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Volumn 7, Issue 4, 2012, Pages

Amyloid-beta (Aβ) D7H mutation increases oligomeric Aβ42 and alters properties of Aβ-zinc/copper assemblies

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; ASPARTIC ACID; COPPER; HISTIDINE; OLIGOMER; ZINC; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); AMYLOID PRECURSOR PROTEIN; PEPTIDE FRAGMENT;

EID: 84860434786     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035807     Document Type: Article
Times cited : (104)

References (55)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics
    • Hardy J, Selkoe DJ, (2002) The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics. Science 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L, Kayed R, Glabe CG, et al. (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440: 352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5
  • 3
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH, Garcia-Munoz A, Shepardson NE, et al. (2008) Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14: 837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3    Garcia-Munoz, A.4    Shepardson, N.E.5
  • 4
    • 57649148788 scopus 로고    scopus 로고
    • Structural Classification of Toxic Amyloid Oligomers
    • Glabe CG, (2008) Structural Classification of Toxic Amyloid Oligomers. J Biol Chem 283: 29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 5
    • 0028292111 scopus 로고
    • Altered cleavage and secretion of a recombinant beta - APP bearing the Swedish familial Alzheimer's disease mutation
    • Felsenstein KM, Hunihan LW, Roberts SB, (1994) Altered cleavage and secretion of a recombinant beta - APP bearing the Swedish familial Alzheimer's disease mutation. Nature Genet 6: 251-256.
    • (1994) Nature Genet , vol.6 , pp. 251-256
    • Felsenstein, K.M.1    Hunihan, L.W.2    Roberts, S.B.3
  • 6
    • 0030599284 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43)
    • Maruyama K, Tomita T, Shinozaki K, Kume H, Asada H, et al. (1996) Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43). Biochem Biophys Res Commun 227: 730-735.
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 730-735
    • Maruyama, K.1    Tomita, T.2    Shinozaki, K.3    Kume, H.4    Asada, H.5
  • 7
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • Suzuki N, Cheung T, Cai X, Odaka A, Otvos L, et al. (1994) An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 264: 1336-1340.
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.2    Cai, X.3    Odaka, A.4    Otvos, L.5
  • 8
    • 79955602314 scopus 로고    scopus 로고
    • Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β′-site increases Aβ generation
    • Zhou L, Brouwers N, Benilova I, Vandersteen A, Mercken M, et al. (2011) Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β′-site increases Aβ generation. EMBO Molecular Medicine 3: 291-302.
    • (2011) EMBO Molecular Medicine , vol.3 , pp. 291-302
    • Zhou, L.1    Brouwers, N.2    Benilova, I.3    Vandersteen, A.4    Mercken, M.5
  • 9
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • Grabowski TJ, Cho HS, Vonsattel JP, Rebeck GW, Greenberg SM, (2001) Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann Neurol 49: 697-705.
    • (2001) Ann Neurol , vol.49 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.3    Rebeck, G.W.4    Greenberg, S.M.5
  • 11
    • 0026879650 scopus 로고
    • Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the [beta]-amyloid precursor protein gene
    • Hendriks L, van Duijn CM, Cras P, Cruts M, Van Hul W, et al. (1992) Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the [beta]-amyloid precursor protein gene. Nat Genet 1: 218-221.
    • (1992) Nat Genet , vol.1 , pp. 218-221
    • Hendriks, L.1    van Duijn, C.M.2    Cras, P.3    Cruts, M.4    van Hul, W.5
  • 12
    • 17944368176 scopus 로고    scopus 로고
    • The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation
    • Nilsberth C, Westlind-Danielsson A, Eckman CB, Condron MM, Axelman K, et al. (2001) The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation. Nat Neurosci 4: 887-893.
    • (2001) Nat Neurosci , vol.4 , pp. 887-893
    • Nilsberth, C.1    Westlind-Danielsson, A.2    Eckman, C.B.3    Condron, M.M.4    Axelman, K.5
  • 13
    • 9144272296 scopus 로고    scopus 로고
    • Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation
    • Cheng IH, Palop JJ, Esposito LA, Bien-Ly N, Yan F, et al. (2004) Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation. Nat Med 10: 1190-1192.
