherny, R.A.3
  • 97
    • 9144235443 scopus 로고    scopus 로고
    • Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta
    • Atwood CS, Perry G, Zeng H, et al. Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta. Biochemistry 2004;43:560-568
    • (2004) Biochemistry , vol.43 , pp. 560-568
    • Atwood, C.S.1    Perry, G.2    Zeng, H.3
  • 98
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994;77:817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 99
    • 9444284334 scopus 로고    scopus 로고
    • Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid
    • Barnham KJ, Haeffner F, Ciccotosto GD, et al. Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid. FASEB J 2004;18:1427-1429
    • (2004) FASEB J , vol.18 , pp. 1427-1429
    • Barnham, K.J.1    Haeffner, F.2    Ciccotosto, G.D.3
  • 100
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Abeta by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood CS, Moir RD, Huang X, et al. Dramatic aggregation of Alzheimer Abeta by Cu(II) is induced by conditions representing physiological acidosis. J Biol Chem 1998;273:12817-12826
    • (1998) J Biol Chem , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Moir, R.D.2    Huang, X.3
  • 101
    • 28244484884 scopus 로고    scopus 로고
    • Cholesterol, copper and Abeta in controls, MCI, AD and the AD cholesterol-lowering treatment trial (ADCLT)
    • Sparks DL, Petanceska S, Sabbagh M, et al. Cholesterol, copper and Abeta in controls, MCI, AD and the AD cholesterol-lowering treatment trial (ADCLT). Curr Alzheimer Res 2005;2:527-539
    • (2005) Curr Alzheimer Res , vol.2 , pp. 527-539
    • Sparks, D.L.1    Petanceska, S.2    Sabbagh, M.3
  • 102
    • 35348981740 scopus 로고    scopus 로고
    • Lipid peroxidation and 4-hydroxy-2-nonenal formation by copper ion bound to amyloid-beta peptide
    • Hayashi T, Shishido N, Nakayama K, et al. Lipid peroxidation and 4-hydroxy-2-nonenal formation by copper ion bound to amyloid-beta peptide. Free Radic Biol Med 2007;43:1552-1559
    • (2007) Free Radic Biol Med , vol.43 , pp. 1552-1559
    • Hayashi, T.1    Shishido, N.2    Nakayama, K.3
  • 103
    • 69249084030 scopus 로고    scopus 로고
    • Paradoxical condensation of copper with elevated beta-amyloid in lipid rafts under cellular copper deficiency conditions: Implications for Alzheimer disease
    • Hung YH, Robb EL, Volitakis I, et al. Paradoxical condensation of copper with elevated beta-amyloid in lipid rafts under cellular copper deficiency conditions: implications for Alzheimer disease. J Biol Chem 2009;284:21899-21907
    • (2009) J Biol Chem , vol.284 , pp. 21899-21907
    • Hung, Y.H.1    Robb, E.L.2    Volitakis, I.3
  • 104
    • 55249115550 scopus 로고    scopus 로고
    • Amyloid beta-Cu2+ complexes in both monomeric and fibrillar forms do not generate H2O2 catalytically but quench hydroxyl radicals
    • Nadal RC, Rigby SE, Viles JH. Amyloid beta-Cu2+ complexes in both monomeric and fibrillar forms do not generate H2O2 catalytically but quench hydroxyl radicals. Biochemistry 2008;47:11653-11664
    • (2008) Biochemistry , vol.47 , pp. 11653-11664
    • Nadal, R.C.1    Rigby, S.E.2    Viles, J.H.3
  • 105
    • 0028177269 scopus 로고
    • The betaA4 amyloid precursor protein binding to copper
    • Hesse L, Beher D, Masters CL, Multhaup G. The betaA4 amyloid precursor protein binding to copper. FEBS Lett 1994;349:109-116
    • (1994) FEBS Lett , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 107
    • 39749193587 scopus 로고    scopus 로고
    • Copper binding to the Alzheimer's disease amyloid precursor protein
    • Kong GK, Miles LA, Crespi GA, et al. Copper binding to the Alzheimer's disease amyloid precursor protein. Eur Biophys J 2008;37:269-279
    • (2008) Eur Biophys J , vol.37 , pp. 269-279
    • Kong, G.K.1    Miles, L.A.2    Crespi, G.A.3
  • 108
    • 33847044093 scopus 로고    scopus 로고
    • Structural studies of the Alzheimer's amyloid precursor protein copper-binding domain reveal how it binds copper ions
    • Kong GK, Adams JJ, Harris HH, et al. Structural studies of the Alzheimer's amyloid precursor protein copper-binding domain reveal how it binds copper ions. J Mol Biol 2007;367:148-161
    • (2007) J Mol Biol , vol.367 , pp. 148-161
    • Kong, G.K.1    Adams, J.J.2    Harris, H.H.3
  • 109
    • 34250834446 scopus 로고    scopus 로고
    • A copper-binding site in the cytoplasmic domain of BACE1 identifies a possible link to metal homoeostasis and oxidative stress in Alzheimer's disease
    • Dingwall C. A copper-binding site in the cytoplasmic domain of BACE1 identifies a possible link to metal homoeostasis and oxidative stress in Alzheimer's disease. Biochem Soc Trans 2007;35:571-573
    • (2007) Biochem Soc Trans , vol.35 , pp. 571-573
    • Dingwall, C.1
  • 110
    • 2442586535 scopus 로고    scopus 로고
    • Copper depletion down-regulates expression of the Alzheimer's disease amyloid-beta precursor protein gene
    • Bellingham SA, Lahiri DK, Maloney B, et al. Copper depletion down-regulates expression of the Alzheimer's disease amyloid-beta precursor protein gene. J Biol Chem 2004;279:20378-20386
    • (2004) J Biol Chem , vol.279 , pp. 20378-20386
    • Bellingham, S.A.1    Lahiri, D.K.2    Maloney, B.3
  • 111
    • 0032830357 scopus 로고    scopus 로고
    • Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice
    • White AR, Reyes R, Mercer JF, et al. Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res 1999;842:439-444
    • (1999) Brain Res , vol.842 , pp. 439-444
    • White, A.R.1    Reyes, R.2    Mercer, J.F.3
  • 112
    • 16844373633 scopus 로고    scopus 로고
    • N-Terminal deletions modify the Cu2+ binding site in amyloid-beta
    • Karr JW, Akintoye H, Kaupp LJ, Szalai VA. N-Terminal deletions modify the Cu2+ binding site in amyloid-beta. Biochemistry 2005;44:5478-5487
    • (2005) Biochemistry , vol.44 , pp. 5478-5487
    • Karr, J.W.1    Akintoye, H.2    Kaupp, L.J.3    Szalai, V.A.4
  • 113
    • 77049095207 scopus 로고    scopus 로고
    • The Cu(II)/Abeta/ human serum albumin model of control mechanism for copper-related amyloid neurotoxicity
    • Rozga M, Bal W. The Cu(II)/Abeta/ human serum albumin model of control mechanism for copper-related amyloid neurotoxicity. Chem Res Toxicol 2010;23:298-308
    • (2010) Chem Res Toxicol , vol.23 , pp. 298-308
    • Rozga, M.1    Bal, W.2
  • 114
    • 70350153272 scopus 로고    scopus 로고
    • The chemistry of Alzheimer's disease
    • Rauk A. The chemistry of Alzheimer's disease. Chem Soc Rev 2009;38:2698-2715
    • (2009) Chem Soc Rev , vol.38 , pp. 2698-2715
    • Rauk, A.1
  • 115
    • 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 1998;14:181-187
    • (1998) Amino Acids , vol.14 , pp. 181-187
