메뉴 건너뛰기




Volumn 384, Issue 4, 2008, Pages 917-928

Anti-oligomeric Aβ Single-chain Variable Domain Antibody Blocks Aβ-induced Toxicity Against Human Neuroblastoma Cells

Author keywords

Alzheimer's disease; A ; oligomers; phage display; ScFv

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; OLIGOMER; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; AMYLOID BETA PROTEIN; ANTIBODY; PEPTIDE LIBRARY;

EID: 56249092747     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.09.068     Document Type: Article
Times cited : (74)

References (64)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron 6 (1991) 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 2
    • 0028986916 scopus 로고
    • beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., and Yankner B.A. beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14 (1995) 879-888
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 3
    • 0032150877 scopus 로고    scopus 로고
    • Genetic dissection of Alzheimer's disease and related dementias: amyloid and its relationship to tau
    • Hardy J., Duff K., Hardy K.G., Perez-Tur J., and Hutton M. Genetic dissection of Alzheimer's disease and related dementias: amyloid and its relationship to tau. Nature Neurosci. 1 (1998) 355-358
    • (1998) Nature Neurosci. , vol.1 , pp. 355-358
    • Hardy, J.1    Duff, K.2    Hardy, K.G.3    Perez-Tur, J.4    Hutton, M.5
  • 4
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J.A., and Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 256 (1992) 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 5
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A., and Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl Acad. Sci. USA 91 (1994) 12243-12247
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 6
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., and Cotman C.W. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13 (1993) 1676-1687
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 8
    • 0022616654 scopus 로고
    • Alzheimer's disease
    • Katzman R. Alzheimer's disease. N. Engl. J. Med. 314 (1986) 964-973
    • (1986) N. Engl. J. Med. , vol.314 , pp. 964-973
    • Katzman, R.1
  • 9
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment
    • Terry R.D., Masliah E., Salmon D.P., Butters N., DeTeresa R., Hill R., et al. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30 (1991) 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
  • 10
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model
    • Dodart J.C., Bales K.R., Gannon K.S., Greene S.J., DeMattos R.B., Mathis C., et al. Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model. Nature Neurosci. 5 (2002) 452-457
    • (2002) Nature Neurosci. , vol.5 , pp. 452-457
    • Dodart, J.C.1    Bales, K.R.2    Gannon, K.S.3    Greene, S.J.4    DeMattos, R.B.5    Mathis, C.6
  • 13
    • 0028828044 scopus 로고
    • Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress
    • Oda T., Wals P., Osterburg H.H., Johnson S.A., Pasinetti G.M., Morgan T.E., et al. Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress. Exp. Neurol. 136 (1995) 22-31
    • (1995) Exp. Neurol. , vol.136 , pp. 22-31
    • Oda, T.1    Wals, P.2    Osterburg, H.H.3    Johnson, S.A.4    Pasinetti, G.M.5    Morgan, T.E.6
  • 14
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl Acad. Sci. USA 95 (1998) 6448-6453
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 15
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean C.A., Cherny R.A., Fraser F.W., Fuller S.J., Smith M.J., Beyreuther K., et al. Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46 (1999) 860-866
    • (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
  • 16
    • 0032893154 scopus 로고    scopus 로고
    • Appearance of sodium dodecyl sulfate-stable amyloid beta-protein (Abeta) dimer in the cortex during aging
    • Enya M., Morishima-Kawashima M., Yoshimura M., Shinkai Y., Kusui K., Khan K., et al. Appearance of sodium dodecyl sulfate-stable amyloid beta-protein (Abeta) dimer in the cortex during aging. Am. J. Pathol. 154 (1999) 271-279
    • (1999) Am. J. Pathol. , vol.154 , pp. 271-279
    • Enya, M.1    Morishima-Kawashima, M.2    Yoshimura, M.3    Shinkai, Y.4    Kusui, K.5    Khan, K.6
  • 17
    • 0032983254 scopus 로고    scopus 로고
