메뉴 건너뛰기




Volumn 5, Issue 2, 1998, Pages 121-142

Structural and kinetic features of amyloid β-protein fibrillogenesis

Author keywords

Alzheimer's disease; Amyloid protein; Amyloidogenesis; Fibrillogenesis; Kinetics; Transthyretin

Indexed keywords

AMYLOID BETA PROTEIN; BIOPOLYMER;

EID: 0032084472     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506129808995290     Document Type: Article
Times cited : (296)

References (223)
  • 1
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis. The β-fibrilloses (First of two parts)
    • Glenner GG (1980). Amyloid deposits and amyloidosis. The β-fibrilloses (First of two parts). New Eng J Med 302, 1283-1292
    • (1980) New Eng J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 2
    • 0025991945 scopus 로고
    • Amyloid protein and Alzheimer's disease
    • Selkoe DJ (1991). Amyloid protein and Alzheimer's disease. Sci Am 265, 68-71, 74-6, 78
    • (1991) Sci Am , vol.265 , pp. 68-71
    • Selkoe, D.J.1
  • 3
    • 0029887389 scopus 로고    scopus 로고
    • The spectrum of behavioral changes in Alzheimer's disease
    • Mega MS, Cummings JL, Fiorello T and Gornbein J (1996). The spectrum of behavioral changes in Alzheimer's disease. Neurology 46, 130-135
    • (1996) Neurology , vol.46 , pp. 130-135
    • Mega, M.S.1    Cummings, J.L.2    Fiorello, T.3    Gornbein, J.4
  • 4
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe DJ (1991). The molecular pathology of Alzheimer's disease. Neuron 6, 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 5
    • 0002205462 scopus 로고
    • Prevalence and neurobiology of Alzheimer's disease
    • (K. Iqbal, D.R.C. McLachlan, B. Winblad and H.M. Winsniewski, eds.) John Wiley and Sons: New York
    • Iqbal K (1991). Prevalence and neurobiology of Alzheimer's disease. In: Alzheimer's Disease: Basic Mechanisms, Diagnosis and Therapeutic Strategies. (K. Iqbal, D.R.C. McLachlan, B. Winblad and H.M. Winsniewski, eds.) John Wiley and Sons: New York. 1-5
    • (1991) Alzheimer's Disease: Basic Mechanisms, Diagnosis and Therapeutic Strategies , pp. 1-5
    • Iqbal, K.1
  • 6
    • 0030944675 scopus 로고    scopus 로고
    • Differential diagnosis of Alzheimer's disease
    • Geldmacher DS and Whitehouse PJ (1997). Differential diagnosis of Alzheimer's disease. Neurology 48, S2-S9
    • (1997) Neurology , vol.48
    • Geldmacher, D.S.1    Whitehouse, P.J.2
  • 8
    • 0030983544 scopus 로고    scopus 로고
    • The family caregivers role in Alzheimer's disease
    • Haley WE (1997). The family caregivers role in Alzheimer's disease. Neurology 48, S25-S29
    • (1997) Neurology , vol.48
    • Haley, W.E.1
  • 9
    • 10244259208 scopus 로고    scopus 로고
    • The efficacy and safety of donepezil in patients with Alzheimer's disease: Results of a US multicentre, randomized, double-blind, placebo-controlled trial. The Donepezil Study Group
    • Rogers SL and Friedhoff LT (1996). The efficacy and safety of donepezil in patients with Alzheimer's disease: Results of a US multicentre, randomized, double-blind, placebo-controlled trial. The Donepezil Study Group. Dementia 7, 293-303
    • (1996) Dementia , vol.7 , pp. 293-303
    • Rogers, S.L.1    Friedhoff, L.T.2
  • 12
    • 0028109336 scopus 로고
    • The US economic and social costs of Alzheimer's disease revisited
    • Ernst RL and Hay JW (1994). The US economic and social costs of Alzheimer's disease revisited. Am J Publ Health 84, 1261-1264
    • (1994) Am J Publ Health , vol.84 , pp. 1261-1264
    • Ernst, R.L.1    Hay, J.W.2
  • 14
    • 0000858425 scopus 로고
    • Über einen eigenartigen schweren Erkrankungsprozeß der Hirnrinde
    • Alzheimer A (1906). Über einen eigenartigen schweren Erkrankungsprozeß der Hirnrinde. Neurol Centr 23, 1129-1136
    • (1906) Neurol Centr , vol.23 , pp. 1129-1136
    • Alzheimer, A.1
  • 16
  • 17
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M, Wischik CM, Crowther RA, Walker JE and Klug A (1988). Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc Natl Acad Sci USA 85, 4051-4055
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 20
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG and Wong CW (1984). Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120, 885-890
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 21
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • Selkoe DJ (1997). Alzheimer's disease: genotypes, phenotypes, and treatments. Science 275, 630-631
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 22
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J (1997). Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci 20, 154-159
    • (1997) Trends Neurosci , vol.20 , pp. 154-159
    • Hardy, J.1
  • 23
    • 0028123071 scopus 로고
    • Alzheimer's disease: A central role for amyloid
    • Selkoe DJ (1994). Alzheimer's disease: A central role for amyloid. J Neuropath Exp Neurol 53, 438-447
    • (1994) J Neuropath Exp Neurol , vol.53 , pp. 438-447
    • Selkoe, D.J.1
  • 24
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe DJ (1996). Amyloid β-protein and the genetics of Alzheimer's disease. J Biol Chem 271, 18295-18298
    • (1996) J Biol Chem , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 25
