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Volumn 25, Issue 5, 2004, Pages 569-580

Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease

Author keywords

ADDLs; Alzheimer's disease; Amyloid; Amyloid protein; Neurotoxicity; Oligomers; Paranucleus; Protofibril

Indexed keywords

AMYLOID BETA PROTEIN; BRAIN PROTEIN; NEUROTOXIN;

EID: 2542455537     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2004.02.010     Document Type: Article
Times cited : (432)

References (78)
  • 1
    • 0034659732 scopus 로고    scopus 로고
    • Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: Maintenance of core components independent of actin filaments and microtubules
    • Allison D.W., Chervin A.S., Gelfand V.I., Craig A.M. Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: maintenance of core components independent of actin filaments and microtubules. J. Neurosci. 20:2000;4545-4554
    • (2000) J. Neurosci. , vol.20 , pp. 4545-4554
    • Allison, D.W.1    Chervin, A.S.2    Gelfand, V.I.3    Craig, A.M.4
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation
    • Barnham K.J., Ciccotosto G.D., Tickler A.K., Ali F.E., Smith D.G., Williamson N.A., et al. Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 278:2003;42959-42965
    • (2003) J. Biol. Chem. , vol.278 , pp. 42959-42965
    • Barnham, K.J.1    Ciccotosto, G.D.2    Tickler, A.K.3    Ali, F.E.4    Smith, D.G.5    Williamson, N.A.6
  • 4
    • 0036281493 scopus 로고    scopus 로고
    • Synapse loss is greater in presenile than senile onset Alzheimer disease: Implications for the cognitive reserve hypothesis
    • Bigio E.H., Hynan L.S., Sontag E., Satumtira S., White C.L. Synapse loss is greater in presenile than senile onset Alzheimer disease: implications for the cognitive reserve hypothesis. Neuropathol. Appl. Neurobiol. 28:2002;218-227
    • (2002) Neuropathol. Appl. Neurobiol. , vol.28 , pp. 218-227
    • Bigio, E.H.1    Hynan, L.S.2    Sontag, E.3    Satumtira, S.4    White, C.L.5
  • 6
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid β-protein oligomerization - Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan G., Lomakin A., Teplow D.B. Amyloid β-protein oligomerization - prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276:2001;35176-35184
    • (2001) J. Biol. Chem. , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 8
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid β-protein oligomerization
    • Bitan G., Vollers S.S., Teplow D.B. Elucidation of primary structure elements controlling early amyloid β-protein oligomerization. J. Biol. Chem. 278:2003;34882-34889
    • (2003) J. Biol. Chem. , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 10
    • 0242479694 scopus 로고    scopus 로고
    • Femtomole immunodetection of synthetic and endogenous amyloid-β oligomers and its application to Alzheimer's disease drug candidate screening
    • Chang L., Bakhos L., Wang Z.Q., Venton D.L., Klein W.L. Femtomole immunodetection of synthetic and endogenous amyloid-β 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.Q.3    Venton, D.L.4    Klein, W.L.5
  • 12
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • Chui D.H., Tanahashi H., Ozawa K., Ikeda S., Checler F., Ueda O., et al. Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation. Nat. Med. 5:1999;560-564
    • (1999) Nat. Med. , vol.5 , pp. 560-564
    • Chui, D.H.1    Tanahashi, H.2    Ozawa, K.3    Ikeda, S.4    Checler, F.5    Ueda, O.6
  • 13
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., Lansbury P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. U.S.A. 97:2000;571-576
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 14
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren K.N., Manelli A.M., Stine W.B., Baker L.K., Krafft G.A., LaDu M.J. Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J. Biol. Chem. 277:2002;32046-32053
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 15
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Aβ 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 Aβ burden in Alzheimer's disease model. Nat. Neurosci. 5:2002;452-457
    • (2002) Nat. 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
  • 16
    • 0033830819 scopus 로고    scopus 로고
    • Scope, limitations and mechanistic aspects of the photo-induced cross-linking of proteins by water-soluble metal complexes
    • Fancy D.A., Denison C., Kim K., Xie Y.Q., Holdeman T., Amini F., et al. Scope, limitations and mechanistic aspects of the photo-induced cross-linking of proteins by water-soluble metal complexes. Chem. Biol. 7:2000;697-708
    • (2000) Chem. Biol. , vol.7 , pp. 697-708
    • Fancy, D.A.1    Denison, C.2    Kim, K.3    Xie, Y.Q.4    Holdeman, T.5    Amini, F.6
  • 17
    • 2542461788 scopus 로고    scopus 로고