    • Metodiewa, D.1
  • 116
    • 50849126063 scopus 로고    scopus 로고
    • Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-beta1-16
    • Shin BK, Saxena S. Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-beta1-16. Biochemistry 2008;47:9117-9123
    • (2008) Biochemistry , vol.47 , pp. 9117-9123
    • Shin, B.K.1    Saxena, S.2
  • 117
    • 61749097242 scopus 로고    scopus 로고
    • Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide
    • Drew SC, Noble CJ, Masters CL, et al. Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide. J Am Chem Soc 2009;131:1195-1207
    • (2009) J Am Chem Soc , vol.131 , pp. 1195-1207
    • Drew, S.C.1    Noble, C.J.2    Masters, C.L.3
  • 118
    • 67649600828 scopus 로고    scopus 로고
    • Alanine-2 carbonyl is an oxygen ligand in Cu2+ coordination of Alzheimer's disease amyloid-beta peptide - relevance to N-terminally truncated forms
    • Drew SC, Masters CL, Barnham KJ. Alanine-2 carbonyl is an oxygen ligand in Cu2+ coordination of Alzheimer's disease amyloid-beta peptide - relevance to N-terminally truncated forms. J Am Chem Soc 2009;131:8760-8761
    • (2009) J Am Chem Soc , vol.131 , pp. 8760-8761
    • Drew, S.C.1    Masters, C.L.2    Barnham, K.J.3
  • 119
    • 72949092936 scopus 로고    scopus 로고
    • Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-beta peptide: A key role of the first two N-terminus residues
    • Dorlet P, Gambarelli S, Faller P, Hureau C. Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-beta peptide: a key role of the first two N-terminus residues. Angew Chem Int Ed Engl 2009;48:9273-9276
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 9273-9276
    • Dorlet, P.1    Gambarelli, S.2    Faller, P.3    Hureau, C.4
  • 120
    • 58849086013 scopus 로고    scopus 로고
    • The amyloid-beta peptide of Alzheimer's disease binds CuI in a linear bis-his coordination environment: Insight into a possible neuroprotective mechanism for the amyloid-beta peptide
    • Shearer J, Szalai VA. The amyloid-beta peptide of Alzheimer's disease binds CuI in a linear bis-his coordination environment: insight into a possible neuroprotective mechanism for the amyloid-beta peptide. J Am Chem Soc 2008;13:17826-17835
    • (2008) J Am Chem Soc , vol.13 , pp. 17826-17835
    • Shearer, J.1    Szalai, V.A.2
  • 121
    • 70349568604 scopus 로고    scopus 로고
    • Importance of dynamical processes in the coordination chemistry and redox conversion of copper amyloid-beta complexes
    • Hureau C, Balland V, Coppel Y, et al. Importance of dynamical processes in the coordination chemistry and redox conversion of copper amyloid-beta complexes. J Biol Inorg Chem 2009;14:995-1000
    • (2009) J Biol Inorg Chem , vol.14 , pp. 995-1000
    • Hureau, C.1    Balland, V.2    Coppel, Y.3
  • 122
    • 56249101018 scopus 로고    scopus 로고
    • Structural studies of copper(I) complexes of amyloid-beta peptide fragments: Formation of two-coordinate bis (histidine) complexes
    • Himes RA, Park GY, Siluvai GS, et al. Structural studies of copper(I) complexes of amyloid-beta peptide fragments: formation of two-coordinate bis (histidine) complexes. Angew Chem Int Ed Engl 2008;47:9084-90877
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 9084-90877
    • Himes, R.A.1    Park, G.Y.2    Siluvai, G.S.3
  • 123
    • 20444470267 scopus 로고    scopus 로고
    • Catechol oxidase-like oxidation chemistry of the 1-20 and 1-16 fragments of Alzheimer's disease-related beta-amyloid peptide: Their structure-activity correlation and the fate of hydrogen peroxide
    • da Silva GF, Tay WM, Ming LJ. Catechol oxidase-like oxidation chemistry of the 1-20 and 1-16 fragments of Alzheimer's disease-related beta-amyloid peptide: their structure-activity correlation and the fate of hydrogen peroxide. J Biol Chem 2005;280:16601-16609
    • (2005) J Biol Chem , vol.280 , pp. 16601-16609
    • Da Silva, G.F.1    Tay, W.M.2    Ming, L.J.3
  • 124
    • 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 CD, Nadal RC, Rigby SE, Viles JH. 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 2004;279:18169-18177
    • (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
  • 125
    • 20244381121 scopus 로고    scopus 로고
    • Methylation of the imidazole side chains of the Alzheimer disease amyloid-beta peptide results in abolition of superoxide dismutase-like structures and inhibition of neurotoxicity
    • Tickler AK, Smith DG, Ciccotosto GD, et al. Methylation of the imidazole side chains of the Alzheimer disease amyloid-beta peptide results in abolition of superoxide dismutase-like structures and inhibition of neurotoxicity. J Biol Chem 2005;280:13355-13363
    • (2005) J Biol Chem , vol.280 , pp. 13355-13363
    • Tickler, A.K.1    Smith, D.G.2    Ciccotosto, G.D.3
  • 126
    • 6044229556 scopus 로고    scopus 로고
    • Amyloid-beta binds Cu2+ in a mononuclear metal ion binding site
    • Karr JW, Kaupp LJ, Szalai VA. Amyloid-beta binds Cu2+ in a mononuclear metal ion binding site. J Am Chem Soc 2004;126:13534-13538
    • (2004) J Am Chem Soc , vol.126 , pp. 13534-13538
    • Karr, J.W.1    Kaupp, L.J.2    Szalai, V.A.3
  • 127
    • 35948936850 scopus 로고    scopus 로고
    • Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron
    • Nakamura M, Shishido N, Nunomura A, et al. Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron. Biochemistry 2007;46:12737-12743
    • (2007) Biochemistry , vol.46 , pp. 12737-12743
    • Nakamura, M.1    Shishido, N.2    Nunomura, A.3
  • 128
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain CC, Ali F, Volitakis I, et al. 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 2001;276:20466-20473
    • (2001) J Biol Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3
  • 129
    • 39749137469 scopus 로고    scopus 로고
    • Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide
    • Tougu V, Karafin A, Palumaa P. Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide. J Neurochem 2008;104:1249-1259
    • (2008) J Neurochem , vol.104 , pp. 1249-1259
    • Tougu, V.1    Karafin, A.2    Palumaa, P.3
  • 130
    • 44649174339 scopus 로고    scopus 로고
    • An observational study on the influence of the APOE-e4 allele on the correlation between 'free' copper toxicosis and EEG activity in Alzheimer disease
    • Zappasodi F, Salustri C, Babiloni C, et al. An observational study on the influence of the APOE-e4 allele on the correlation between 'free' copper toxicosis and EEG activity in Alzheimer disease. Brain Res 2008;1215:183-189
    • (2008) Brain Res , vol.1215 , pp. 183-189
    • Zappasodi, F.1    Salustri, C.2    Babiloni, C.3
  • 131
    • 0029765553 scopus 로고    scopus 로고
    • Apolipoprotein e allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides