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson MP (1997). Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol Rev 77, 1081-1132
    • (1997) Physiol Rev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 26
    • 0031003233 scopus 로고    scopus 로고
    • The Alzheimer family of diseases - Many etiologies, one pathogenesis
    • Hardy J (1997). The Alzheimer family of diseases - Many etiologies, one pathogenesis. Proc Natl Acad Sci USA 94, 2095-2097
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2095-2097
    • Hardy, J.1
  • 27
    • 0029792928 scopus 로고    scopus 로고
    • New clues to Alzheimer's disease - Unraveling the roles of amyloid and tau
    • Yankner BA (1996). New clues to Alzheimer's disease - Unraveling the roles of amyloid and tau. Nature Med 2, 850-852
    • (1996) Nature Med , vol.2 , pp. 850-852
    • Yankner, B.A.1
  • 28
    • 0030046401 scopus 로고    scopus 로고
    • Anti-amyloid drugs: Potential in the treatment of diseases associated with aging
    • Kisilevsky R (1996). Anti-amyloid drugs: Potential in the treatment of diseases associated with aging. Drugs Aging 8, 75-83
    • (1996) Drugs Aging , vol.8 , pp. 75-83
    • Kisilevsky, R.1
  • 29
    • 0030930122 scopus 로고    scopus 로고
    • Alzheimer's disease: Towards therapeutic manipulation of the amyloid precursor protein and amyloid β-peptides
    • Larner AJ and Rossor MN (1997). Alzheimer's disease: towards therapeutic manipulation of the amyloid precursor protein and amyloid β-peptides. Exp Opin Ther Patents 7, 1115-1127
    • (1997) Exp Opin Ther Patents , vol.7 , pp. 1115-1127
    • Larner, A.J.1    Rossor, M.N.2
  • 30
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly JW (1997). Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 5, 595-600
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 31
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell RW and Lomas DA (1997). Conformational disease. Lancet 350, 134-138
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 32
    • 0002898753 scopus 로고
    • Reexamination of the pathogenesis of the senile plaque
    • Wisniewski HM and Terry RD (1973). Reexamination of the pathogenesis of the senile plaque. Prog Neuropath 2, 1-26
    • (1973) Prog Neuropath , vol.2 , pp. 1-26
    • Wisniewski, H.M.1    Terry, R.D.2
  • 33
    • 78651158156 scopus 로고
    • Ultrastructural studies in Alzheimer's presenile dementia
    • Terry RD, Gonatas NK and Weiss M (1964). Ultrastructural studies in Alzheimer's presenile dementia. Am J Pathol 44, 269-297
    • (1964) Am J Pathol , vol.44 , pp. 269-297
    • Terry, R.D.1    Gonatas, N.K.2    Weiss, M.3
  • 34
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • Dickson DW (1997). The pathogenesis of senile plaques. J Neuropathol Exp Neurol 56, 321-339
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 321-339
    • Dickson, D.W.1
  • 35
    • 0001120692 scopus 로고
    • Alzheimer's disease- An electron microscopical study
    • Kidd M (1964). Alzheimer's disease- An electron microscopical study. Brain 87, 307-320
    • (1964) Brain , vol.87 , pp. 307-320
    • Kidd, M.1
  • 36
    • 0019136822 scopus 로고
    • High-resolution electron microscopic analysis of the amyloid fibril in Alzheimer's disease
    • Narang HK (1980). High-resolution electron microscopic analysis of the amyloid fibril in Alzheimer's disease. J Neuropath Exp Neurol 39, 621-631
    • (1980) J Neuropath Exp Neurol , vol.39 , pp. 621-631
    • Narang, H.K.1
  • 37
    • 0022912701 scopus 로고
    • Ultrastructure of amyloid fibrils in Alzheimer's disease and Down's syndrome
    • Miyakawa T, Watanabe K and Katsuragi S (1986). Ultrastructure of amyloid fibrils in Alzheimer's disease and Down's syndrome. Virchows Arch [Cell Pathol] 52, 99-106
    • (1986) Virchows Arch [Cell Pathol] , vol.52 , pp. 99-106
    • Miyakawa, T.1    Watanabe, K.2    Katsuragi, S.3
  • 39
    • 0026753096 scopus 로고
    • Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease
    • Yamaguchi H, Yamazaki T, Lemere CA, Frosch MP and Selkoe DJ (1992). Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. Am J Pathol 141, 249-259
    • (1992) Am J Pathol , vol.141 , pp. 249-259
    • Yamaguchi, H.1    Yamazaki, T.2    Lemere, C.A.3    Frosch, M.P.4    Selkoe, D.J.5
  • 40
    • 0024237246 scopus 로고
    • Diffuse type of senile plaques in the brains of Alzheimer-type dementia
    • Yamaguchi H, Hirai S, Morimatsu M, Shoji M and Harigaya Y (1988). Diffuse type of senile plaques in the brains of Alzheimer-type dementia. Acta Neuropath 77, 113-119
    • (1988) Acta Neuropath , vol.77 , pp. 113-119
    • Yamaguchi, H.1    Hirai, S.2    Morimatsu, M.3    Shoji, M.4    Harigaya, Y.5
  • 41
    • 0024420556 scopus 로고
    • Electron micrograph of diffuse plaques: Initial stage of senile plaque formation in the Alzheimer brain
    • Yamaguchi H, Nakazato Y, Hirai S, Shoji M and Harigaya Y (1989). Electron micrograph of diffuse plaques: Initial stage of senile plaque formation in the Alzheimer brain. Am J Pathol 135, 593-597
    • (1989) Am J Pathol , vol.135 , pp. 593-597
    • Yamaguchi, H.1    Nakazato, Y.2    Hirai, S.3    Shoji, M.4    Harigaya, Y.5
  • 43
    • 0027787636 scopus 로고
    • Is the "preamyloid" of diffuse plaques in Alzheimer's disease really nonfibrillar?