    • Differential effects of oligomeric amyloid-β on synaptic plasticity in human apoE targeted replacement mice
    • Gamkrelidze G, Shah C, Yun SH, Pasternak JF, Stine B, Manelli A. Differential effects of oligomeric amyloid-β on synaptic plasticity in human apoE targeted replacement mice. Soc Neurosci Abstr 2003;29:945.17.
    • (2003) Soc Neurosci Abstr , vol.29 , pp. 94517
    • Gamkrelidze, G.1    Shah, C.2    Yun, S.H.3    Pasternak, J.F.4    Stine, B.5    Manelli, A.6
  • 18
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβ 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 Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. U.S.A. 100:2003;10417-10422
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 19
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • Grabowski T.J., Cho H.S., Vonsattel J.P.G., Rebeck G.W., Greenberg S.M. Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann. Neurol. 49:2001;697-705
    • (2001) Ann. Neurol. , vol.49 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.G.3    Rebeck, G.W.4    Greenberg, S.M.5
  • 20
    • 0036200702 scopus 로고    scopus 로고
    • Insights into immediate-early gene function in hippocampal memory consolidation using antisense oligonucleotide and fluorescent imaging approaches
    • Guzowski J.F. Insights into immediate-early gene function in hippocampal memory consolidation using antisense oligonucleotide and fluorescent imaging approaches. Hippocampus. 12:2002;86-104
    • (2002) Hippocampus , vol.12 , pp. 86-104
    • Guzowski, J.F.1
  • 21
    • 0034869176 scopus 로고    scopus 로고
    • Protofibrils, the unifying toxic molecule of neurodegenerative disorders?
    • Haass C., Steiner H. Protofibrils, the unifying toxic molecule of neurodegenerative disorders? Nat. Neurosci. 4:2001;859-860
    • (2001) Nat. Neurosci. , vol.4 , pp. 859-860
    • Haass, C.1    Steiner, H.2
  • 22
    • 0037135111 scopus 로고    scopus 로고
    • Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. Medicine - 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
  • 23
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4:1997;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
  • 24
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D.M., Walsh D.M., Ye C.P.P., Diehl T., Vasquez S., Vassilev P.M., et al. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19:1999;8876-8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6
  • 25
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β
    • Hoshi M., Sato M., Matsumoto S., Noguchi A., Yasutake K., Yoshida N., et al. Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β Proc. Natl. Acad. Sci. U.S.A. 100:2003;6370-6375
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5    Yoshida, N.6
  • 27
    • 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 J.T., Berger E.P., Lansbury P.T. Jr. 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. 32:1993;4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 28
    • 0346026775 scopus 로고    scopus 로고
    • Oxidation induced changes of β-amyloid peptide fibrillization rate - Possible implications for Alzheimer's disease
    • Johansson A.-S., Päiviö A., Lannfelt L., Westlind-Danielsson A. Oxidation induced changes of β-amyloid peptide fibrillization rate - possible implications for Alzheimer's disease. Neurobiol. Aging. 23:2002;S187
    • (2002) Neurobiol. Aging , vol.23 , pp. 187
    • Johansson, A.-S.1    Päiviö, A.2    Lannfelt, L.3    Westlind-Danielsson, A.4
  • 29
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 300:2003;486-489
    • (2003) Science , vol.300 , 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
  • 30
    • 0041342036 scopus 로고    scopus 로고
    • Experience-dependent regulation of the immediate-early gene Arc differs across brain regions
    • Kelly M.P., Deadwyler S.A. Experience-dependent regulation of the immediate-early gene Arc differs across brain regions. J. Neurosci. 23:2003;6443-6451
    • (2003) J. Neurosci. , vol.23 , pp. 6443-6451
    • Kelly, M.P.1    Deadwyler, S.A.2
  • 31
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
    • Kirkitadze M.D., Condron M.M., Teplow D.B. Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis. J. Mol. Biol. 312:2001;1103-1119
    • (2001) J. Mol. Biol. , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 32
    • 0002665739 scopus 로고    scopus 로고
    • Aβ toxicity in Alzheimer's disease
    • Chesselet MF, editor. Totowa, NJ: Humana Press;
    • Klein WL. Aβ toxicity in Alzheimer's disease. In: Chesselet MF, editor. Molecular mechanisms of neurodegenerative diseases. Totowa, NJ: Humana Press; 2000. p. 1-49.
    • (2000) Molecular Mechanisms of Neurodegenerative Diseases , pp. 1-49
    • Klein, W.L.1
  • 33
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein W.L., Krafft G.A., Finch C.E. Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24:2001;219-224