    • Presence of sodium dodecyl sulfate-stable amyloid beta-protein dimers in the hippocampus CA1 not exhibiting neurofibrillary tangle formation
    • Funato H., Enya M., Yoshimura M., Morishima-Kawashima M., and Ihara Y. Presence of sodium dodecyl sulfate-stable amyloid beta-protein dimers in the hippocampus CA1 not exhibiting neurofibrillary tangle formation. Am. J. Pathol. 155 (1999) 23-28
    • (1999) Am. J. Pathol. , vol.155 , pp. 23-28
    • Funato, H.1    Enya, M.2    Yoshimura, M.3    Morishima-Kawashima, M.4    Ihara, Y.5
  • 18
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • Roher A.E., Chaney M.O., Kuo Y.M., Webster S.D., Stine W.B., Haverkamp L.J., et al. Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J. Biol. Chem. 271 (1996) 20631-20635
    • (1996) J. Biol. Chem. , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Kuo, Y.M.3    Webster, S.D.4    Stine, W.B.5    Haverkamp, L.J.6
  • 19
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , 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
  • 21
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar G.M., Bloodgood B.L., Townsend M., Walsh D.M., Selkoe D.J., and Sabatini B.L. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27 (2007) 2866-2875
    • (2007) J. Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 22
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S., Koh M.T., Kotilinek L., Kayed R., Glabe C.G., Yang A., et al. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440 (2006) 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    Yang, A.6
  • 23
    • 0037151046 scopus 로고    scopus 로고
    • Accelerated plaque accumulation, associative learning deficits, and up-regulation of alpha 7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins
    • Dineley K.T., Xia X., Bui D., Sweatt J.D., and Zheng H. Accelerated plaque accumulation, associative learning deficits, and up-regulation of alpha 7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins. J. Biol. Chem. 277 (2002) 22768-22780
    • (2002) J. Biol. Chem. , vol.277 , pp. 22768-22780
    • Dineley, K.T.1    Xia, X.2    Bui, D.3    Sweatt, J.D.4    Zheng, H.5
  • 25
    • 34248190279 scopus 로고    scopus 로고
    • Abeta Oligomers - a decade of discovery
    • Walsh D.M., and Selkoe D.J. Abeta Oligomers - a decade of discovery. J. Neurochem. 101 (2007) 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 26
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: a feedforward mechanism for Alzheimer's disease
    • Maloney M.T., Minamide L.S., Kinley A.W., Boyle J.A., and Bamburg J.R. Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: a feedforward mechanism for Alzheimer's disease. J. Neurosci. 25 (2005) 11313-11321
    • (2005) J. Neurosci. , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 28
    • 33748792254 scopus 로고    scopus 로고
    • beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons
    • Kelly B.L., and Ferreira A. beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons. J. Biol. Chem. 281 (2006) 28079-28089
    • (2006) J. Biol. Chem. , vol.281 , pp. 28079-28089
    • Kelly, B.L.1    Ferreira, A.2
  • 29
    • 33745228920 scopus 로고    scopus 로고
    • The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression
    • Tamagno E., Bardini P., Guglielmotto M., Danni O., and Tabaton M. The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression. Free Radic. Biol. Med. 41 (2006) 202-212
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 202-212
    • Tamagno, E.1    Bardini, P.2    Guglielmotto, M.3    Danni, O.4    Tabaton, M.5
  • 30
    • 31544476561 scopus 로고    scopus 로고
    • Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
    • Zhao L., Ma Q.L., Calon F., Harris-White M.E., Yang F., Lim G.P., et al. Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease. Nature Neurosci. 9 (2006) 234-242
    • (2006) Nature Neurosci. , vol.9 , pp. 234-242
    • Zhao, L.1    Ma, Q.L.2    Calon, F.3    Harris-White, M.E.4    Yang, F.5    Lim, G.P.6
  • 31
    • 0036780877 scopus 로고    scopus 로고
    • Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning
    • Schenk D. Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning. Nature Rev. Neurosci. 3 (2002) 824-828
    • (2002) Nature Rev. Neurosci. , vol.3 , pp. 824-828
    • Schenk, D.1
  • 32
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D., Barbour R., Dunn W., Gordon G., Grajeda H., Guido T., et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400 (1999) 173-177