    • Davies CA and Mann DMA (1993). Is the "preamyloid" of diffuse plaques in Alzheimer's disease really nonfibrillar? Am J Pathol 143, 1594-1605
    • (1993) Am J Pathol , vol.143 , pp. 1594-1605
    • Davies, C.A.1    Mann, D.M.A.2
  • 44
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED and Glenner GG (1968). X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 16, 673-677
    • (1968) J Histochem Cytochem , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 45
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG and Wong CW (1984). Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 122, 1131-1135
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 46
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D, Lerman MI, McBridge OW, V S and Gajdusek DC (1987). Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235, 877-880
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBridge, O.W.3    S, V.4    Gajdusek, D.C.5
  • 47
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides
    • Robakis NK, Ramakrishna N, Wolfe G and Wisniewski HM (1987). Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides. Proc Natl Acad Sci USA 84, 4190-4194
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 49
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli F, Castaño E, Glenner GG and Frangione B (1988). Differences between vascular and plaque core amyloid in Alzheimer's disease. J Neurochem 51, 648-651
    • (1988) J Neurochem , vol.51 , pp. 648-651
    • Prelli, F.1    Castaño, E.2    Glenner, G.G.3    Frangione, B.4
  • 50
    • 0024232950 scopus 로고
    • Protein chemical and immunocytochemical studies of meningovascular β-amyloid protein in Alzheimer's disease and normal aging
    • Joachim CL, Duffy LK, Morris JH and Selkoe DJ (1988). Protein chemical and immunocytochemical studies of meningovascular β-amyloid protein in Alzheimer's disease and normal aging. Brain Res 474, 100-111
    • (1988) Brain Res , vol.474 , pp. 100-111
    • Joachim, C.L.1    Duffy, L.K.2    Morris, J.H.3    Selkoe, D.J.4
  • 51
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid β protein in Alzheimer's disease
    • Mori H, Takio K, Ogawara M and Selkoe DJ (1992). Mass spectrometry of purified amyloid β protein in Alzheimer's disease. J Biol Chem 267, 17082-17086
    • (1992) J Biol Chem , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3    Selkoe, D.J.4
  • 52
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • Miller DL, Papayannopoulos IA, Styles J and Bobin SA (1993). Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch Biochem Biophys 301, 41-52
    • (1993) Arch Biochem Biophys , vol.301 , pp. 41-52
    • Miller, D.L.1    Papayannopoulos, I.A.2    Styles, J.3    Bobin, S.A.4
  • 53
    • 0027332081 scopus 로고
    • β-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher AE, Lowenson JD, Clarke S, Woods AS, Cotter RJ, Gowing E and Ball MJ (1993). β-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease. Proc Natl Acad Sci USA 90, 10836-10840
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 55
    • 0031559602 scopus 로고    scopus 로고
    • Isolation, chemical characterization, and quantitation of Aβ 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits
    • Kuo YM, Emmerling MR, Woods AS, Cotter RJ and Roher AE (1997). Isolation, chemical characterization, and quantitation of Aβ 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits. Biochem Biophys Res Commun 237, 188-191
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 188-191
    • Kuo, Y.M.1    Emmerling, M.R.2    Woods, A.S.3    Cotter, R.J.4    Roher, A.E.5
  • 56
    • 0028179341 scopus 로고
    • Chemical characterization of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
    • Gowing E, Roher AE, Woods AS, Cotter RJ, Chaney M, Little SP and Ball MJ (1994). Chemical characterization of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. J Biol Chem 269, 10987-10990
    • (1994) J Biol Chem , vol.269 , pp. 10987-10990
    • Gowing, E.1    Roher, A.E.2    Woods, A.S.3    Cotter, R.J.4    Chaney, M.5    Little, S.P.6    Ball, M.J.7
  • 58
    • 0030035922 scopus 로고    scopus 로고
    • p3 β-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain
    • Higgins LS, Murphy GM, Forno LS, Catalano R and Cordell B (1996). p3 β-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain. Am J Pathol 149, 585-596
    • (1996) Am J Pathol , vol.149 , pp. 585-596
    • Higgins, L.S.1    Murphy, G.M.2    Forno, L.S.3    Catalano, R.4    Cordell, B.5
  • 59
    • 0029849644 scopus 로고    scopus 로고
    • Full-length amyloid-β(1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques
    • Iwatsubo T, Saido TC, Mann DMA, Lee VMY and Trojanowski JQ (1996). Full-length amyloid-β(1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques. Am J Pathol 149, 1823-1830
    • (1996) Am J Pathol , vol.149 , pp. 1823-1830
    • Iwatsubo, T.1    Saido, T.C.2    Mann, D.M.A.3    Lee, V.M.Y.4    Trojanowski, J.Q.5
  • 60
    • 0023854844 scopus 로고
    • Neuritic plaque amyloid in Alzheimer's disease is highly racemized
    • Shapira R, Austin GE and Mirra SS (1988). Neuritic plaque amyloid in Alzheimer's disease is highly racemized. J Neurochem 50, 69-74
    • (1988) J Neurochem , vol.50 , pp. 69-74
    • Shapira, R.1    Austin, G.E.2    Mirra, S.S.3
  • 62
    • 0022654027 scopus 로고
    • Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease
    • Selkoe DJ, Abraham CR, Podlisny MB and Duffy LK (1986). Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease. J Neurochem 146, 1820-1834
    • (1986) J Neurochem , vol.146 , pp. 1820-1834
    • Selkoe, D.J.1    Abraham, C.R.2    Podlisny, M.B.3    Duffy, L.K.4
  • 63
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive western blot assay
    • Ida N, Hartmann T, Pantel J, Schroder J, Zerfass R, Forstl H, Sandbrink R, Masters CL and Beyreuther K (1996). Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive western blot assay. J Biol Chem 271, 22908-22914
    • (1996) J Biol Chem , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 65
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I and Schenk DB (1993). Characterization of β-amyloid peptide from human cerebrospinal fluid. J Neurochem 61, 1965-1968
    • (1993) J Neurochem , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 71
    • 0027956675 scopus 로고
    • High tissue content of soluble β1-40 is linked to cerebral amyloid angiopathy
    • Suzuki N, Iwatsubo T, Odaka A, Ishibashi Y, Kitada C and Ihara Y (1994). High tissue content of soluble β1-40 is linked to cerebral amyloid angiopathy. Am J Pathol 145, 452-460
    • (1994) Am J Pathol , vol.145 , pp. 452-460
    • Suzuki, N.1    Iwatsubo, T.2    Odaka, A.3    Ishibashi, Y.4    Kitada, C.5    Ihara, Y.6
  • 73
    • 0030742712 scopus 로고    scopus 로고
    • Heterogeneity of water-soluble amyloid β-peptide in Alzheimer's disease and Down's syndrome brains