    • (2004) Nat Med , vol.10 , pp. 1190-1192
    • Cheng, I.H.1    Palop, J.J.2    Esposito, L.A.3    Bien-Ly, N.4    Yan, F.5
  • 14
    • 33947505097 scopus 로고    scopus 로고
    • The Tottori (D7N) and English (H6R) familial Alzheimer disease mutations accelerate Abeta fibril formation without increasing protofibril formation
    • Hori Y, Hashimoto T, Wakutani Y, Urakami K, Nakashima K, et al. (2007) The Tottori (D7N) and English (H6R) familial Alzheimer disease mutations accelerate Abeta fibril formation without increasing protofibril formation. J Biol Chem 282: 4916-4923.
    • (2007) J Biol Chem , vol.282 , pp. 4916-4923
    • Hori, Y.1    Hashimoto, T.2    Wakutani, Y.3    Urakami, K.4    Nakashima, K.5
  • 15
    • 78751692575 scopus 로고    scopus 로고
    • Anti-Amyloid beta Therapeutics in Alzheimer's Disease: The Need for a Paradigm Shift
    • Golde TE, Schneider LS, Koo EH, (2011) Anti-Amyloid beta Therapeutics in Alzheimer's Disease: The Need for a Paradigm Shift. Neuron 69: 203-213.
    • (2011) Neuron , vol.69 , pp. 203-213
    • Golde, T.E.1    Schneider, L.S.2    Koo, E.H.3
  • 17
    • 79952513228 scopus 로고    scopus 로고
    • Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity
    • Tõugu V, Tiiman A, Palumaa P, (2011) Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity. Metallomics 3: 250-261.
    • (2011) Metallomics , vol.3 , pp. 250-261
    • Tõugu, V.1    Tiiman, A.2    Palumaa, P.3
  • 18
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid [beta] peptide
    • Smith DG, Cappai R, Barnham KJ, (2007) The redox chemistry of the Alzheimer's disease amyloid [beta] peptide. Biochim Biophys Acta 1768: 1976-1990.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 19
    • 44849096899 scopus 로고    scopus 로고
    • Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides
    • Minicozzi V, Stellato F, Comai M, Serra MD, Potrich C, et al. (2008) Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides. J Biol Chem 283: 10784-10792.
    • (2008) J Biol Chem , vol.283 , pp. 10784-10792
    • Minicozzi, V.1    Stellato, F.2    Comai, M.3    Serra, M.D.4    Potrich, C.5
  • 20
    • 77954482455 scopus 로고    scopus 로고
    • NMR studies of zinc, copper, and iron binding to histidine, the principal metal ion complexing site of amyloid-beta peptide
    • Nair N, Perry G, Smith M, Reddy V, (2010) NMR studies of zinc, copper, and iron binding to histidine, the principal metal ion complexing site of amyloid-beta peptide. J Alzheimers Dis 20: 57-66.
    • (2010) J Alzheimers Dis , vol.20 , pp. 57-66
    • Nair, N.1    Perry, G.2    Smith, M.3    Reddy, V.4
  • 21
    • 77953940704 scopus 로고    scopus 로고
    • Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics
    • Duce JA, Bush AI, (2010) Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics. Prog Neurobiol 92: 1-18.
    • (2010) Prog Neurobiol , vol.92 , pp. 1-18
    • Duce, J.A.1    Bush, A.I.2
  • 22
    • 77954344206 scopus 로고    scopus 로고
    • PBT2 Rapidly Improves Cognition in Alzheimer's Disease: Additional Phase II Analyses J Alzheimers Dis
    • Faux N, Ritchie C, Gunn A, Rembach A, Tsatsanis A, et al. (2010) PBT2 Rapidly Improves Cognition in Alzheimer's Disease: Additional Phase II Analyses J Alzheimers Dis 20: 509-516.
    • (2010) , vol.20 , pp. 509-516
    • Faux, N.1    Ritchie, C.2    Gunn, A.3    Rembach, A.4    Tsatsanis, A.5
  • 23
    • 67849090892 scopus 로고    scopus 로고
    • Challenges associated with metal chelation therapy in Alzheimer's disease
    • Hegde M, Bharathi P, Suram A, Venugopal C, Jagannathan R, et al. (2009) Challenges associated with metal chelation therapy in Alzheimer's disease. J Alzheimers Dis 17: 457-468.