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 39
    • 0034740197 scopus 로고    scopus 로고
    • Vaccination with soluble Aβ oligomers generates toxicity- neutralizing antibodies
    • Lambert M.P., Viola K.L., Chromy B.A., Chang L., Morgan T.E., Yu J.X., et al. Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies. J. Neurochem. 79:2001;595-605
    • (2001) J. Neurochem. , vol.79 , pp. 595-605
    • Lambert, M.P.1    Viola, K.L.2    Chromy, B.A.3    Chang, L.4    Morgan, T.E.5    Yu, J.X.6
  • 40
    • 0032830123 scopus 로고    scopus 로고
    • Monitoring protein assembly using quasielastic light scattering spectroscopy
    • Lomakin A., Benedek G.B., Teplow D.B. Monitoring protein assembly using quasielastic light scattering spectroscopy. Methods Enzymol. 309:1999;429-459
    • (1999) Methods Enzymol. , vol.309 , pp. 429-459
    • Lomakin, A.1    Benedek, G.B.2    Teplow, D.B.3
  • 41
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue L.F., Kuo Y.M., Roher A.E., Brachova L., Shen Y., Sue L., et al. Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 155:1999;853-862
    • (1999) Am. J. Pathol. , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3    Brachova, L.4    Shen, Y.5    Sue, L.6
  • 43
    • 2542430828 scopus 로고    scopus 로고
    • ApoE and Aβ1-42 interactions: Effects of isoform and conformation on structure and function
    • in press.
    • Manelli AM, Stine Jr WB, Van Eldik LJ, LaDu MJ. ApoE and Aβ1-42 interactions: effects of isoform and conformation on structure and function. J Mol Neurosci 2004, in press.
    • (2004) J Mol Neurosci
    • Manelli, A.M.1    Stine Jr., W.B.2    Van Eldik, L.J.3    LaDu, M.J.4
  • 44
    • 2542458968 scopus 로고    scopus 로고
    • Aβ1-42 induced neurotoxicity in cells co-cultured with glia from apoE targeted replacement mice
    • Manelli AM, Sullivan PM, LaDu MJ. Aβ1-42 induced neurotoxicity in cells co-cultured with glia from apoE targeted replacement mice. Soc Neurosci Abstr 2003;29:407-18.
    • (2003) Soc Neurosci Abstr , vol.29 , pp. 407-418
    • Manelli, A.M.1    Sullivan, P.M.2    LaDu, M.J.3
  • 45
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ 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 Aβ 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
  • 46
    • 84984755327 scopus 로고    scopus 로고
    • Aβ 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. Aβ 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
  • 47
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of Aβ(1-42) in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke L., Masliah E., Yu G.Q., Mallory M., Rockenstein E.M., Tatsuno G., et al. High-level neuronal expression of Aβ(1-42) in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J. Neurosci. 20:2000;4050-4058
    • (2000) J. Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6
  • 48
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • Näslund J., Haroutunian V., Mohs R., Davis K.L., Davies P., Greengard P., et al. Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA. 283:2000;1571-1577
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Näslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6
  • 51
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • Oddo S., Caccamo A., Shepherd J.D., Murphy M.P., Golde T.E., Kayed R., et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction. Neuron. 39:2003;409-421
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6
  • 52
    • 0037205434 scopus 로고    scopus 로고
    • Oxidation of methionine 35 attenuates formation of amyloid β-peptide 1-40 oligomers
    • Palmblad M., Westlind-Danielsson A., Bergquist J. Oxidation of methionine 35 attenuates formation of amyloid β-peptide 1-40 oligomers. J. Biol. Chem. 277:2002;19506-19510
    • (2002) J. Biol. Chem. , vol.277 , pp. 19506-19510
    • Palmblad, M.1    Westlind-Danielsson, A.2    Bergquist, J.3
  • 53
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., Cotman C.W. Neurodegeneration induced by β-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
  • 54
    • 0036592640 scopus 로고    scopus 로고
    • Apolipoprotein e and Alzheimer's disease: The protective effects of ApoE2 and E3
    • Rebeck G.W., Kindy M., LaDu M.J. Apolipoprotein E and Alzheimer's disease: the protective effects of ApoE2 and E3. J. Alzheimers Dis. 4:2002;145-154
    • (2002) J. Alzheimers Dis. , vol.4 , pp. 145-154
    • Rebeck, G.W.1    Kindy, M.2    Ladu, M.J.3
  • 57
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Aβ(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 Aβ(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
  • 58
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β 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-β 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
  • 59