    • Russo C, Saido TC, DeBusk LM, Tabaton M, Gambetti P and Teller JK (1997). Heterogeneity of water-soluble amyloid β-peptide in Alzheimer's disease and Down's syndrome brains. FEBS Lett 409, 411-6
    • (1997) FEBS Lett , vol.409 , pp. 411-416
    • Russo, C.1    Saido, T.C.2    DeBusk, L.M.3    Tabaton, M.4    Gambetti, P.5    Teller, J.K.6
  • 75
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain
    • Saido TC, Yamao-Harigaya W, Iwatsubo T and Kawashima S (1996). Amino- and carboxyl-terminal heterogeneity of β-amyloid peptides deposited in human brain. Neurosci Lett 215, 173-176
    • (1996) Neurosci Lett , vol.215 , pp. 173-176
    • Saido, T.C.1    Yamao-Harigaya, W.2    Iwatsubo, T.3    Kawashima, S.4
  • 76
    • 0030464914 scopus 로고    scopus 로고
    • β-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • Cummings BJ, Pike CJ, Shankle R and Cotman CW (1996). β-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol Aging 17, 921-933
    • (1996) Neurobiol Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 77
    • 0014313861 scopus 로고
    • The association between quantitative measures of dementia and senile change in the cerebral grey matter of elderly subjects
    • Blessed G, Tomlinson BE and Roth M (1968). The association between quantitative measures of dementia and senile change in the cerebral grey matter of elderly subjects. Br J Psych 114, 797-811
    • (1968) Br J Psych , vol.114 , pp. 797-811
    • Blessed, G.1    Tomlinson, B.E.2    Roth, M.3
  • 78
    • 0025773225 scopus 로고
    • Neuritic pathology and dementia in Alzheimer's disease
    • McKee AC, Kosik KS and Kowall NW (1991). Neuritic pathology and dementia in Alzheimer's disease. Ann Neurol 30, 156-165
    • (1991) Ann Neurol , vol.30 , pp. 156-165
    • McKee, A.C.1    Kosik, K.S.2    Kowall, N.W.3
  • 80
    • 0027249001 scopus 로고
    • Two distinct ubiquitin immunoreactive senile plaques in Alzheimer's disease: Relationship with the intellectual status in 29 cases
    • He Y, Delaere P, Duyckaerts C, Wasowicz M, Piette F and Hauw JJ (1993). Two distinct ubiquitin immunoreactive senile plaques in Alzheimer's disease: relationship with the intellectual status in 29 cases. Acta Neuropath 86, 109-116
    • (1993) Acta Neuropath , vol.86 , pp. 109-116
    • He, Y.1    Delaere, P.2    Duyckaerts, C.3    Wasowicz, M.4    Piette, F.5    Hauw, J.J.6
  • 81
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP, Butters N, DeTeresa R, Hill R, Hansen LA and Katzman R (1991). Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann Neurol 30, 572-580
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 82
    • 0001611370 scopus 로고
    • Electron microscopic observation on a fibrous component in amyloid of diverse origins
    • Cohen AS and Calkins E (1959). Electron microscopic observation on a fibrous component in amyloid of diverse origins. Nature 183, 1202-1203
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 83
    • 0014098295 scopus 로고
    • High-resolution electron microscopic analysis of the amyloid fibril
    • Shirahama T and Cohen AS (1967). High-resolution electron microscopic analysis of the amyloid fibril. J Cell Biol 33, 679-708
    • (1967) J Cell Biol , vol.33 , pp. 679-708
    • Shirahama, T.1    Cohen, A.S.2
  • 85
  • 86
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik SB, Inouye H, Szumowski KE and Kirschner DA (1998). Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils. Biophysical J 74, 537-545
    • (1998) Biophysical J , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 88
    • 0015408029 scopus 로고
    • The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation
    • Glenner GG, Eanes ED and Page DL (1972). The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation. J Histochem Cytochem 20, 821-826
    • (1972) J Histochem Cytochem , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.D.2    Page, D.L.3
  • 89
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer's disease indicates cross-β conformation
    • Kirschner DA, Abraham C and Selkoe DJ (1986). X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer's disease indicates cross-β conformation. Proc Natl Acad Sci USA 83, 503-507
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 90
    • 0027411230 scopus 로고
    • Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by X-ray diffraction
    • Inouye H, Fraser PE and Kirschner DA (1993). Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: analysis by X-ray diffraction. Biophysical J 64, 502-519
    • (1993) Biophysical J , vol.64 , pp. 502-519
    • Inouye, H.1    Fraser, P.E.2    Kirschner, D.A.3
  • 91
    • 0014578835 scopus 로고
    • Characterization of the amyloid fibril as a cross-β protein
    • Bonar L, Cohen AS and Skinner MM (1969). Characterization of the amyloid fibril as a cross-β protein. Proc Soc Exp Biol Med 131, 1373-1375
    • (1969) Proc Soc Exp Biol Med , vol.131 , pp. 1373-1375
    • Bonar, L.1    Cohen, A.S.2    Skinner, M.M.3
  • 92
    • 0000573263 scopus 로고
    • Configuration of polypeptide chains with favoured orientation around single bonds: Two new pleated sheets
    • Pauling L and Corey R (1951). Configuration of polypeptide chains with favoured orientation around single bonds: two new pleated sheets. Proc Natl Acad Sci USA 37, 729-739
    • (1951) Proc Natl Acad Sci USA , vol.37 , pp. 729-739
    • Pauling, L.1    Corey, R.2
  • 95
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake C and Serpell L (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4, 989-998
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 97
    • 0015914783 scopus 로고
    • Conformation of twisted β-pleated sheets in proteins
    • Chothia C (1973). Conformation of twisted β-pleated sheets in proteins. J Mol Biol 75, 295-302
    • (1973) J Mol Biol , vol.75 , pp. 295-302
    • Chothia, C.1
  • 98
    • 0001419932 scopus 로고
    • CCLXXIX. The X-ray interpretation of denaturation and the structure of the seed globulins
    • Astbury WT, Dickinson S and Bailey K (1935). CCLXXIX. The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem J 29, 2351-2360
    • (1935) Biochem J , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 99
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder MD, Keen NT and Jurnak F (1993). New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260, 1503-1507
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 101
    • 0000694354 scopus 로고    scopus 로고
    • Amyloidosis
    • (D.J. Weatherall, J.G.G. Ledingham and D.A. Warell, eds.) Oxford University Press: Oxford
    • Pepys MB (1996). Amyloidosis. In: The Oxford Textbook of Medicine. (D.J. Weatherall, J.G.G. Ledingham and D.A. Warell, eds.) Oxford University Press: Oxford. 1512-1524
    • (1996) The Oxford Textbook of Medicine , pp. 1512-1524
    • Pepys, M.B.1
  • 102
    • 0343223445 scopus 로고
    • The folded conformation of globular proteins
    • W. H. Freeman: New York