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 33
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C., Pearson J., McLaurin J., Mathews P.M., Jiang Y., Schmidt S.D., et al. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 408 (2000) 979-982
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3    Mathews, P.M.4    Jiang, Y.5    Schmidt, S.D.6
  • 34
    • 84984755327 scopus 로고    scopus 로고
    • A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan D., Diamond D.M., Gottschall P.E., Ugen K.E., Dickey C., Hardy J., et al. A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 408 (2000) 982-985
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1    Diamond, D.M.2    Gottschall, P.E.3    Ugen, K.E.4    Dickey, C.5    Hardy, J.6
  • 35
    • 0036127580 scopus 로고    scopus 로고
    • Set back to Alzheimer vaccine studies
    • Birmingham K., and Frantz S. Set back to Alzheimer vaccine studies. Nature Med. 8 (2002) 199-200
    • (2002) Nature Med. , vol.8 , pp. 199-200
    • Birmingham, K.1    Frantz, S.2
  • 36
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo J.M., Gilman S., Dartigues J.F., Laurent B., Puel M., Kirby L.C., et al. Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology 61 (2003) 46-54
    • (2003) Neurology , vol.61 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3    Laurent, B.4    Puel, M.5    Kirby, L.C.6
  • 38
    • 0037452779 scopus 로고    scopus 로고
    • Epitope and isotype specificities of antibodies to beta -amyloid peptide for protection against Alzheimer's disease-like neuropathology
    • Bard F., Barbour R., Cannon C., Carretto R., Fox M., Games D., et al. Epitope and isotype specificities of antibodies to beta -amyloid peptide for protection against Alzheimer's disease-like neuropathology. Proc. Natl Acad. Sci. USA 100 (2003) 2023-2028
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2023-2028
    • Bard, F.1    Barbour, R.2    Cannon, C.3    Carretto, R.4    Fox, M.5    Games, D.6
  • 39
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F., Cannon C., Barbour R., Burke R.L., Games D., Grajeda H., et al. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nature Med. 6 (2000) 916-919
    • (2000) Nature Med. , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5    Grajeda, H.6
  • 41
    • 2642578354 scopus 로고    scopus 로고
    • Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity
    • Liu R., Yuan B., Emadi S., Zameer A., Schulz P., McAllister C., et al. Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity. Biochemistry 43 (2004) 6959-6967
    • (2004) Biochemistry , vol.43 , pp. 6959-6967
    • Liu, R.1    Yuan, B.2    Emadi, S.3    Zameer, A.4    Schulz, P.5    McAllister, C.6
  • 42
    • 33749034211 scopus 로고    scopus 로고
    • Single chain Fv antibodies against the 25-35 Abeta fragment inhibit aggregation and toxicity of Abeta42
    • Zameer A., Schulz P., Wang M.S., and Sierks M.R. Single chain Fv antibodies against the 25-35 Abeta fragment inhibit aggregation and toxicity of Abeta42. Biochemistry 45 (2006) 11532-11539
    • (2006) Biochemistry , vol.45 , pp. 11532-11539
    • Zameer, A.1    Schulz, P.2    Wang, M.S.3    Sierks, M.R.4
  • 43
    • 33750291199 scopus 로고    scopus 로고
    • Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies
    • Barkhordarian H., Emadi S., Schulz P., and Sierks M.R. Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies. Protein Eng. Des. Sel. 19 (2006) 497-502
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 497-502
    • Barkhordarian, H.1    Emadi, S.2    Schulz, P.3    Sierks, M.R.4
  • 44
    • 34147130637 scopus 로고    scopus 로고
    • Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity
    • Emadi S., Barkhordarian H., Wang M.S., Schulz P., and Sierks M.R. Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity. J. Mol. Biol. 368 (2007) 1132-1144
    • (2007) J. Mol. Biol. , vol.368 , pp. 1132-1144
    • Emadi, S.1    Barkhordarian, H.2    Wang, M.S.3    Schulz, P.4    Sierks, M.R.5
  • 46
    • 33749507375 scopus 로고    scopus 로고
    • Conformation-dependent anti-amyloid oligomer antibodies
    • Kayed R., and Glabe C.G. Conformation-dependent anti-amyloid oligomer antibodies. Methods Enzymol. 413 (2006) 326-344
    • (2006) Methods Enzymol. , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 48