    • Miyata M, Smith JD. Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides. Nat Genet 1996;14(1):55-61
    • (1996) Nat Genet , vol.14 , Issue.1 , pp. 55-61
    • Miyata, M.1    Smith, J.D.2
  • 132
    • 0032999810 scopus 로고    scopus 로고
    • Mounting evidence for the involvement of zinc and copper in Alzheimer's disease
    • Moir RD, Atwood CS, Huang X, et al. Mounting evidence for the involvement of zinc and copper in Alzheimer's disease. Eur J Clin Invest 1999;29:569-570
    • (1999) Eur J Clin Invest , vol.29 , pp. 569-570
    • Moir, R.D.1    Atwood, C.S.2    Huang, X.3
  • 133
    • 0033637208 scopus 로고    scopus 로고
    • Aluminum forms in drinking water and risk of Alzheimer's disease
    • Gauthier E, Fortier I, Courchesne F, et al. Aluminum forms in drinking water and risk of Alzheimer's disease. Environ Res 2000;84:234-246
    • (2000) Environ Res , vol.84 , pp. 234-246
    • Gauthier, E.1    Fortier, I.2    Courchesne, F.3
  • 134
    • 0025764799 scopus 로고
    • Aluminium, Alzheimer's disease, and drinking water
    • Neri LC, Hewitt D. Aluminium, Alzheimer's disease, and drinking water. Lancet 1991;338:390
    • (1991) Lancet , vol.338 , pp. 390
    • Neri, L.C.1    Hewitt, D.2
  • 135
    • 60149098848 scopus 로고    scopus 로고
    • Aluminum and silica in drinking water and the risk of Alzheimer's disease or cognitive decline: Findings from 15-year follow-up of the PAQUID cohort
    • Rondeau V, Jacqmin-Gadda H, Commenges D, et al. Aluminum and silica in drinking water and the risk of Alzheimer's disease or cognitive decline: findings from 15-year follow-up of the PAQUID cohort. Am J Epidemiol 2009;169:489-496
    • (2009) Am J Epidemiol , vol.169 , pp. 489-496
    • Rondeau, V.1    Jacqmin-Gadda, H.2    Commenges, D.3
  • 136
    • 0036902043 scopus 로고    scopus 로고
    • Neurotoxic effects of aluminium among foundry workers and Alzheimer's disease
    • Polizzi S, Pira E, Ferrara M, et al. Neurotoxic effects of aluminium among foundry workers and Alzheimer's disease. Neurotoxicology 2002;23:761-774
    • (2002) Neurotoxicology , vol.23 , pp. 761-774
    • Polizzi, S.1    Pira, E.2    Ferrara, M.3
  • 137
    • 70350036064 scopus 로고    scopus 로고
    • Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer's disease
    • Yumoto S, Kakimi S, Ohsaki A, Ishikawa A. Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer's disease. J Inorg Biochem 2009;103:1579-1584
    • (2009) J Inorg Biochem , vol.103 , pp. 1579-1584
    • Yumoto, S.1    Kakimi, S.2    Ohsaki, A.3    Ishikawa, A.4
  • 138
    • 3042743587 scopus 로고    scopus 로고
    • First evidence for helical transitions in supercoiled DNA by amyloid beta peptide (1-42) and aluminum: A new insight in understanding Alzheimer's disease
    • Hegde ML, Anitha S, Latha KS, et al. First evidence for helical transitions in supercoiled DNA by amyloid beta peptide (1-42) and aluminum: a new insight in understanding Alzheimer's disease. J Mol Neurosci 2004;22:19-31
    • (2004) J Mol Neurosci , vol.22 , pp. 19-31
    • Hegde, M.L.1    Anitha, S.2    Latha, K.S.3
  • 139
    • 0037069320 scopus 로고    scopus 로고
    • Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging
    • Atamna H, Killilea DW, Killilea AN, Ames BN. Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging. Proc Natl Acad Sci USA 2002;99:14807-14812
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14807-14812
    • Atamna, H.1    Killilea, D.W.2    Killilea, A.N.3    Ames, B.N.4
  • 140
    • 84863985242 scopus 로고    scopus 로고
    • Aluminium exposure induces Alzheimer's disease-like histopathological alterations in mouse brain
    • Rodella LF, Ricci F, Borsani E, et al. Aluminium exposure induces Alzheimer's disease-like histopathological alterations in mouse brain. Histol Histopathol 2008;23:433-439
    • (2008) Histol Histopathol , vol.23 , pp. 433-439
    • Rodella, L.F.1    Ricci, F.2    Borsani, E.3
  • 141
    • 0036634409 scopus 로고    scopus 로고
    • Aluminum modulates brain amyloidosis through oxidative stress in APP transgenic mice
    • Pratico D, Uryu K, Sung S, et al. Aluminum modulates brain amyloidosis through oxidative stress in APP transgenic mice. FASEB J 2002;16:1138-1140
    • (2002) FASEB J , vol.16 , pp. 1138-1140
    • Pratico, D.1    Uryu, K.2    Sung, S.3
  • 142
    • 56349087892 scopus 로고    scopus 로고
    • Effects of oral aluminum exposure on behavior and neurogenesis in a transgenic mouse model of Alzheimer's disease
    • Ribes D, Colomina MT, Vicens P, Domingo JL. Effects of oral aluminum exposure on behavior and neurogenesis in a transgenic mouse model of Alzheimer's disease. Exp Neurol 2008;214:293-300
    • (2008) Exp Neurol , vol.214 , pp. 293-300
    • Ribes, D.1    Colomina, M.T.2    Vicens, P.3    Domingo, J.L.4
  • 143
    • 54249163572 scopus 로고    scopus 로고
    • Aluminum modulates effects of betaamyloid1-42 on neuronal calcium homeostasis and mitochondria functioning and is altered in a triple transgenic mouse model of Alzheimer's disease
    • Drago D, Cavaliere A, Mascetra N, et al. Aluminum modulates effects of betaamyloid1-42 on neuronal calcium homeostasis and mitochondria functioning and is altered in a triple transgenic mouse model of Alzheimer's disease. Rejuvenation Res 2008;11:861-871
    • (2008) Rejuvenation Res , vol.11 , pp. 861-871
    • Drago, D.1    Cavaliere, A.2    Mascetra, N.3
  • 144
    • 0036813102 scopus 로고    scopus 로고
    • The degradation of Abeta (25-35) by the serine protease plasmin is inhibited by aluminium
    • Korchazhkina OV, Ashcroft AE, Kiss T, Exley C. The degradation of Abeta (25-35) by the serine protease plasmin is inhibited by aluminium. J Alzheimers Dis 2002;4:357-367
    • (2002) J Alzheimers Dis , vol.4 , pp. 357-367
    • Korchazhkina, O.V.1    Ashcroft, A.E.2    Kiss, T.3    Exley, C.4
  • 145
    • 33646180185 scopus 로고    scopus 로고
    • Aluminum in hippocampal neurons from humans with Alzheimer's disease
    • Walton JR. Aluminum in hippocampal neurons from humans with Alzheimer's disease. Neurotoxicology 2006;27:385-394
    • (2006) Neurotoxicology , vol.27 , pp. 385-394
    • Walton, J.R.1
  • 146
    • 0018827099 scopus 로고
    • Alzheimer's disease: X-ray spectrometric evidence of aluminum accumulation in neurofibrillary tangle-bearing neurons
    • Perl DP, Brody AR. Alzheimer's disease: X-ray spectrometric evidence of aluminum accumulation in neurofibrillary tangle-bearing neurons. Science 1980;208:297-299
    • (1980) Science , vol.208 , pp. 297-299
    • Perl, D.P.1    Brody, A.R.2
  • 147
    • 0026515734 scopus 로고
    • Aluminium accumulation in relation to senile plaque and neurofibrillary tangle formation in the brains of patients with renal failure