    • Creighton TE (1993). The folded conformation of globular proteins. In: Proteins: Structures and Molecular Properties. W. H. Freeman: New York. 201-260
    • (1993) Proteins: Structures and Molecular Properties , pp. 201-260
    • Creighton, T.E.1
  • 103
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD and Lansbury PT, Jr. (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Ann Rev Biochem 66, 385-407
    • (1997) Ann Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 104
    • 0022878817 scopus 로고
    • In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein
    • Castaño EM, Ghiso J, Prelli F, Gorevic PD, Migheli A and Frangione B (1986). In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein. Biochem Biophys Res Commun 141, 782-789
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 782-789
    • Castaño, E.M.1    Ghiso, J.2    Prelli, F.3    Gorevic, P.D.4    Migheli, A.5    Frangione, B.6
  • 105
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to β protein from Alzheimer disease forms amyloid-like fibrils in vitro
    • Kirschner DA, Inouye Y, Duffy LK, Sinclair A, Lind M and Selkoe DJ (1987). Synthetic peptide homologous to β protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc Natl Acad Sci USA 84, 6953-6957
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6953-6957
    • Kirschner, D.A.1    Inouye, Y.2    Duffy, L.K.3    Sinclair, A.4    Lind, M.5    Selkoe, D.J.6
  • 106
    • 0023473545 scopus 로고
    • Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern
    • Gorevic PD, Castaño EM, Sarma R and Frangione B (1987). Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern. Biochem Biophys Res Commun 147, 854-862
    • (1987) Biochem Biophys Res Commun , vol.147 , pp. 854-862
    • Gorevic, P.D.1    Castaño, E.M.2    Sarma, R.3    Frangione, B.4
  • 107
    • 0025734549 scopus 로고
    • Human and rodent sequence analogs of Alzheimer's amyloid βA4 share similar properties and can be solubilized in buffers of pH 7.4
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL and Beyreuther K (1991). Human and rodent sequence analogs of Alzheimer's amyloid βA4 share similar properties and can be solubilized in buffers of pH 7.4. Eur J Biochem 201, 61-69
    • (1991) Eur J Biochem , vol.201 , pp. 61-69
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 108
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4
    • Wood SJ, Wetzel R, Martin JD and Hurle MR (1995). Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry 34, 724-730
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 109
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
    • Halverson K, Fraser PE, Kirschner DA and Lansbury PT, Jr. (1990). Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments. Biochemistry 29, 2639-2644
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury Jr., P.T.4
  • 111
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL and Beyreuther K (1991). Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J Mol Biol 218, 149-163
    • (1991) J Mol Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 113
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG and Cotman CW (1995). Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity. J Neurochem 64, 253-265
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 114
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease βA4 peptides
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL and Beyreuther K (1992). Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease βA4 peptides. J Mol Biol 228, 460-473
    • (1992) J Mol Biol , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 115
    • 0002395242 scopus 로고    scopus 로고
    • Effects of β-protein mutations on amyloid fibril nucleation and elongation
    • (K. Iqbal, B. Winblad, T. Nishimura, M. Takeda and H.M. Wisniewski, eds.) John Wiley & Sons Ltd.: Chichester, England
    • Teplow DB, Lomakin A, Benedek GB, Kirschner DA and Walsh DM (1997). Effects of β-protein mutations on amyloid fibril nucleation and elongation. In: Alzheimer's Disease: Biology, Diagnosis and Therapeutics. (K. Iqbal, B. Winblad, T. Nishimura, M. Takeda and H.M. Wisniewski, eds.) John Wiley & Sons Ltd.: Chichester, England. 311-319
    • (1997) Alzheimer's Disease: Biology, Diagnosis and Therapeutics , pp. 311-319
    • Teplow, D.B.1    Lomakin, A.2    Benedek, G.B.3    Kirschner, D.A.4    Walsh, D.M.5
  • 117
    • 0030024168 scopus 로고    scopus 로고
    • Aggregation and metal-binding properties of mutant forms of the amyloid Aβ peptide of Alzheimer's disease
    • Clements A, Allsop D, Walsh DM and Williams CH (1996). Aggregation and metal-binding properties of mutant forms of the amyloid Aβ 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    Williams, C.H.4
  • 119
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease
    • Barrow CJ, Yasuda A, Kenny PTM and Zagorski M (1992). Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. J Mol Biol 225, 1075-1093
    • (1992) J Mol Biol , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.M.3    Zagorski, M.4
  • 120
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
    • Dyson HJ, Rance M, Houghten RA, Wright PE and Lerner RA (1988). Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J Mol Biol 201, 201-217
    • (1988) J Mol Biol , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 123
    • 0027249811 scopus 로고
    • Comparative analysis of human and Dutch-type Alzheimer β-amyloid peptides by infrared spectroscopy and circular dichroism
    • Fabian H, Szendrei GI, Mantsch HH and Otvos L, Jr. (1993). Comparative analysis of human and Dutch-type Alzheimer β-amyloid peptides by infrared spectroscopy and circular dichroism. Biochem Biophys Res Commun 191, 232-239
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 232-239
    • Fabian, H.1    Szendrei, G.I.2    Mantsch, H.H.3    Otvos Jr., L.4
  • 126
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood SJ, Maleeff B, Hart T and Wetzel R (1996). Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ. J Mol Biol 256, 870-877
    • (1996) J Mol Biol , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 127
    • 0028220163 scopus 로고
    • Synthetic post-translationally modified human Aβ peptide exhibits a markedly increased tendency to form β-pleated sheets in vitro
    • Fabian H, Szendrei GI, Mantsch HH, Greenberg BD and Otvos L, Jr. (1994). Synthetic post-translationally modified human Aβ peptide exhibits a markedly increased tendency to form β-pleated sheets in vitro. Eur J Biochem 221, 959-964
    • (1994) Eur J Biochem , vol.221 , pp. 959-964
    • Fabian, H.1    Szendrei, G.I.2    Mantsch, H.H.3    Greenberg, B.D.4    Otvos Jr., L.5
  • 128
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow CJ and Zagorski MG (1991). Solution structures of β peptide and its constituent fragments: relation to amyloid deposition. Science 253, 179-182
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 131