    • (2009) J Alzheimers Dis , vol.17 , pp. 457-468
    • Hegde, M.1    Bharathi, P.2    Suram, A.3    Venugopal, C.4    Jagannathan, R.5
  • 24
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid Precursor Protein Processing and Alzheimer's Disease
    • O'Brien RJ, Wong PC, (2011) Amyloid Precursor Protein Processing and Alzheimer's Disease. Annu Rev Neurosci 34: 185-204.
    • (2011) Annu Rev Neurosci , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 25
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-Protein Oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan G, Lomakin A, Teplow DB, (2001) Amyloid beta-Protein Oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276: 35176-35184.
    • (2001) J Biol Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 26
    • 77950529014 scopus 로고    scopus 로고
    • Genetic screening of Alzheimer's disease genes in Iberian and African samples yields novel mutations in presenilins and APP
    • Guerreiro RJ, Baquero M, Blesa R, Boada M, Bras JM, et al. (2010) Genetic screening of Alzheimer's disease genes in Iberian and African samples yields novel mutations in presenilins and APP. Neurobiol of aging 31: 725-731.
    • (2010) Neurobiol of Aging , vol.31 , pp. 725-731
    • Guerreiro, R.J.1    Baquero, M.2    Blesa, R.3    Boada, M.4    Bras, J.M.5
  • 27
    • 79953225854 scopus 로고    scopus 로고
    • Distinct Effects of Zn2+, Cu2+, Fe3+, and Al3+ on Amyloid-beta Stability, Oligomerization, and Aggregation
    • Chen WT, Liao YH, Yu HM, Cheng IH, Chen YR, (2011) Distinct Effects of Zn2+, Cu2+, Fe3+, and Al3+ on Amyloid-beta Stability, Oligomerization, and Aggregation. J Biol Chem 286: 9646-9656.
    • (2011) J Biol Chem , vol.286 , pp. 9646-9656
    • Chen, W.T.1    Liao, Y.H.2    Yu, H.M.3    Cheng, I.H.4    Chen, Y.R.5
  • 28
    • 0036667331 scopus 로고    scopus 로고
    • 4,4(′)-Dianilino-1,1(′)-binaphthyl-5,5(′)-disulfonate: report on non-beta-sheet conformers of Alzheimer's peptide beta(1-40)
    • LeVine H, 3rd, (2002) 4,4(′)-Dianilino-1,1(′)-binaphthyl-5,5(′)-disulfonate: report on non-beta-sheet conformers of Alzheimer's peptide beta(1-40). Arch Biochem Biophys 404: 106-115.
    • (2002) Arch Biochem Biophys , vol.404 , pp. 106-115
    • LeVine 3rd, H.1
  • 29
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang X, Cuajungco MP, Atwood CS, Hartshorn MA, Tyndall JD, et al. (1999) Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J Bio Chem 274: 37111-37116.
    • (1999) J Bio Chem , vol.274 , pp. 37111-37116
    • Huang, X.1    Cuajungco, M.P.2    Atwood, C.S.3    Hartshorn, M.A.4    Tyndall, J.D.5
  • 30
    • 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, (2008) Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide. J Neurochem 104: 1249-1259.
    • (2008) J Neurochem , vol.104 , pp. 1249-1259
    • Tougu, V.1    Karafin, A.2    Palumaa, P.3
  • 31
    • 69949167074 scopus 로고    scopus 로고
    • Zn(II)- and Cu(II)-induced non-fibrillar 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, Chung RS, Howells C, et al. (2009) Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta(1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators. J Neurochem 110: 1784-1795.
    • (2009) J Neurochem , vol.110 , pp. 1784-1795
    • Tougu, V.1    Karafin, A.2    Zovo, K.3    Chung, R.S.4    Howells, C.5
  • 32
    • 79960694577 scopus 로고    scopus 로고
    • Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides
    • Pedersen J, Østergaard J, Rozlosnik N, Gammelgaard B, Heegaard N, (2011) Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides. J Biol Chem 286: 26952-26963.
    • (2011) J Biol Chem , vol.286 , pp. 26952-26963
    • Pedersen, J.1    Østergaard, J.2    Rozlosnik, N.3    Gammelgaard, B.4    Heegaard, N.5
  • 33
    • 62449330486 scopus 로고    scopus 로고
    • A Recessive Mutation in the APP Gene with Dominant-Negative Effect on Amyloidogenesis
    • Di Fede G, Catania M, Morbin M, Rossi G, Suardi S, et al. (2009) A Recessive Mutation in the APP Gene with Dominant-Negative Effect on Amyloidogenesis. Science 323: 1473-1477.