    • Candy JM, McArthur FK, Oakley AE, et al. Aluminium accumulation in relation to senile plaque and neurofibrillary tangle formation in the brains of patients with renal failure. J Neurol Sci 1992;107:210-218
    • (1992) J Neurol Sci , vol.107 , pp. 210-218
    • Candy, J.M.1    McArthur, F.K.2    Oakley, A.E.3
  • 148
    • 0033591309 scopus 로고    scopus 로고
    • Potentiation of beta-folding of beta-amyloid peptide 25-35 by aluminum salts
    • Bondy SC, Truong A. Potentiation of beta-folding of beta-amyloid peptide 25-35 by aluminum salts. Neurosci Lett 1999;267:25-28
    • (1999) Neurosci Lett , vol.267 , pp. 25-28
    • Bondy, S.C.1    Truong, A.2
  • 149
    • 0028000280 scopus 로고
    • The solubilization of model Alzheimer tangles: Reversing the beta-sheet conformation induced by aluminum with silicates
    • Fasman GD, Moore CD. The solubilization of model Alzheimer tangles: reversing the beta-sheet conformation induced by aluminum with silicates. Proc Natl Acad Sci USA 1994;91:11232-11235
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11232-11235
    • Fasman, G.D.1    Moore, C.D.2
  • 150
    • 3042666730 scopus 로고    scopus 로고
    • Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease
    • House E, Collingwood J, Khan A, et al. Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease. J Alzheimers Dis 2004;6:291-301
    • (2004) J Alzheimers Dis , vol.6 , pp. 291-301
    • House, E.1    Collingwood, J.2    Khan, A.3
  • 151
    • 2942750367 scopus 로고    scopus 로고
    • Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: Structural characterization of its zinc(II) and copper (II) complexes
    • Di Vaira M, Bazzicalupi C, Orioli P, et al. Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: structural characterization of its zinc(II) and copper (II) complexes. Inorg Chem 2004;43:3795-3797
    • (2004) Inorg Chem , vol.43 , pp. 3795-3797
    • Di Vaira, M.1    Bazzicalupi, C.2    Orioli, P.3
  • 152
    • 18144374793 scopus 로고    scopus 로고
    • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid beta peptide
    • Raman B, Ban T, Yamaguchi K, et al. Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid beta peptide. J Biol Chem 2005;280:16157-16162
    • (2005) J Biol Chem , vol.280 , pp. 16157-16162
    • Raman, B.1    Ban, T.2    Yamaguchi, K.3
  • 153
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999;400:173-177
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 154
    • 10644280708 scopus 로고    scopus 로고
    • Clioquinol mediates copper uptake and counteracts copper efflux activities of the amyloid precursor protein of Alzheimer's disease
    • Treiber C, Simons A, Strauss M, et al. Clioquinol mediates copper uptake and counteracts copper efflux activities of the amyloid precursor protein of Alzheimer's disease. J Biol Chem 2004;279:51958-51964
    • (2004) J Biol Chem , vol.279 , pp. 51958-51964
    • Treiber, C.1    Simons, A.2    Strauss, M.3
  • 155
    • 0030704680 scopus 로고    scopus 로고
    • Zinc-induced Alzheimer's Abeta1-40 aggregation is mediated by conformational factors
    • Huang X, Atwood CS, Moir RD, et al. Zinc-induced Alzheimer's Abeta1-40 aggregation is mediated by conformational factors. J Biol Chem 1997;272:26464-26470
    • (1997) J Biol Chem , vol.272 , pp. 26464-26470
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3
  • 156
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 2001;30:665-676
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 157
    • 0036860349 scopus 로고    scopus 로고
    • Metal complexing agents as therapies for Alzheimer's disease
    • Bush AI. Metal complexing agents as therapies for Alzheimer's disease. Neurobiol Aging 2002;23:1031-1038
    • (2002) Neurobiol Aging , vol.23 , pp. 1031-1038
    • Bush, A.I.1
  • 158
    • 58649090275 scopus 로고    scopus 로고
    • The anti-neurodegeneration drug clioquinol inhibits the aging-associated protein CLK-1
    • Wang Y, Branicky R, Stepanyan Z, et al. The anti-neurodegeneration drug clioquinol inhibits the aging-associated protein CLK-1. J Biol Chem 2009;284:314-323
    • (2009) J Biol Chem , vol.284 , pp. 314-323
    • Wang, Y.1    Branicky, R.2    Stepanyan, Z.3
  • 159
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush AI. The metallobiology of Alzheimer's disease. Trends Neurosci 2003;26:207-214
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 160
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: A pilot Phase 2 clinical trial
    • Ritchie CW, Bush AI, Mackinnon A, et al. Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: a pilot Phase 2 clinical trial. Arch Neurol 2003;60:1685-1691
    • (2003) Arch Neurol , vol.60 , pp. 1685-1691
    • Ritchie, C.W.1    Bush, A.I.2    MacKinnon, A.3
  • 161
    • 63149091152 scopus 로고    scopus 로고
    • Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease
    • Rodriguez-Rodriguez C, Sanchez de Groot N, Rimola A, et al. Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease. J Am Chem Soc 2009;131:1436-1451
    • (2009) J Am Chem Soc , vol.131 , pp. 1436-1451
    • Rodriguez-Rodriguez, C.1    Sanchez De Groot, N.2    Rimola, A.3
  • 162
    • 44949217583 scopus 로고    scopus 로고
    • Metal protein attenuating compounds for the treatment of Alzheimer's disease
    • Sampson E, Jenagaratnam L, McShane R. Metal protein attenuating compounds for the treatment of Alzheimer's disease. Cochrane Database Syst Rev 2008;(1):CD005380
    • (2008) Cochrane Database Syst Rev , Issue.1
    • Sampson, E.1    Jenagaratnam, L.2    McShane, R.3
  • 163
    • 46149107512 scopus 로고    scopus 로고
    • Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Abeta
    • Adlard PA, Cherny RA, Finkelstein DI, et al. Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Abeta. Neuron 2008;59:43-55
    • (2008) Neuron , vol.59 , pp. 43-55
    • Adlard, P.A.1    Cherny, R.A.2    Finkelstein, D.I.3
  • 164
    • 77954344206 scopus 로고    scopus 로고
    • PBT2 rapidly improves cognition in Alzheimer's disease: Additional Phase II analyses
    • Faux NG, Ritchie CW, Gunn A, et al. PBT2 rapidly improves cognition in Alzheimer's disease: additional Phase II analyses. J Alzheimers Dis 2010;20:509-516
    • (2010) J Alzheimers Dis , vol.20 , pp. 509-516
    • Faux, N.G.1    Ritchie, C.W.2    Gunn, A.3
  • 165
    • 48949098573 scopus 로고    scopus 로고
    • Safety, efficacy, and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimer's disease: A phase IIa, double-blind, randomised, placebo-controlled trial
    • Lannfelt L, Blennow K, Zetterberg H, et al. Safety, efficacy, and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial. Lancet Neurol 2008;7:779-786
    • (2008) Lancet Neurol , vol.7 , pp. 779-786