    • 0026631361 scopus 로고
    • NMR studies of amyloid β-peptides: Proton assignments, secondary structure, and mechanism of an α-helix->β-sheet conversion for a homologous, 28-residue, N-terminal fragment
    • Zagorski MG and Barrow CJ (1992). NMR studies of amyloid β-peptides: proton assignments, secondary structure, and mechanism of an α-helix->β-sheet conversion for a homologous, 28-residue, N-terminal fragment. Biochemistry 31, 5621-5631
    • (1992) Biochemistry , vol.31 , pp. 5621-5631
    • Zagorski, M.G.1    Barrow, C.J.2
  • 133
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP and Lansbury PT, Jr. (1993). The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 134
    • 0027425060 scopus 로고
    • The C-terminus of the β protein is critical in amyloidogenesis
    • Jarrett JT, Berger EP and Lansbury PT, Jr. (1993). The C-terminus of the β protein is critical in amyloidogenesis. Ann N Y Acad Sci, 144-148
    • (1993) Ann N Y Acad Sci , pp. 144-148
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 135
    • 0025607816 scopus 로고
    • Identification of a β-turn in the tertiary structure of a peptide fragment of the Alzheimer amyloid protein
    • Sorimachi K, Craik DJ, Lloyd EJ, Beyreuther K and Masters CL (1990). Identification of a β-turn in the tertiary structure of a peptide fragment of the Alzheimer amyloid protein. Biochem Int 22, 447-454
    • (1990) Biochem Int , vol.22 , pp. 447-454
    • Sorimachi, K.1    Craik, D.J.2    Lloyd, E.J.3    Beyreuther, K.4    Masters, C.L.5
  • 136
    • 0027953616 scopus 로고
    • Structure determination of extracellular fragments of amyloid proteins involved in Alzheimer's disease and Dutch-type hereditary cerebral haemorrhage with amyloidosis
    • Sorimachi K and Craik DJ (1994). Structure determination of extracellular fragments of amyloid proteins involved in Alzheimer's disease and Dutch-type hereditary cerebral haemorrhage with amyloidosis. Eur J Biochem 219, 237-251
    • (1994) Eur J Biochem , vol.219 , pp. 237-251
    • Sorimachi, K.1    Craik, D.J.2
  • 141
    • 0028980362 scopus 로고
    • The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto C, Castaño EM, Frangione B and Inestrosa NC (1995). The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J Biol Chem 270, 3063-3067
    • (1995) J Biol Chem , vol.270 , pp. 3063-3067
    • Soto, C.1    Castaño, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 142
    • 0026708694 scopus 로고
    • Kinetics of aggregation of synthetic β-amyloid peptide
    • Tomski SJ and Murphy RM (1992). Kinetics of aggregation of synthetic β-amyloid peptide. Arch Biochem Biophys 294, 630-638
    • (1992) Arch Biochem Biophys , vol.294 , pp. 630-638
    • Tomski, S.J.1    Murphy, R.M.2
  • 143
    • 0028917968 scopus 로고
    • Two conformational states of amyloid β-peptide: Implications for the pathogenesis of Alzheimer's disease
    • Soto C and Frangione B (1995). Two conformational states of amyloid β-peptide: implications for the pathogenesis of Alzheimer's disease. Neurosci Lett 186, 115-118
    • (1995) Neurosci Lett , vol.186 , pp. 115-118
    • Soto, C.1    Frangione, B.2
  • 144
    • 0028971326 scopus 로고
    • Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure
    • Soto C, Castaño EM, Kumar RA, Beavis RC and Frangione B (1995). Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure. Neurosci Lett 200, 105-108
    • (1995) Neurosci Lett , vol.200 , pp. 105-108
    • Soto, C.1    Castaño, E.M.2    Kumar, R.A.3    Beavis, R.C.4    Frangione, B.5
  • 145
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT and Lansbury PT, Jr (1993). Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 146
    • 0022456807 scopus 로고
    • The measurement of cooperative protein self-assembly by turbidity and other techniques
    • Andreu JM and Timasheff SN (1986). The measurement of cooperative protein self-assembly by turbidity and other techniques. Meth Enzymol 130, 47-59
    • (1986) Meth Enzymol , vol.130 , pp. 47-59
    • Andreu, J.M.1    Timasheff, S.N.2
  • 149
    • 0027989805 scopus 로고
    • Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide
    • Shen CL, Fitzgerald MC and Murphy RM (1994). Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide. Biophysical J 67, 1238-1246
    • (1994) Biophysical J , vol.67 , pp. 1238-1246
    • Shen, C.L.1    Fitzgerald, M.C.2    Murphy, R.M.3
  • 151
    • 0000424908 scopus 로고
    • Dynamics of rigid and semi-rigid rodlike polymers
    • Tracy MA and Pecora R (1992). Dynamics of rigid and semi-rigid rodlike polymers. Ann Rev Phys Chem 43, 525-557
    • (1992) Ann Rev Phys Chem , vol.43 , pp. 525-557
    • Tracy, M.A.1    Pecora, R.2
  • 152
    • 0029157531 scopus 로고
    • Solvent effects on self-assembly of β-amyloid peptide
    • Shen CL and Murphy RM (1995). Solvent effects on self-assembly of β-amyloid peptide. Biophysical J 69, 640-651
    • (1995) Biophysical J , vol.69 , pp. 640-651
    • Shen, C.L.1    Murphy, R.M.2
  • 154
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology
    • Seilheimer B, Bohrmann B, Bondolfi L, Muller F, Stuber D and Döbeli H (1997). The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology. J Struct Biol 119, 59-71
    • (1997) J Struct Biol , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Döbeli, H.6
  • 156
    • 0021772650 scopus 로고
    • Kinetics of unfolding of proteins on hydrophobic surfaces in reversed-phase liquid chromatography
    • Benedek K, Dong S and Karger BL (1984). Kinetics of unfolding of proteins on hydrophobic surfaces in reversed-phase liquid chromatography. J Chromatogr 317, 227-243
    • (1984) J Chromatogr , vol.317 , pp. 227-243
    • Benedek, K.1    Dong, S.2    Karger, B.L.3
  • 157
    • 0015916486 scopus 로고
    • Nuclear magnetic resonance studies of a polypeptide in a nonprotonating solvent system
    • Bradbury EM, Crane-Robinson C and Temussi LP (1973). Nuclear magnetic resonance studies of a polypeptide in a nonprotonating solvent system. J Am Chem Soc 95, 1683-1684
    • (1973) J Am Chem Soc , vol.95 , pp. 1683-1684
    • Bradbury, E.M.1    Crane-Robinson, C.2    Temussi, L.P.3
  • 159
    • 0000113382 scopus 로고    scopus 로고
    • Conformations of β-amyloid in solution - Reply
    • Kaneko I (1997). Conformations of β-amyloid in solution - Reply. J Neurochem 68, 438-439
    • (1997) J Neurochem , vol.68 , pp. 438-439
    • Kaneko, I.1
  • 160
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis - Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM and Teplow DB (1997). Amyloid β-protein fibrillogenesis - Detection of a protofibrillar intermediate. J Biol Chem 272, 22364-22372
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 161
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation
    • Soreghan B, Kosmoski J and Glabe C (1994). Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation. J Biol Chem 269, 28551-28554