    • (2009) Science , vol.323 , pp. 1473-1477
    • Di Fede, G.1    Catania, M.2    Morbin, M.3    Rossi, G.4    Suardi, S.5
  • 34
    • 0031742418 scopus 로고    scopus 로고
    • Flemish and Dutch Mutations in Amyloid [beta] Precursor Protein Have Different Effects on Amyloid [beta] Secretion
    • De Jonghe C, Zehr C, Yager D, Prada C-M, Younkin S, et al. (1998) Flemish and Dutch Mutations in Amyloid [beta] Precursor Protein Have Different Effects on Amyloid [beta] Secretion. Neurobiology of Disease 5: 281-286.
    • (1998) Neurobiology of Disease , vol.5 , pp. 281-286
    • de Jonghe, C.1    Zehr, C.2    Yager, D.3    Prada, C.-M.4    Younkin, S.5
  • 36
    • 79953137657 scopus 로고    scopus 로고
    • Copper promotes the trafficking of the amyloid precursor protein
    • Acevedo KM, Hung YH, Dalziel AH, Li QX, Laughton K, et al. (2011) Copper promotes the trafficking of the amyloid precursor protein. J Biol Chem 286: 8252-8262.
    • (2011) J Biol Chem , vol.286 , pp. 8252-8262
    • Acevedo, K.M.1    Hung, Y.H.2    Dalziel, A.H.3    Li, Q.X.4    Laughton, K.5
  • 37
    • 72749101173 scopus 로고    scopus 로고
    • Divalent metal transporter 1 is involved in amyloid precursor protein processing and Abeta generation
    • Zheng W, Xin N, Chi ZH, Zhao BL, Zhang J, et al. (2009) Divalent metal transporter 1 is involved in amyloid precursor protein processing and Abeta generation. FASEB 23: 4207-4217.
    • (2009) FASEB , vol.23 , pp. 4207-4217
    • Zheng, W.1    Xin, N.2    Chi, Z.H.3    Zhao, B.L.4    Zhang, J.5
  • 38
    • 78650719200 scopus 로고    scopus 로고
    • Zinc overload enhances APP cleavage and Abeta deposition in the Alzheimer mouse brain
    • Wang CY, Wang T, Zheng W, Zhao BL, Danscher G, et al. (2010) Zinc overload enhances APP cleavage and Abeta deposition in the Alzheimer mouse brain. PloS one 5: e15349.
    • (2010) PloS One , vol.5
    • Wang, C.Y.1    Wang, T.2    Zheng, W.3    Zhao, B.L.4    Danscher, G.5
  • 39
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease
    • Duce JA, Tsatsanis A, Cater MA, James SA, Robb E, et al. (2010) Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell 142: 857-867.
    • (2010) Cell , vol.142 , pp. 857-867
    • Duce, J.A.1    Tsatsanis, A.2    Cater, M.A.3    James, S.A.4    Robb, E.5
  • 40
    • 84856713089 scopus 로고    scopus 로고
    • Metal Binding Dictates Conformation and Function of the Amyloid Precursor Protein (APP) E2 Domain
    • Dahms SO, Konnig I, Roeser D, Guhrs KH, Mayer MC, et al. (2012) Metal Binding Dictates Conformation and Function of the Amyloid Precursor Protein (APP) E2 Domain. J Mol Biol 416: 438-452.
    • (2012) J Mol Biol , vol.416 , pp. 438-452
    • Dahms, S.O.1    Konnig, I.2    Roeser, D.3    Guhrs, K.H.4    Mayer, M.C.5
  • 41
    • 73949117777 scopus 로고    scopus 로고
    • Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures
    • Schmidt M, Sachse C, Richter W, Xu C, Fandrich M, et al. (2009) Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci USA 106: 19813-19818.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 19813-19818
    • Schmidt, M.1    Sachse, C.2    Richter, W.3    Xu, C.4    Fandrich, M.5
  • 42
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions
    • Olofsson A, Lindhagen-Persson M, Sauer-Eriksson AE, Ohman A, (2007) Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions. Biochem J 404: 63-70.