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 49
    • 0042822112 scopus 로고    scopus 로고
    • Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid
    • Butler A.E., Janson J., Soeller W.C., and Butler P.C. Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52 (2003) 2304-2314
    • (2003) Diabetes , vol.52 , pp. 2304-2314
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 51
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach N., Deechongkit S., Jiang X., Kelly J.W., and Buxbaum J.N. Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc. Natl Acad. Sci. USA 101 (2004) 2817-2822
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 52
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y., Chang L., Viola K.L., Lacor P.N., Lambert M.P., Finch C.E., et al. Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl Acad. Sci. USA 100 (2003) 10417-10422
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 53
    • 0242479694 scopus 로고    scopus 로고
    • Femtomole immunodetection of synthetic and endogenous amyloid-beta oligomers and its application to Alzheimer's disease drug candidate screening
    • Chang L., Bakhos L., Wang Z., Venton D.L., and Klein W.L. Femtomole immunodetection of synthetic and endogenous amyloid-beta oligomers and its application to Alzheimer's disease drug candidate screening. J. Mol. Neurosci. 20 (2003) 305-313
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 305-313
    • Chang, L.1    Bakhos, L.2    Wang, Z.3    Venton, D.L.4    Klein, W.L.5
  • 55
    • 0041332884 scopus 로고    scopus 로고
    • Evidence for peripheral clearance of cerebral Abeta protein following chronic, active Abeta immunization in PSAPP mice
    • Lemere C.A., Spooner E.T., LaFrancois J., Malester B., Mori C., Leverone J.F., et al. Evidence for peripheral clearance of cerebral Abeta protein following chronic, active Abeta immunization in PSAPP mice. Neurobiol. Dis. 14 (2003) 10-18
    • (2003) Neurobiol. Dis. , vol.14 , pp. 10-18
    • Lemere, C.A.1    Spooner, E.T.2    LaFrancois, J.3    Malester, B.4    Mori, C.5    Leverone, J.F.6
  • 56
    • 0141457897 scopus 로고    scopus 로고
    • Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice
    • Das P., Howard V., Loosbrock N., Dickson D., Murphy M.P., and Golde T.E. Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice. J. Neurosci. 23 (2003) 8532-8538
    • (2003) J. Neurosci. , vol.23 , pp. 8532-8538
    • Das, P.1    Howard, V.2    Loosbrock, N.3    Dickson, D.4    Murphy, M.P.5    Golde, T.E.6
  • 57
    • 13444283725 scopus 로고    scopus 로고
    • Efficacy of anti-Abeta antibody isotypes used for intracerebroventricular immunization in TgCRND8
    • Chauhan N.B., and Siegel G.J. Efficacy of anti-Abeta antibody isotypes used for intracerebroventricular immunization in TgCRND8. Neurosci. Lett. 375 (2005) 143-147
    • (2005) Neurosci. Lett. , vol.375 , pp. 143-147
    • Chauhan, N.B.1    Siegel, G.J.2
  • 58
    • 12444268257 scopus 로고    scopus 로고
    • Prototype Alzheimer's disease vaccine using the immunodominant B cell epitope from beta-amyloid and promiscuous T cell epitope pan HLA DR-binding peptide
    • Agadjanyan M.G., Ghochikyan A., Petrushina I., Vasilevko V., Movsesyan N., Mkrtichyan M., et al. Prototype Alzheimer's disease vaccine using the immunodominant B cell epitope from beta-amyloid and promiscuous T cell epitope pan HLA DR-binding peptide. J. Immunol. 174 (2005) 1580-1586
    • (2005) J. Immunol. , vol.174 , pp. 1580-1586
    • Agadjanyan, M.G.1    Ghochikyan, A.2    Petrushina, I.3    Vasilevko, V.4    Movsesyan, N.5    Mkrtichyan, M.6
  • 60
    • 4444362840 scopus 로고    scopus 로고
    • Current progress in beta-amyloid immunotherapy
    • Schenk D., Hagen M., and Seubert P. Current progress in beta-amyloid immunotherapy. Curr. Opin. Immunol. 16 (2004) 599-606
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 599-606
    • Schenk, D.1    Hagen, M.2    Seubert, P.3
  • 61
    • 0035993237 scopus 로고    scopus 로고
    • Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets
    • Klein W.L. Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem. Int. 41 (2002) 345-352
    • (2002) Neurochem. Int. , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 64
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine III H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine III, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.