    • (1994) J Biol Chem , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 162
    • 0028180196 scopus 로고
    • Modulation of Aβ adhesiveness and secretase site cleavage by zinc
    • Bush AI, Pettingell WHJ, de Paradis M and Tanzi RE (1994). Modulation of Aβ adhesiveness and secretase site cleavage by zinc. J Biol Chem 269, 12152-12158
    • (1994) J Biol Chem , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell, W.H.J.2    De Paradis, M.3    Tanzi, R.E.4
  • 166
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki H and Nakakuki K (1996). First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab Invest 74, 374-383
    • (1996) Lab Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 167
    • 0016740820 scopus 로고
    • Immunoassay by light scattering spectroscopy
    • Cohen RJ and Benedek GB (1975). Immunoassay by light scattering spectroscopy. Immunochemistry 12, 349-351
    • (1975) Immunochemistry , vol.12 , pp. 349-351
    • Cohen, R.J.1    Benedek, G.B.2
  • 168
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils - Detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA and Teplow DB (1996). On the nucleation and growth of amyloid β-protein fibrils - Detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 93, 1125-1129
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 170
    • 0028832472 scopus 로고
    • Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution
    • LeVine H, III (1995). Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution. Neurobiol Aging 16, 755-764
    • (1995) Neurobiol Aging , vol.16 , pp. 755-764
    • LeVine III, H.1
  • 171
    • 0030611858 scopus 로고    scopus 로고
    • Soluble amyloid Aβ-(1-40) exists as a stable dimer at low concentrations
    • Garzon-Rodriguez W, Sepulveda-Becerra M, Milton S and Glabe CG (1997). Soluble amyloid Aβ-(1-40) exists as a stable dimer at low concentrations. J Biol Chem 272, 21037-21044
    • (1997) J Biol Chem , vol.272 , pp. 21037-21044
    • Garzon-Rodriguez, W.1    Sepulveda-Becerra, M.2    Milton, S.3    Glabe, C.G.4
  • 172
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM and Lansbury PT (1997). Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem Biol 4, 119-125
    • (1997) Chem Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 173
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper JD, Lieber CM and Lansbury PT (1997). Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem Biol 4, 951-959
    • (1997) Chem Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 175
    • 0029914688 scopus 로고    scopus 로고
    • Apolipoprotein E and Alzheimer's disease
    • Strittmatter WJ and Roses AD (1996). Apolipoprotein E and Alzheimer's disease. Ann Rev Neurosci 19, 53-77
    • (1996) Ann Rev Neurosci , vol.19 , pp. 53-77
    • Strittmatter, W.J.1    Roses, A.D.2
  • 183
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • Wisniewski T, Castaño EM, Golabek A, Vogel T and Frangione B (1994). Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am J Pathol 145, 1030-1035
    • (1994) Am J Pathol , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castaño, E.M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 185
    • 0028173205 scopus 로고
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature 372, 92-94
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.Y.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 187
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation
    • Golabek AA, Soto C, Vogel T and Wisniewski T (1996). The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation. J Biol Chem 271, 10602-10606
    • (1996) J Biol Chem , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4
  • 188
    • 0028872558 scopus 로고
    • Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer's disease
    • Evans KC, Berger EP, Cho CG, Weisgraber KH and Lansbury PT (1995). Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer's disease. Proc Natl Acad Sci USA 92, 163-161
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 163-1161
    • Evans, K.C.1    Berger, E.P.2    Cho, C.G.3    Weisgraber, K.H.4    Lansbury, P.T.5
  • 189
    • 0029836629 scopus 로고    scopus 로고
    • Seeding of Aβ fibril formation is inhibited by all three isotypes of apolipoprotein E
    • Wood SJ, Chan W and Wetzel R (1996). Seeding of Aβ fibril formation is inhibited by all three isotypes of apolipoprotein E. Biochemistry 35, 12623-12628
    • (1996) Biochemistry , vol.35 , pp. 12623-12628
    • Wood, S.J.1    Chan, W.2    Wetzel, R.3
  • 191
    • 0030977663 scopus 로고    scopus 로고
    • Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's β-amyloid fibril formation in vitro
    • Naiki H, Gejyo F and Nakakuki K (1997). Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's β-amyloid fibril formation in vitro. Biochemistry 36, 6243-6250
    • (1997) Biochemistry , vol.36 , pp. 6243-6250
    • Naiki, H.1    Gejyo, F.2    Nakakuki, K.3
  • 192
    • 0030592330 scopus 로고    scopus 로고
    • α1-Antichymotrypsin interaction with Aβ(1-42) does not inhibit fibril formation but attenuates the peptide toxicity
    • Aksenov MY, Aksenova MV, Carney JM and Butterfield DA (1996). α1-Antichymotrypsin interaction with Aβ(1-42) does not inhibit fibril formation but attenuates the peptide toxicity. Neurosci Lett 217, 117-120
    • (1996) Neurosci Lett , vol.217 , pp. 117-120
    • Aksenov, M.Y.1    Aksenova, M.V.2    Carney, J.M.3    Butterfield, D.A.4
  • 193
    • 0027322517 scopus 로고
    • α1-Antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro
    • Fraser PE, Nguyen JT, McLachlan DR, Abraham CR and Kirschner DA (1993). α1-Antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro. J Neurochem 61, 298-305
    • (1993) J Neurochem , vol.61 , pp. 298-305
    • Fraser, P.E.1    Nguyen, J.T.2    McLachlan, D.R.3    Abraham, C.R.4    Kirschner, D.A.5
  • 194
    • 0028986858 scopus 로고
    • α1-Antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation
    • Eriksson S, Janciauskiene S and Lannfelt L (1995). α1-Antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation. Proc Natl Acad Sci USA 92, 2313-2317
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2313-2317
    • Eriksson, S.1    Janciauskiene, S.2    Lannfelt, L.3
  • 195
    • 0029758030 scopus 로고    scopus 로고
    • Relative efficacies of amyloid β peptide (Aβ) binding proteins in Aβ aggregation
    • Webster S and Rogers J (1996). Relative efficacies of amyloid β peptide (Aβ) binding proteins in Aβ aggregation. J Neurosci Res 46, 58-66
    • (1996) J Neurosci Res , vol.46 , pp. 58-66
    • Webster, S.1    Rogers, J.2
  • 196
    • 0030329641 scopus 로고    scopus 로고
    • Interaction of transthyretin with amyloid β-protein: Binding and inhibition of amyloid formation
    • Schwarzman AL and Goldgaber D (1996). Interaction of transthyretin with amyloid β-protein: binding and inhibition of amyloid formation. Ciba Foundation Symposium 199, 146-164
    • (1996) Ciba Foundation Symposium , vol.199 , pp. 146-164
