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Volumn 6, Issue 1, 2011, Pages

Extracellular and intraneuronal HMW-AbetaOs represent a molecular basis of memory loss in Alzheimer's disease model mouse

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; DIMER; HIGH MOLECULAR WEIGH AMYLOID BETA OLIGOMER; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1A9; MONOCLONAL ANTIBODY 2C3; OLIGOMER; TETRAMER; UNCLASSIFIED DRUG;

EID: 79952196722     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-6-20     Document Type: Article
Times cited : (31)

References (36)
  • 1
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • 10.1016/0165-6147(91)90609-V. 1763432
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease. J Hardy D Allsop, Trends Pharmacol Sci 1991 12 383 388 10.1016/0165-6147(91)90609-V 1763432
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 3
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • 10.1002/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M. 10589538
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. CA McLean RA Cherny FW Fraser SJ Fuller MJ Smith K Beyreuther AI Bush CL Masters, Ann Neurol 1999 46 860 866 10.1002/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M 10589538
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5    Beyreuther, K.6    Bush, A.I.7    Masters, C.L.8
  • 4
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small A β oligomers: The solution to an Alzheimer's disease conundrum?
    • DOI 10.1016/S0166-2236(00)01749-5, PII S0166223600017495
    • Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? WL Klein GA Krafft CE Finch, Trends Neurosci 2001 24 219 224 10.1016/S0166-2236(00)01749-5 11250006 (Pubitemid 32204378)
    • (2001) Trends in Neurosciences , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 5
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • DOI 10.1126/science.1074069
    • Alzheimer's disease is a synaptic failure. DJ Selkoe, Science 2002 298 789 791 10.1126/science.1074069 12399581 (Pubitemid 35231524)
    • (2002) Science , vol.298 , Issue.5594 , pp. 789-791
    • Selkoe, D.J.1
  • 6
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid -peptide. C Hass DJ Selkoe, Nat Rev Mol Cell Biol 2007 8 101 112 10.1038/nrm2101 17245412 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 8
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • 10.1126/science.1566067. 1566067
    • Alzheimer's disease: the amyloid cascade hypothesis. JA Hardy GA Higgins, Science 1992 256 184 185 10.1126/science.1566067 1566067
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 12
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. R Kayed E Head JL Thompson TM Mclntire SC Milton CW Cotman CG Glabe, Science 2003 300 486 489 10.1126/science.1079469 12702875 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 14
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo. DM Walsh I Klyubin JV Fadeeva WK Cullen R Anwyl MS Wolfe MJ Rowan DJ Selkoe, Nature 2002 16 535 539 10.1038/416535a (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 25
    • 4444229469 scopus 로고    scopus 로고
    • Lipid membrane formation by vesicle fusion on silicon dioide surfaces modified with alkyl self-assembled monolayer islands
    • 10.1021/la0400306. 15323498
    • Lipid membrane formation by vesicle fusion on silicon dioide surfaces modified with alkyl self-assembled monolayer islands. R Tero M Takizawa YJ Li M Yamazaki T Urisu, Langmuir 2004 20 7526 7531 10.1021/la0400306 15323498
    • (2004) Langmuir , vol.20 , pp. 7526-7531
    • Tero, R.1    Takizawa, M.2    Li, Y.J.3    Yamazaki, M.4    Urisu, T.5
  • 27
    • 33645220400 scopus 로고    scopus 로고
    • Targeting amyloid-β peptide (Aβ) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Aβ precursor protein (APP) transgenic mice
    • DOI 10.1074/jbc.M511018200
    • Targeting amyloid- peptide (A) oligomers by passive immunization with a conformation-selective monoclonal antibodies improves learning and memory in A precursor protein (APP) transgenic mice. EB Lee LZ Leng B Zhang L Kwong JQ Trojanowski VM Lee, J Biol Chem 2006 281 4292 4299 10.1074/jbc.M511018200 16361260 (Pubitemid 43847859)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 4292-4299
    • Lee, E.B.1    Leng, L.Z.2    Zhang, B.3    Kwong, L.4    Trojanowski, J.Q.5    Abel, T.6    Lee, V.M.-Y.7
  • 28
    • 34347399599 scopus 로고    scopus 로고
    • Oral vaccination with a viral vector containing Aβ cDNA attenuates age-related Aβ accumulation and memory deficits without causing inflammation in a mouse Alzheimer model
    • DOI 10.1096/fj.06-7685com
    • Oral vaccination with a viral vector containing A cDNA attenuates age-related A accumulation and memory deficits without causing inflammation in a mouse Alzheimer model. A Mouri Y Noda H Hara H Mizoguchi T Tabira T Nabeshim, FASEB J 2007 21 2135 2148 10.1096/fj.06-7685com 17341681 (Pubitemid 47026449)
    • (2007) FASEB Journal , vol.21 , Issue.9 , pp. 2135-2148
    • Mouri, A.1    Noda, Y.2    Hara, H.3    Mizoguchi, H.4    Tabira, T.5    Nabeshima, T.6
  • 29
    • 0034714392 scopus 로고    scopus 로고
    • A high affinity fluorescent marker for the localization of neuronal degeneration
    • 10.1016/S0006-8993(00)02513-0. 10960596
    • A high affinity fluorescent marker for the localization of neuronal degeneration. LC Schmued KJ Hopkins B Fluoro-Jade, Brain Res 2000 874 123 130 10.1016/S0006-8993(00)02513-0 10960596
    • (2000) Brain Res , vol.874 , pp. 123-130
    • Schmued, L.C.1    Hopkins, K.J.2    Fluoro-Jade, B.3
  • 32
    • 11144356498 scopus 로고    scopus 로고
    • Dimeric Amyloid β Protein Rapidly Accumulates in Lipid Rafts followed by Apolipoprotein E and Phosphorylated Tau Accumulation in the Tg2576 Mouse Model of Alzheimer's Disease
    • DOI 10.1523/JNEUROSCI.5543-03.2004
    • Dimeric amyloid beta protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease. T Kawarabayashi M Shoji LH Younkin L Wen-Lang DW Dickson T Murakami E Matsubara K Abe KH Ashe SG Younkin, J Neurosci 2004 24 3801 3809 10.1523/JNEUROSCI.5543-03.2004 15084661 (Pubitemid 38509410)
    • (2004) Journal of Neuroscience , vol.24 , Issue.15 , pp. 3801-3809
    • Kawarabayashi, T.1    Shoji, M.2    Younkin, L.H.3    Wen-Lang, L.4    Dickson, D.W.5    Murakami, T.6    Matsubara, E.7    Abe, K.8    Ashe, K.H.9    Younkin, S.G.10
  • 34
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • 10.1073/pnas.0911281106. 19910533
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. X Hu SL Crick G Bu C Frieden RV Pappu JM Lee, Proc Natl Acad Sci USA 2009 106 20324 20329 10.1073/pnas.0911281106 19910533
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 36
    • 0028921915 scopus 로고
    • Characterization of apolipoprotein J-Alzheimer's A beta interaction
    • 10.1074/jbc.270.13.7563. 7706304
    • Characterization of apolipoprotein J-Alzheimer's A beta interaction. E Matsubara B Frangione J Ghiso, J Biol Chem 1995 270 7563 7567 10.1074/jbc.270.13.7563 7706304
    • (1995) J Biol Chem , vol.270 , pp. 7563-7567
    • Matsubara, E.1    Frangione, B.2    Ghiso, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.