    • (2007) Biochem J , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Ohman, A.4
  • 43
    • 77950189704 scopus 로고    scopus 로고
    • Copper Enhances Amyloid-β Peptide Neurotoxicity and non β-Aggregation: A Series of Experiments Conducted upon Copper-Bound and Copper-Free Amyloid-β Peptide
    • Dai X, Sun Y, Gao Z, Jiang Z, (2010) Copper Enhances Amyloid-β Peptide Neurotoxicity and non β-Aggregation: A Series of Experiments Conducted upon Copper-Bound and Copper-Free Amyloid-β Peptide. J Mol Neurosci 41: 66-73.
    • (2010) J Mol Neurosci , vol.41 , pp. 66-73
    • Dai, X.1    Sun, Y.2    Gao, Z.3    Jiang, Z.4
  • 44
    • 80052210889 scopus 로고    scopus 로고
    • Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-beta(1-16) at physiological pH and its significance
    • Shin BK, Saxena S, (2011) Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-beta(1-16) at physiological pH and its significance. J Physi Chemi A 115: 9590-9602.
    • (2011) J Physi Chemi A , vol.115 , pp. 9590-9602
    • Shin, B.K.1    Saxena, S.2
  • 45
    • 16844373633 scopus 로고    scopus 로고
    • N-Terminal deletions modify the Cu2+ binding site in amyloid-beta
    • Karr JW, Akintoye H, Kaupp LJ, Szalai VA, (2005) N-Terminal deletions modify the Cu2+ binding site in amyloid-beta. Biochemistry 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
  • 47
    • 77953113490 scopus 로고    scopus 로고
    • Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states
    • Miller Y, Ma B, Nussinov R, (2010) Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states. Proc Natl Acad Sci U S A 107: 9490-9495.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9490-9495
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 48
    • 0030024168 scopus 로고    scopus 로고
    • Aggregation and Metal-Binding Properties of Mutant Forms of the Amyloid Beta Peptide of Alzheimer's Disease
    • Clements A, Allsop D, Walsh DM, (1996) Aggregation and Metal-Binding Properties of Mutant Forms of the Amyloid Beta Peptide of Alzheimer's Disease. J Neurochem 66: 740-747.
    • (1996) J Neurochem , vol.66 , pp. 740-747
    • Clements, A.1    Allsop, D.2    Walsh, D.M.3
  • 49
    • 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, Smith MA, Perry G, et al. (2007) Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron. Biochemistry 46: 12737-12743.
    • (2007) Biochemistry , vol.46 , pp. 12737-12743
    • Nakamura, M.1    Shishido, N.2    Nunomura, A.3    Smith, M.A.4    Perry, G.5
  • 50
    • 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, Curtain CC, Tew D, et al. (2004) Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid. FASEB J 18: 1427-1429.
    • (2004) FASEB J , vol.18 , pp. 1427-1429
    • Barnham, K.J.1    Haeffner, F.2    Ciccotosto, G.D.3    Curtain, C.C.4    Tew, D.5
  • 51
    • 33947265861 scopus 로고    scopus 로고
    • Concentration Dependent Cu2+ Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-beta Peptide
    • Smith DP, Ciccotosto GD, Tew DJ, Fodero-Tavoletti MT, Johanssen T, et al. (2007) Concentration Dependent Cu2+ Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-beta Peptide. Biochemistry 46: 2881-2891.
    • (2007) Biochemistry , vol.46 , pp. 2881-2891
    • Smith, D.P.1    Ciccotosto, G.D.2    Tew, D.J.3    Fodero-Tavoletti, M.T.4    Johanssen, T.5
  • 52
    • 9144235443 scopus 로고    scopus 로고
    • Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta
    • Atwood CS, Perry G, Zeng H, Kato Y, Jones WD, et al. (2004) Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta. Biochemistry 43: 560-568.
    • (2004) Biochemistry , vol.43 , pp. 560-568
    • Atwood, C.S.1    Perry, G.2    Zeng, H.3    Kato, Y.4    Jones, W.D.5
  • 53
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs
    • Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, et al. (1992) Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs. J Biol Chem 267: 546-554.
    • (1992) J Biol Chem , vol.267 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3    Kosmoski, J.4    Knauer, M.5
  • 54
    • 77956698237 scopus 로고
    • Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research
    • Jan A, Hartley D, Lashuel H, (1992) Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research. Nat Protoc 5: 1186-1209.
    • (1992) Nat Protoc , vol.5 , pp. 1186-1209
    • Jan, A.1    Hartley, D.2    Lashuel, H.3
  • 55
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H, (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6: 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1


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