    • Lannfelt, L.1    Blennow, K.2    Zetterberg, H.3
  • 166
    • 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 JY, Friedman JE, Angel I, et al. The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice. Neurobiol Aging 2004;25:1315-1321
    • (2004) Neurobiol Aging , vol.25 , pp. 1315-1321
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3
  • 167
    • 9644275375 scopus 로고    scopus 로고
    • A new strategy to combat Alzheimer's disease. Combining radical-scavenging potential with metal-protein-attenuating ability in one molecule
    • Ji HF, Zhang HY. A new strategy to combat Alzheimer's disease. Combining radical-scavenging potential with metal-protein-attenuating ability in one molecule. Bioorg Med Chem Lett 2005;15:21-24
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 21-24
    • Ji, H.F.1    Zhang, H.Y.2
  • 168
    • 57449119060 scopus 로고    scopus 로고
    • Physiological and pathological aspects of Abeta in iron homeostasis via 5¢UTR in the APP mRNA and the therapeutic use of iron-chelators
    • Avramovich-Tirosh Y, Amit T, Bar-Am O, et al. Physiological and pathological aspects of Abeta in iron homeostasis via 5¢UTR in the APP mRNA and the therapeutic use of iron-chelators. BMC Neurosci 2008;9(Suppl 2):S2
    • (2008) BMC Neurosci , vol.9 , Issue.SUPPL. 2
    • Avramovich-Tirosh, Y.1    Amit, T.2    Bar-Am, O.3
  • 169
    • 0033974529 scopus 로고    scopus 로고
    • Changes in uptake of vitamin B12 and trace metals in brains of mice treated with clioquinol
    • Yassin MS, Ekblom J, Xilinas M, et al. Changes in uptake of vitamin B12 and trace metals in brains of mice treated with clioquinol. J Neurol Sci 2000;173:40-44
    • (2000) J Neurol Sci , vol.173 , pp. 40-44
    • Yassin, M.S.1    Ekblom, J.2    Xilinas, M.3
  • 170
    • 0042021925 scopus 로고    scopus 로고
    • Current status of metals as therapeutic targets in Alzheimer's disease
    • Finefrock AE, Bush AI, Doraiswamy PM. Current status of metals as therapeutic targets in Alzheimer's disease. J Am Geriatr Soc 2003;51:1143-1148
    • (2003) J Am Geriatr Soc , vol.51 , pp. 1143-1148
    • Finefrock, A.E.1    Bush, A.I.2    Doraiswamy, P.M.3
  • 171
    • 0025726462 scopus 로고
    • Intramuscular desferrioxamine in patients with Alzheimer's disease
    • Crapper McLachlan DR, Dalton AJ, Kruck TP, et al. Intramuscular desferrioxamine in patients with Alzheimer's disease. Lancet 1991;337:1304-1308
    • (1991) Lancet , vol.337 , pp. 1304-1308
    • Crapper McLachlan, D.R.1    Dalton, A.J.2    Kruck, T.P.3
  • 172
    • 0034527983 scopus 로고    scopus 로고
    • Metal chelation as a potential therapy for Alzheimer's disease
    • Cuajungco MP, Faget KY, Huang X, et al. Metal chelation as a potential therapy for Alzheimer's disease. Ann NY Acad Sci 2000;920:292-304
    • (2000) Ann NY Acad Sci , vol.920 , pp. 292-304
    • Cuajungco, M.P.1    Faget, K.Y.2    Huang, X.3
  • 173
    • 33748756621 scopus 로고    scopus 로고
    • Aluminum and other metals in Alzheimer's disease: A review of potential therapy with chelating agents
    • Domingo JL. Aluminum and other metals in Alzheimer's disease: a review of potential therapy with chelating agents. J Alzheimers Dis 2006;10:331-341
    • (2006) J Alzheimers Dis , vol.10 , pp. 331-341
    • Domingo, J.L.1
  • 174
    • 33845879870 scopus 로고    scopus 로고
    • Therapeutic targets and potential of the novel brain- permeable multifunctional iron chelator-monoamine oxidase inhbitor drug, M-30, for the treatment of Alzheimer's disease
    • Avramovich-Tirosh Y, Amit T, Bar-Am O, et al. Therapeutic targets and potential of the novel brain- permeable multifunctional iron chelator-monoamine oxidase inhbitor drug, M-30, for the treatment of Alzheimer's disease. J Neurochem 2006;100:490-502
    • (2006) J Neurochem , vol.100 , pp. 490-502
    • Avramovich-Tirosh, Y.1    Amit, T.2    Bar-Am, O.3
  • 175
    • 77953826537 scopus 로고    scopus 로고
    • Up-regulation of hypoxia-inducible factor (HIF) -1beta and HIF-target genes in cortical neurons by the Novel Multifunctional Iron Chelator Anti-Alzheimer Drug, M30
    • Avramovich-Tirosh Y, Bar-Am O, Amit T, et al. Up-regulation of hypoxia-inducible factor (HIF) -1beta and HIF-target genes in cortical neurons by the Novel Multifunctional Iron Chelator Anti-Alzheimer Drug, M30. Curr Alzheimer Res 2010;7:300-306
    • (2010) Curr Alzheimer Res , vol.7 , pp. 300-306
    • Avramovich-Tirosh, Y.1    Bar-Am, O.2    Amit, T.3
  • 176
    • 12244296145 scopus 로고    scopus 로고
    • Rasagiline: Neurodegeneration, neuroprotection, and mitochondrial permeability transition
    • Youdim MB, Bar Am O, Yogev-Falach M, et al. Rasagiline: neurodegeneration, neuroprotection, and mitochondrial permeability transition. J Neurosci Res 2005;79:172-179
    • (2005) J Neurosci Res , vol.79 , pp. 172-179
    • Youdim, M.B.1    Bar Am, O.2    Yogev-Falach, M.3
  • 177
    • 9744219638 scopus 로고    scopus 로고
    • Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis
    • Dedeoglu A, Cormier K, Payton S, et al. Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis. Exp Gerontol 2004;39:1641-1649
    • (2004) Exp Gerontol , vol.39 , pp. 1641-1649
    • Dedeoglu, A.1    Cormier, K.2    Payton, S.3
  • 178
    • 64549084963 scopus 로고    scopus 로고
    • Glycosylated tetrahydrosalens as multifunctional molecules for Alzheimer's therapy
    • Storr T, Scott LE, Bowen ML, et al. Glycosylated tetrahydrosalens as multifunctional molecules for Alzheimer's therapy. Dalton Trans 2009;28:3034-3043
    • (2009) Dalton Trans , vol.28 , pp. 3034-3043
    • Storr, T.1    Scott, L.E.2    Bowen, M.L.3
  • 179
    • 34347237264 scopus 로고    scopus 로고
    • Synthesis, characterization, and metal coordinating ability of multifunctional carbohydrate-containing compounds for Alzheimer's therapy
    • Storr T, Merkel M, Song-Zhao GX, et al. Synthesis, characterization, and metal coordinating ability of multifunctional carbohydrate-containing compounds for Alzheimer's therapy. J Am Chem Soc 2007;129:7453-7463
    • (2007) J Am Chem Soc , vol.129 , pp. 7453-7463
    • Storr, T.1    Merkel, M.2    Song-Zhao, G.X.3
  • 180
    • 76749124448 scopus 로고    scopus 로고
    • In vitro studies of 3-hydroxy-4- pyridinones and their glycosylated derivatives as potential agents for Alzheimer's disease
    • Green DE, Bowen ML, Scott LE, et al. In vitro studies of 3-hydroxy-4- pyridinones and their glycosylated derivatives as potential agents for Alzheimer's disease. Dalton Trans 2010;39:1604-1615
    • (2010) Dalton Trans , vol.39 , pp. 1604-1615
    • Green, D.E.1    Bowen, M.L.2    Scott, L.E.3
  • 181
    • 34248208975 scopus 로고    scopus 로고
    • Combating Alzheimer's disease with multifunctional molecules designed for metal passivation
