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Volumn 154, Issue 1, 1999, Pages 271-279

Appearance of sodium dodecyl sulfate-stable amyloid β-protein (Aβ) dimer in the cortex during aging

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; DODECYL SULFATE SODIUM; OLIGOMER;

EID: 0032893154     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)65273-X     Document Type: Article
Times cited : (90)

References (40)
  • 5
    • 0029813177 scopus 로고    scopus 로고
    • Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F β-amyloid precursor protein and Alzheimer's disease
    • Masliah E, Sisk A, Mallory M, Mucke L, Schenk D, Games D: Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F β-amyloid precursor protein and Alzheimer's disease. J Neurosci 1996, 16:5795-5811
    • (1996) J Neurosci , vol.16 , pp. 5795-5811
    • Masliah, E.1    Sisk, A.2    Mallory, M.3    Mucke, L.4    Schenk, D.5    Games, D.6
  • 6
    • 0030611097 scopus 로고    scopus 로고
    • Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F (PDAPP) transgenic mouse
    • Irizarry MC, Soriano F, McNamara M, Page KJ, Schenk D, Games D, Hyman BT: Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F (PDAPP) transgenic mouse. J Neurosci 1997, 17:7053-7059
    • (1997) J Neurosci , vol.17 , pp. 7053-7059
    • Irizarry, M.C.1    Soriano, F.2    McNamara, M.3    Page, K.J.4    Schenk, D.5    Games, D.6    Hyman, B.T.7
  • 8
    • 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, Lansbury PTJr: 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 1993, 32:4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 9
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y: Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron 1994, 13:45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 10
    • 0028919919 scopus 로고
    • Amyloid β-protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down's syndrome
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y: Amyloid β-protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down's syndrome: Ann Neurol 1995, 37:294-299
    • (1995) Ann Neurol , vol.37 , pp. 294-299
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 11
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants
    • Suzuki N, Cheung TT, Cai X-D, Odaka A, Otvos LJr, Eckman C, Golde TE, Younkin SG: An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants. Science 1994, 264:1336-1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.-D.3    Odaka, A.4    Otvos L., Jr.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 18
    • 0029664434 scopus 로고    scopus 로고
    • Aβ-peptide length and apolipoprotein E genotype in Alzheimer's disease
    • Gearing M, Mori H, Mirra SS: Aβ-peptide length and apolipoprotein E genotype in Alzheimer's disease. Ann Neurol 1997, 39:395-399
    • (1997) Ann Neurol , vol.39 , pp. 395-399
    • Gearing, M.1    Mori, H.2    Mirra, S.S.3
  • 21
    • 0028984919 scopus 로고
    • Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells
    • Asami-Odaka A, Ishibashi Y, Kikuchi T, Kitada C, Suzuki N: Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells. Biochemistry 1995, 34:10272-10278
    • (1995) Biochemistry , vol.34 , pp. 10272-10278
    • Asami-Odaka, A.1    Ishibashi, Y.2    Kikuchi, T.3    Kitada, C.4    Suzuki, N.5
  • 24
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid β-protein (Aβ): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K, Odaka A, Suzuki N, Ihara Y: GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nat Med 1995, 1:1062-1066
    • (1995) Nat Med , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 25
    • 0031886976 scopus 로고    scopus 로고
    • Diffuse plaques associated with astroglial amyloid β protein, possibly showing disappearing stage of senile plaques
    • Yamaguchi H, Sugihara S, Ogawa A, Saido TC, Ihara Y: Diffuse plaques associated with astroglial amyloid β protein, possibly showing disappearing stage of senile plaques. Acta Neuropathol (Berl) 1998, 95:217-222
    • (1998) Acta Neuropathol (Berl) , vol.95 , pp. 217-222
    • Yamaguchi, H.1    Sugihara, S.2    Ogawa, A.3    Saido, T.C.4    Ihara, Y.5
  • 26
    • 0025257612 scopus 로고
    • Restriction isotyping of human apolipoprotein E by gene amplification and cleavage with Hhal
    • Hixson JE, Vernier DT: Restriction isotyping of human apolipoprotein E by gene amplification and cleavage with Hhal. J Lipid Res 1990, 31:545-548
    • (1990) J Lipid Res , vol.31 , pp. 545-548
    • Hixson, J.E.1    Vernier, D.T.2
  • 27
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid β protein in Alzheimer's disease
    • Mori H, Takio K, Ogawara M, Selkoe DJ: Mass spectrometry of purified amyloid β protein in Alzheimer's disease. J Biol Chem 1992, 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
  • 30
    • 0031862969 scopus 로고    scopus 로고
    • Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease
    • Kuo Y-M, Webster S, Emmerling MR, Lima ND, Roher AE: Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease. Biochim Biophys Acta 1998, 1406:291-298
    • (1998) Biochim Biophys Acta , vol.1406 , pp. 291-298
    • Kuo, Y.-M.1    Webster, S.2    Emmerling, M.R.3    Lima, N.D.4    Roher, A.E.5
  • 31
    • 0030775361 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) 1-40 but not Aβ1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain
    • Shin R-W, Ogino K, Kondo A, Saido TC, Trojanowski JQ, Kitamoto T, Tateishi J: Amyloid β-protein (Aβ) 1-40 but not Aβ1-42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain. J Neurosci 1997, 17:8187-8193
    • (1997) J Neurosci , vol.17 , pp. 8187-8193
    • Shin, R.-W.1    Ogino, K.2    Kondo, A.3    Saido, T.C.4    Trojanowski, J.Q.5    Kitamoto, T.6    Tateishi, J.7
  • 32
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I, Schenk DB: Characterization of β-amyloid peptide from human cerebrospinal fluid. J Neurochem 1993, 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
  • 33
    • 0031587429 scopus 로고    scopus 로고
    • Detection of apolipoprotein E/dimeric soluble amyloid β complexes in Alzheimer's disease brain supernatants
    • Permanne B, Perez C, Soto C, Frangione B, Wisniewski T: Detection of apolipoprotein E/dimeric soluble amyloid β complexes in Alzheimer's disease brain supernatants. Biochem Biophys Res Commun 1997, 240:715-720
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 715-720
    • Permanne, B.1    Perez, C.2    Soto, C.3    Frangione, B.4    Wisniewski, T.5
  • 35
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia W, Zhang J, Kholodenko D, Citron M, Podlisny MB, Teplow DB, Haass C, Seubert P, Koo EH, Selkoe DJ: Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J Biol Chem 1997, 272:7977-7982
    • (1997) J Biol Chem , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haass, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 36
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • Podlisny MB, Walsh DM, Amarante P, Ostaszewski BL, Stimson ER, Maggio JE, Treplow DB, Selkoe DJ: Oligomerization of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 1998, 37:3602-3611
    • (1998) Biochemistry , vol.37 , pp. 3602-3611
    • Podlisny, M.B.1    Walsh, D.M.2    Amarante, P.3    Ostaszewski, B.L.4    Stimson, E.R.5    Maggio, J.E.6    Treplow, D.B.7    Selkoe, D.J.8
  • 37
  • 38
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB: Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate. J Biol Chem 1997, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.