    • Schwarzman, A.L.1    Goldgaber, D.2
  • 199
    • 0029920929 scopus 로고    scopus 로고
    • Glycoprotein 330/megalin: Probable role in receptor-mediated transport of apolipoprotein J alone and in complex with Alzheimer disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers
    • Zlokovic BV, Martel CL, Matsubara E, McComb JG, Zheng G, McCluskey RT, Frangione B and Ghiso J (1996). Glycoprotein 330/megalin: Probable role in receptor-mediated transport of apolipoprotein J alone and in complex with Alzheimer disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers. Proc Natl Acad Sci USA 93, 4229-4234
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4229-4234
    • Zlokovic, B.V.1    Martel, C.L.2    Matsubara, E.3    McComb, J.G.4    Zheng, G.5    McCluskey, R.T.6    Frangione, B.7    Ghiso, J.8
  • 200
    • 0029063033 scopus 로고
    • Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid
    • Golabek A, Marques MA, Lalowski M and Wisniewski T (1995). Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid. Neurosci Lett 191, 79-82
    • (1995) Neurosci Lett , vol.191 , pp. 79-82
    • Golabek, A.1    Marques, M.A.2    Lalowski, M.3    Wisniewski, T.4
  • 201
    • 0023626638 scopus 로고
    • The cytoskeletal pathology of Alzheimer's disease is characterized by aberrant tau distribution
    • Kowall NW and Kosik KS (1987). The cytoskeletal pathology of Alzheimer's disease is characterized by aberrant tau distribution. Ann Neurol 22, 639-643
    • (1987) Ann Neurol , vol.22 , pp. 639-643
    • Kowall, N.W.1    Kosik, K.S.2
  • 203
    • 0027186334 scopus 로고
    • The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
    • Ghiso J, Matsubara E, Koudinov A, Choi-Miura NH, Tomita M, Wisniewski T and Frangione B (1993). The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. Biochem J 293, 27-30
    • (1993) Biochem J , vol.293 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3    Choi-Miura, N.H.4    Tomita, M.5    Wisniewski, T.6    Frangione, B.7
  • 204
    • 0028609448 scopus 로고
    • The soluble form of Alzheimer's amyloid beta protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma
    • Koudinov A, Matsubara E, Frangione B and Ghiso J (1994). The soluble form of Alzheimer's amyloid beta protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma. Biochem Biophys Res Commun 205, 1164-1171
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1164-1171
    • Koudinov, A.1    Matsubara, E.2    Frangione, B.3    Ghiso, J.4
  • 206
    • 0028988187 scopus 로고
    • 2+-dependent binding of human serum amyloid P component to Alzheimer's β-amyloid peptide
    • 2+-dependent binding of human serum amyloid P component to Alzheimer's β-amyloid peptide. J Biol Chem 270, 10392-10394
    • (1995) J Biol Chem , vol.270 , pp. 10392-10394
    • Hamazaki, H.1
  • 207
    • 0028135459 scopus 로고
    • Enhanced aggregation and β structure of amyloid β peptide after coincubation with C1q
    • Webster S, O'Barr S and Rogers J (1994). Enhanced aggregation and β structure of amyloid β peptide after coincubation with C1q. J Neurosci Res 39, 448-456
    • (1994) J Neurosci Res , vol.39 , pp. 448-456
    • Webster, S.1    O'Barr, S.2    Rogers, J.3
  • 209
    • 0028298620 scopus 로고
    • Transglutaminase facilitates the formation of polymers of the β-amyloid peptide
    • Dudek SM and Johnson G (1994). Transglutaminase facilitates the formation of polymers of the β-amyloid peptide. Brain Res 651, 129-133
    • (1994) Brain Res , vol.651 , pp. 129-133
    • Dudek, S.M.1    Johnson, G.2
  • 211
    • 0028818362 scopus 로고
    • Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides
    • Alvarez A, Bronfman F, Perez CA, Vicente M, Garrido J and Inestrosa NC (1995). Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides. Neurosci Lett 201, 49-52
    • (1995) Neurosci Lett , vol.201 , pp. 49-52
    • Alvarez, A.1    Bronfman, F.2    Perez, C.A.3    Vicente, M.4    Garrido, J.5    Inestrosa, N.C.6
  • 212
    • 0031054785 scopus 로고    scopus 로고
    • The interaction between Alzheimer amyloid β(1-40) peptide and ganglioside GM1-containing membranes
    • Choo-Smith LP and Surewicz WK (1997). The interaction between Alzheimer amyloid β(1-40) peptide and ganglioside GM1-containing membranes. FEBS Lett 402, 95-98
    • (1997) FEBS Lett , vol.402 , pp. 95-98
    • Choo-Smith, L.P.1    Surewicz, W.K.2
  • 213
    • 0028978227 scopus 로고
    • Proteoglycan-mediated inhibition of Aβ proteolysis - A potential cause of senile plaque accumulation
    • Guptabansal R, Frederickson RCA and Brunden KR (1995). Proteoglycan-mediated inhibition of Aβ proteolysis - A potential cause of senile plaque accumulation. J Biol Chem 270, 18666-18671
    • (1995) J Biol Chem , vol.270 , pp. 18666-18671
    • Guptabansal, R.1    Frederickson, R.C.A.2    Brunden, K.R.3
  • 214
    • 0030725311 scopus 로고    scopus 로고
    • Perlecan binds to the β-amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability
    • Castillo GM, Ngo C, Cummings J, Wight TN and Snow AD (1997). Perlecan binds to the β-amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability. J Neurochem 69, 2452-2465
    • (1997) J Neurochem , vol.69 , pp. 2452-2465
    • Castillo, G.M.1    Ngo, C.2    Cummings, J.3    Wight, T.N.4    Snow, A.D.5
  • 215
    • 0024339115 scopus 로고
    • Cationic dyes reveal proteoglycans structurally integrated within the characteristic lesions of Alzheimer's disease
    • Snow AD, Lara S, Nochlin D and Wight TN (1989). Cationic dyes reveal proteoglycans structurally integrated within the characteristic lesions of Alzheimer's disease. Acta Neuropath 78, 113-123
    • (1989) Acta Neuropath , vol.78 , pp. 113-123
    • Snow, A.D.1    Lara, S.2    Nochlin, D.3    Wight, T.N.4
  • 216
    • 0000416462 scopus 로고    scopus 로고
    • Specific proteoglycans as potential causative agents and relevant targets for therapeutic intervention in Alzheimer's disease and other amyloidoses
    • Snow AD and Castillo GM (1997). Specific proteoglycans as potential causative agents and relevant targets for therapeutic intervention in Alzheimer's disease and other amyloidoses. Amyloid: Int J Exp Clin Invest 4, 135-141
    • (1997) Amyloid: Int J Exp Clin Invest , vol.4 , pp. 135-141
    • Snow, A.D.1    Castillo, G.M.2
  • 219
    • 0028542113 scopus 로고
    • Aggregation of amyloid β-protein and its neurotoxicity: Enhancement by aluminum and other metals
    • Kuroda Y and Kawahara M (1994). Aggregation of amyloid β-protein and its neurotoxicity: Enhancement by aluminum and other metals. Tohoku J Exp Med 174, 263-268
    • (1994) Tohoku J Exp Med , vol.174 , pp. 263-268
    • Kuroda, Y.1    Kawahara, M.2
  • 222
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson DM and Binder LI (1997). Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am J Pathol 150, 2181-2195
    • (1997) Am J Pathol , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.