    • Schugar H, Green DE, Bowen ML, et al. Combating Alzheimer's disease with multifunctional molecules designed for metal passivation. Angew Chem Int Ed Engl 2007;46:1716-1718
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 1716-1718
    • Schugar, H.1    Green, D.E.2    Bowen, M.L.3
  • 182
    • 39149091398 scopus 로고    scopus 로고
    • Multi-target-directed ligands to combat neurodegenerative diseases
    • Cavalli A, Bolognesi ML, Minarini A, et al. Multi-target-directed ligands to combat neurodegenerative diseases. J Med Chem 2008;51:347-372
    • (2008) J Med Chem , vol.51 , pp. 347-372
    • Cavalli, A.1    Bolognesi, M.L.2    Minarini, A.3
  • 183
    • 57649130599 scopus 로고    scopus 로고
    • Sequestration of copper from beta-amyloid promotes selective lysis by cyclen-hybrid cleavage agents
    • Wu WH, Lei P, Liu Q, et al. Sequestration of copper from beta-amyloid promotes selective lysis by cyclen-hybrid cleavage agents. J Biol Chem 2008;283:31657-31664
    • (2008) J Biol Chem , vol.283 , pp. 31657-31664
    • Wu, W.H.1    Lei, P.2    Liu, Q.3
  • 184
    • 0024347923 scopus 로고
    • Tetrahydroaminoacridine (THA) as a pharmacological probe in Alzheimer's disease (AD) and other neurodegenerative disorders
    • Sattin A, Muhoberac BB, Aprison MH, Schauf CL. Tetrahydroaminoacridine (THA) as a pharmacological probe in Alzheimer's disease (AD) and other neurodegenerative disorders. Med Hypotheses 1989;29:155-159
    • (1989) Med Hypotheses , vol.29 , pp. 155-159
    • Sattin, A.1    Muhoberac, B.B.2    Aprison, M.H.3    Schauf, C.L.4
  • 185
    • 0037462303 scopus 로고    scopus 로고
    • A novel trivalent cation chelator Feralex dissociates binding of aluminum and iron associated with hyperphosphorylated tau of Alzheimer's disease
    • Shin RW, Kruck TP, Murayama H, Kitamoto T. A novel trivalent cation chelator Feralex dissociates binding of aluminum and iron associated with hyperphosphorylated tau of Alzheimer's disease. Brain Res 2003;96:139-146
    • (2003) Brain Res , vol.96 , pp. 139-146
    • Shin, R.W.1    Kruck, T.P.2    Murayama, H.3    Kitamoto, T.4
  • 187
    • 64049104164 scopus 로고    scopus 로고
    • Nanoparticle-chelator conjugates as inhibitors of amyloid-beta aggregation and neurotoxicity: A novel therapeutic approach for Alzheimer disease
    • Liu G, Men P, Kudo W, et al. Nanoparticle-chelator conjugates as inhibitors of amyloid-beta aggregation and neurotoxicity: a novel therapeutic approach for Alzheimer disease. Neurosci Lett 2009;455:187-190
    • (2009) Neurosci Lett , vol.455 , pp. 187-190
    • Liu, G.1    Men, P.2    Kudo, W.3
  • 188
    • 33748202940 scopus 로고    scopus 로고
    • Nanoparticle iron chelators: A new therapeutic approach in Alzheimer disease and other neurologic disorders associated with trace metal imbalance
    • Liu G, Men P, Harris PL, et al. Nanoparticle iron chelators: a new therapeutic approach in Alzheimer disease and other neurologic disorders associated with trace metal imbalance. Neurosci Lett 2006;406:189-193
    • (2006) Neurosci Lett , vol.406 , pp. 189-193
    • Liu, G.1    Men, P.2    Harris, P.L.3
  • 189
    • 25144481422 scopus 로고    scopus 로고
    • Nanoparticle and other metal chelation therapeutics in Alzheimer disease
    • Liu G, Garrett MR, Men P, et al. Nanoparticle and other metal chelation therapeutics in Alzheimer disease. Biochim Biophys Acta 2005;1741:246-252
    • (2005) Biochim Biophys Acta , vol.1741 , pp. 246-252
    • Liu, G.1    Garrett, M.R.2    Men, P.3
  • 190
    • 77449089898 scopus 로고    scopus 로고
    • Nanoparticle and iron chelators as a potential novel Alzheimer therapy
    • Liu G, Men P, Perry G, Smith MA. Nanoparticle and iron chelators as a potential novel Alzheimer therapy. Methods Mol Biol 2010;610:123-144
    • (2010) Methods Mol Biol , vol.610 , pp. 123-144
    • Liu, G.1    Men, P.2    Perry, G.3    Smith, M.A.4
  • 191
    • 41949115990 scopus 로고    scopus 로고
    • Selective intracellular release of copper and zinc ions from bis (thiosemicarbazonato) complexes reduces levels of Alzheimer disease amyloid-beta peptide
    • Donnelly PS, Caragounis A, Du T, et al. Selective intracellular release of copper and zinc ions from bis (thiosemicarbazonato) complexes reduces levels of Alzheimer disease amyloid-beta peptide. J Biol Chem 2008;283:4568-4577
    • (2008) J Biol Chem , vol.283 , pp. 4568-4577
    • Donnelly, P.S.1    Caragounis, A.2    Du, T.3
  • 192
    • 0017877241 scopus 로고
    • Stability and structure of binary and ternary complexes of alpha-lipoate and lipoate derivatives with Mn2+, Cu2+, and Zn2+ in solution
    • Sigel H, Prijs B, McCormick DB, Shih JC. Stability and structure of binary and ternary complexes of alpha-lipoate and lipoate derivatives with Mn2+, Cu2+, and Zn2+ in solution. Arch Biochem Biophys 1978;187:208-214
    • (1978) Arch Biochem Biophys , vol.187 , pp. 208-214
    • Sigel, H.1    Prijs, B.2    McCormick, D.B.3    Shih, J.C.4
  • 193
    • 0029031443 scopus 로고
    • Thioctic (lipoic) acid: A therapeutic metal-chelating antioxidant?
    • Ou P, Tritschler HJ, Wolff SP. Thioctic (lipoic) acid: a therapeutic metal-chelating antioxidant? Biochem Pharmacol 1995;50:123-126
    • (1995) Biochem Pharmacol , vol.50 , pp. 123-126
    • Ou, P.1    Tritschler, H.J.2    Wolff, S.P.3
  • 194
    • 0142010609 scopus 로고    scopus 로고
    • Protection against amyloid beta peptide and iron/hydrogen peroxide toxicity by alpha lipoic acid
    • Lovell MA, Xie C, Xiong S, Markesbery WR. Protection against amyloid beta peptide and iron/hydrogen peroxide toxicity by alpha lipoic acid. J Alzheimers Dis 2003;5:229-239
    • (2003) J Alzheimers Dis , vol.5 , pp. 229-239
    • Lovell, M.A.1    Xie, C.2    Xiong, S.3    Markesbery, W.R.4
  • 195
    • 47249106357 scopus 로고    scopus 로고
    • Lipoic acid: A novel therapeutic approach for multiple sclerosis and other chronic inflammatory diseases of the CNS
    • Salinthone S, Yadav V, Bourdette DN, Carr DW. Lipoic acid: a novel therapeutic approach for multiple sclerosis and other chronic inflammatory diseases of the CNS. Endocr Metab Immune Disord Drug Targets 2008;8:132-142
    • (2008) Endocr Metab Immune Disord Drug Targets , vol.8 , pp. 132-142
    • Salinthone, S.1    Yadav, V.2    Bourdette, D.N.3    Carr, D.W.4
  • 196
    • 33845442944 scopus 로고    scopus 로고
    • Chronic dietary alpha-lipoic acid reduces deficits in hippocampal memory of aged Tg2576 mice
    • Quinn JF, Bussiere JR, Hammond RS, et al. Chronic dietary alpha-lipoic acid reduces deficits in hippocampal memory of aged Tg2576 mice. Neurobiol Aging 2007;28:213-225
    • (2007) Neurobiol Aging , vol.28 , pp. 213-225
    • Quinn, J.F.1    Bussiere, J.R.2    Hammond, R.S.3
  • 197
    • 56349157854 scopus 로고    scopus 로고
    • Benefits from dietary polyphenols for brain aging and Alzheimer's disease
    • Rossi L, Mazzitelli S, Arciello M, et al. Benefits from dietary polyphenols for brain aging and Alzheimer's disease. Neurochem Res 2008;33:2390-2400
    • (2008) Neurochem Res , vol.33 , pp. 2390-2400
    • Rossi, L.1    Mazzitelli, S.2    Arciello, M.3
  • 198
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim GP, Chu T, Yang F, et al. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci 2001;21:8370-8377
    • (2001) J Neurosci , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3
  • 199
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid beta peptide
    • Smith DG, Cappai R, Barnham KJ. The redox chemistry of the Alzheimer's disease amyloid beta peptide. Biochim Biophys Acta 2007;1768:1976-1990
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 200
    • 56049088324 scopus 로고    scopus 로고
    • Simultaneous manipulation of multiple brain targets by green tea catechins: A potential neuroprotective strategy for Alzheimer and Parkinson diseases
    • Mandel SA, Amit T, Weinreb O, et al. Simultaneous manipulation of multiple brain targets by green tea catechins: a potential neuroprotective strategy for Alzheimer and Parkinson diseases. CNS Neurosci Ther 2008;14:352-365
    • (2008) CNS Neurosci Ther , vol.14 , pp. 352-365
    • Mandel, S.A.1    Amit, T.2    Weinreb, O.3
  • 201
    • 44249116000 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice
    • Rezai-Zadeh K, Arendash GW, Hou H, et al. Green tea epigallocatechin-3- gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice. Brain Res 2008;1214:177-187
    • (2008) Brain Res , vol.1214 , pp. 177-187
    • Rezai-Zadeh, K.1    Arendash, G.W.2    Hou, H.3
  • 202
    • 33745209915 scopus 로고    scopus 로고
    • ADAM10 activation is required for green tea (-)-epigallocatechin-3- gallateinduced alpha-secretase cleavage of amyloid precursor protein
    • Obregon DF, Rezai-Zadeh K, Bai Y, et al. ADAM10 activation is required for green tea (-)-epigallocatechin-3-gallateinduced alpha-secretase cleavage of amyloid precursor protein. J Biol Chem 2006;281:16419-16427
    • (2006) J Biol Chem , vol.281 , pp. 16419-16427
    • Obregon, D.F.1    Rezai-Zadeh, K.2    Bai, Y.3
  • 203
    • 0036725818 scopus 로고    scopus 로고
    • Risk factors for Alzheimer's disease: A prospective analysis from the Canadian Study of Health and Aging
    • Lindsay J, Laurin D, Verreault R, et al. Risk factors for Alzheimer's disease: a prospective analysis from the Canadian Study of Health and Aging. Am J Epidemiol 2002;156:445-453
    • (2002) Am J Epidemiol , vol.156 , pp. 445-453
    • Lindsay, J.1    Laurin, D.2    Verreault, R.3
  • 204
    • 0030977937 scopus 로고    scopus 로고
    • Wine consumption and dementia in the elderly: A prospective community study in the Bordeaux area
    • Orgogozo JM, Dartigues JF, Lafont S, et al. Wine consumption and dementia in the elderly: a prospective community study in the Bordeaux area. Rev Neurol (Paris) 1997;153:185-192
    • (1997) Rev Neurol (Paris) , vol.153 , pp. 185-192
    • Orgogozo, J.M.1    Dartigues, J.F.2    Lafont, S.3
  • 205
    • 0037069290 scopus 로고    scopus 로고
    • Amount and type of alcohol and risk of dementia: The Copenhagen City Heart Study
    • Truelsen T, Thudium D, Gronbaek M. Amount and type of alcohol and risk of dementia: the Copenhagen City Heart Study. Neurology 2002;59:1313-1319
    • (2002) Neurology , vol.59 , pp. 1313-1319
    • Truelsen, T.1    Thudium, D.2    Gronbaek, M.3
  • 206
    • 77950575506 scopus 로고    scopus 로고
    • AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-beta peptide metabolism
    • Vingtdeux V, Giliberto L, Zhao H, et al. AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-beta peptide metabolism. J Biol Chem 2010;285:9100-9113
    • (2010) J Biol Chem , vol.285 , pp. 9100-9113
    • Vingtdeux, V.1    Giliberto, L.2    Zhao, H.3
  • 207
    • 0346688728 scopus 로고    scopus 로고
    • Reduced risk of Alzheimer disease in users of antioxidant vitamin supplements: The Cache County Study
    • Zandi PP, Anthony JC, Khachaturian AS, et al. Reduced risk of Alzheimer disease in users of antioxidant vitamin supplements: the Cache County Study. Arch Neurol 2004;61:82-88
    • (2004) Arch Neurol , vol.61 , pp. 82-88
    • Zandi, P.P.1    Anthony, J.C.2    Khachaturian, A.S.3
  • 208
    • 16544373763 scopus 로고    scopus 로고
    • Gossypin protects primary cultured rat cortical cells from oxidative stress- and β-amyloid-induced toxicity
    • Yoon I, Lee KH, Cho J. Gossypin protects primary cultured rat cortical cells from oxidative stress- and beta-amyloid-induced toxicity. Arch Pharm Res 2004;27:454-459 (Pubitemid 43073744)
    • (2004) Archives of Pharmacal Research , vol.27 , Issue.4 , pp. 454-459
    • Yoon, I.1    Kwang, H.L.2    Cho, J.3
  • 209
    • 0031788259 scopus 로고    scopus 로고
    • The efficacy of Ginkgo biloba on cognitive function in Alzheimer disease
    • Oken BS, Storzbach DM, Kaye JA. The efficacy of Ginkgo biloba on cognitive function in Alzheimer disease. Arch Neurol 1998;55:1409-1415
    • (1998) Arch Neurol , vol.55 , pp. 1409-1415
    • Oken, B.S.1    Storzbach, D.M.2    Kaye, J.A.3
  • 210
    • 33644839704 scopus 로고    scopus 로고
    • Melatonin and 6-hydroxymelatonin protect against iron-induced neurotoxicity
    • Maharaj DS, Maharaj H, Daya S, Glass BD. Melatonin and 6-hydroxymelatonin protect against iron-induced neurotoxicity. J Neurochem 2006;96:78-81
    • (2006) J Neurochem , vol.96 , pp. 78-81
    • Maharaj, D.S.1    Maharaj, H.2    Daya, S.3    Glass, B.D.4
  • 211
    • 0037159210 scopus 로고    scopus 로고
    • Elevation of serum copper levels in Alzheimer's disease
    • Squitti R, Lupoi D, Pasqualetti P, et al. Elevation of serum copper levels in Alzheimer's disease. Neurology 2002;59:1153-1161
    • (2002) Neurology , vol.59 , pp. 1153-1161
    • Squitti, R.1    Lupoi, D.2    Pasqualetti, P.3
  • 212
    • 0037003044 scopus 로고    scopus 로고
    • D-penicillamine reduces serum oxidative stress in Alzheimer's disease patients
    • Squitti R, Rossini PM, Cassetta E, et al. D-penicillamine reduces serum oxidative stress in Alzheimer's disease patients. Eur J Clin Invest 2002;32:51-59
    • (2002) Eur J Clin Invest , vol.32 , pp. 51-59
    • Squitti, R.1    Rossini, P.M.2    Cassetta, E.3
  • 213
    • 0022870125 scopus 로고
    • Treatment of Wilson's disease with zinc. II. Validation of oral 64copper with copper balance
    • Hill GM, Brewer GJ, Juni JE, et al. Treatment of Wilson's disease with zinc. II. Validation of oral 64copper with copper balance. Am J Med Sci 1986;292:344-349
    • (1986) Am J Med Sci , vol.292 , pp. 344-349
    • Hill, G.M.1    Brewer, G.J.2    Juni, J.E.3
  • 214
    • 77649181022 scopus 로고    scopus 로고
    • Copper toxicity in the general population
    • Brewer GJ. Copper toxicity in the general population. Clin Neurophysiol 2010;121:459-460
    • (2010) Clin Neurophysiol , vol.121 , pp. 459-460
    • Brewer, G.J.1
  • 215
    • 70449514549 scopus 로고    scopus 로고
    • Anti-copper therapies in Alzheimer's disease: New concepts
    • Squitti R, Zito G. Anti-copper therapies in Alzheimer's disease: new concepts. Recent Pat CNS Drug Discov 2009;4:209-219
    • (2009) Recent Pat CNS Drug Discov , vol.4 , pp. 209-219
    • Squitti, R.1    Zito, G.2
  • 216
    • 43249100611 scopus 로고    scopus 로고
    • Targeting multiple Alzheimer's disease etiologies with multimodal neuroprotective and neurorestorative iron chelators
    • Amit T, Avramovich-Tirosh Y, Youdim MB, Mandel S. Targeting multiple Alzheimer's disease etiologies with multimodal neuroprotective and neurorestorative iron chelators. FASEB J 2008;22:1296-1305
    • (2008) FASEB J , vol.22 , pp. 1296-1305
    • Amit, T.1    Avramovich-Tirosh, Y.2    Youdim, M.B.3    Mandel, S.4
  • 217
    • 14944372817 scopus 로고    scopus 로고
    • FDA-preapproved drugs targeted to the translational regulation and processing of the amyloid precursor protein
    • Morse LJ, Payton SM, Cuny GD, Rogers JT. FDA-preapproved drugs targeted to the translational regulation and processing of the amyloid precursor protein. J Mol Neurosci 2004;24:129-136
    • (2004) J Mol Neurosci , vol.24 , pp. 129-136
    • Morse, L.J.1    Payton, S.M.2    Cuny, G.D.3    Rogers, J.T.4
  • 218
    • 67649371133 scopus 로고    scopus 로고
    • The use of copper-lowering therapy with tetrathiomolybdate in medicine
    • Brewer GJ. The use of copper-lowering therapy with tetrathiomolybdate in medicine. Expert Opin Investig Drugs 2009;18:89-97
    • (2009) Expert Opin Investig Drugs , vol.18 , pp. 89-97
    • Brewer, G.J.1
  • 219
    • 24644497684 scopus 로고    scopus 로고
    • Anticholinesterase and pharmacokinetic profile of phenserine in healthy elderly human subjects
    • Greig NH, Ruckle J, Comer P, et al. Anticholinesterase and pharmacokinetic profile of phenserine in healthy elderly human subjects. Curr Alzheimer Res 2005;2:483-492
    • (2005) Curr Alzheimer Res , vol.2 , pp. 483-492
    • Greig, N.H.1    Ruckle, J.2    Comer, P.3
  • 220
    • 33747089589 scopus 로고    scopus 로고
    • A high-throughput drug screen targeted to the 5¢untranslated region of Alzheimer amyloid precursor protein mRNA
    • Bandyopadhyay S, Ni J, Ruggiero A, et al. A high-throughput drug screen targeted to the 5¢untranslated region of Alzheimer amyloid precursor protein mRNA. J Biomol Screen 2006;11:469-480
    • (2006) J Biomol Screen , vol.11 , pp. 469-480
    • Bandyopadhyay, S.1    Ni, J.2    Ruggiero, A.3
  • 221
    • 0035877756 scopus 로고    scopus 로고
    • Early-onset amyloid deposition and cognitive deficits in transgenic mice expressing a double mutant form of amyloid precursor protein 695
    • Chishti MA, Yang DS, Janus C, et al. Early-onset amyloid deposition and cognitive deficits in transgenic mice expressing a double mutant form of amyloid precursor protein 695. J Biol Chem 2001;276:21562-21570
    • (2001) J Biol Chem , vol.276 , pp. 21562-21570
    • Chishti, M.A.1    Yang, D.S.2    Janus, C.3
  • 222
    • 0028873173 scopus 로고
    • Iron levels modulate alpha-secretase cleavage of amyloid precursor protein
    • Bodovitz S, Falduto MT, Frail DE, Klein WL. Iron levels modulate alpha-secretase cleavage of amyloid precursor protein. J Neurochem 1995;64:307-315
    • (1995) J Neurochem , vol.64 , pp. 307-315
    • Bodovitz, S.1    Falduto, M.T.2    Frail, D.E.3    Klein, W.L.4
  • 223
    • 36749037180 scopus 로고    scopus 로고
    • Role of the APP non-amyloidogenic signaling pathway and targeting alpha-secretase as an alternative drug target for treatment of Alzheimer's disease
    • Bandyopadhyay S, Goldstein LE, Lahiri DK, Rogers JT. Role of the APP non-amyloidogenic signaling pathway and targeting alpha-secretase as an alternative drug target for treatment of Alzheimer's disease. Curr Med Chem 2007;14:2848-2864
    • (2007) Curr Med Chem , vol.14 , pp. 2848-2864
    • Bandyopadhyay, S.1    Goldstein, L.E.2    Lahiri, D.K.3    Rogers, J.T.4
  • 224
    • 33745793612 scopus 로고    scopus 로고
    • Interleukin-1alpha stimulates non-amyloidogenic pathway by alpha-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase
    • Bandyopadhyay S, Hartley DM, Cahill CM, et al. Interleukin-1alpha stimulates non-amyloidogenic pathway by alpha-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase. J Neurosci Res 2006;84:106-118
    • (2006) J Neurosci Res , vol.84 , pp. 106-118
    • Bandyopadhyay, S.1    Hartley, D.M.2    Cahill, C.M.3
  • 225
    • 58449133739 scopus 로고    scopus 로고
    • S100A7, a novel Alzheimer's disease biomarker with non-amyloidogenic alpha-secretase activity acts via selective promotion of ADAM-10
    • Qin W, Ho L, Wang J, et al. S100A7, a novel Alzheimer's disease biomarker with non-amyloidogenic alpha-secretase activity acts via selective promotion of ADAM-10. PLoS One 2009;4(1):e4183
    • (2009) PLoS One , vol.4 , Issue.1
    • Qin, W.1    Ho, L.2    Wang, J.3
  • 226
    • 77957771842 scopus 로고    scopus 로고
    • Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1
    • published online 29 Jun 2010, doi:10.1074/jbc. M110.149161
    • Cho HH, Cahill CM, Vanderburg CR, et al. Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1. J Biol Chem 2010: published online 29 Jun 2010, doi:10.1074/jbc. M110.149161
    • (2010) J Biol Chem
    • Cho, H.H.1    Cahill, C.M.2    Vanderburg, C.R.3
  • 227
    • 57149089667 scopus 로고    scopus 로고
    • Regulating amyloid precursor protein synthesis through an internal ribosomal entry site
    • Beaudoin ME, Poirel VJ, Krushel LA. Regulating amyloid precursor protein synthesis through an internal ribosomal entry site. Nucleic Acids Res 2008;36:6835-6847
    • (2008) Nucleic Acids Res , vol.36 , pp. 6835-6847
    • Beaudoin, M.E.1    Poirel, V.J.2    Krushel, L.A.3
  • 228
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of tau by GSK-3beta influences tau binding to microtubules and microtubule organisation
    • Wagner U, Utton M, Gallo JM, Miller CC. Cellular phosphorylation of tau by GSK-3beta influences tau binding to microtubules and microtubule organisation. J Cell Sci 1996;109:1537-1543
    • (1996) J Cell Sci , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3    Miller, C.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.