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe D.J. Alzheimer's disease is a synaptic failure. Science. 298:2002;789-791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 60
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science. 289:2000;1317-1321
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 62
    • 0032235398 scopus 로고    scopus 로고
    • The Sixth International Conference on Alzheimer's disease, Amsterdam, the Netherlands, July 1998. The amyloid cascade hypothesis debate: Emerging consensus on the role of Aβ and amyloid in Alzheimer's disease
    • Small D.H. The Sixth International Conference on Alzheimer's disease, Amsterdam, The Netherlands, July 1998. The amyloid cascade hypothesis debate: emerging consensus on the role of Aβ and amyloid in Alzheimer's disease. Amyloid. 5:1998;301-304
    • (1998) Amyloid , vol.5 , pp. 301-304
    • Small, D.H.1
  • 63
    • 0028168336 scopus 로고
    • Amyloid-β aggregation: Selective inhibition of aggregation in mixtures of amyloid with different chain lengths
    • Snyder S.W., Ladror U.S., Wade W.S., Wang G.T., Barrett L.W., Matayoshi E.D., et al. Amyloid-β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J. 67:1994;1216-1228
    • (1994) Biophys. J. , vol.67 , pp. 1216-1228
    • Snyder, S.W.1    Ladror, U.S.2    Wade, W.S.3    Wang, G.T.4    Barrett, L.W.5    Matayoshi, E.D.6
  • 64
    • 0028971326 scopus 로고
    • Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure
    • Soto C., Castaño E.M., Kumar R.A., Beavis R.C., Frangione B. Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure. Neurosci. Lett. 200:1995;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
  • 65
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine W.B., Dahlgren K.N., Krafft G.A., LaDu M.J. In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J. Biol. Chem. 278:2003;11612-11622
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    Ladu, M.J.4
  • 68
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid β-protein fibrillogenesis
    • Teplow D.B. Structural and kinetic features of amyloid β-protein fibrillogenesis. Amyloid: Int. J. Exp. Clin. Invest. 5:1998;121-142
    • (1998) Amyloid: Int. J. Exp. Clin. Invest. , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 69
    • 0002395242 scopus 로고    scopus 로고
    • Effects of β-protein mutations on amyloid fibril nucleation and elongation
    • Iqbal K, Winblad B, Nishimura T, Takeda M, Wisniewski HM, editors. Chichester, UK: John Wiley & Sons Ltd.;
    • Teplow DB, Lomakin A, Benedek GB, Kirschner DA, Walsh DM. Effects of β-protein mutations on amyloid fibril nucleation and elongation. In: Iqbal K, Winblad B, Nishimura T, Takeda M, Wisniewski HM, editors. Alzheimer's disease: biology, diagnosis and therapeutics. Chichester, UK: John Wiley & Sons Ltd.; 1997. p. 311-9.
    • (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
  • 70
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(25-35)
    • Varadarajan S., Kanski J., Aksenova M., Lauderback C., Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(25-35). J. Am. Chem. Soc. 123:2001;5625-5631
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 71
    • 0033860372 scopus 로고    scopus 로고
    • Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity. J. Struct. Biol. 130:2000;184-208
    • (2000) J. Struct. Biol. , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 73
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis - Structure and biological activity of protofibrillar intermediates
    • Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A., et al. Amyloid β-protein fibrillogenesis - structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274:1999;25945-25952
    • (1999) J. Biol. Chem. , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 74
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β 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 β 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
  • 75
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis - Detection of a protofibrillar intermediate
    • Walsh D.M., Lomakin A., Benedek G.B., Condron M.M., Teplow D.B. Amyloid β-protein fibrillogenesis - detection of a protofibrillar intermediate. J. Biol. Chem. 272:1997;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
  • 76
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • Wang H.W., Pasternak J.F., Kuo H., Ristic H., Lambert M.P., Chromy B., et al. Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res. 924:2002;133-140
    • (2002) Brain Res. , vol.924 , pp. 133-140
    • Wang, H.W.1    Pasternak, J.F.2    Kuo, H.3    Ristic, H.4    Lambert, M.P.5    Chromy, B.6
  • 78
    • 0035846576 scopus 로고    scopus 로고
    • Spontaneous in vitro formation of supramolecular β-amyloid structures, "βamyballs", by β-amyloid 1-40 peptide
    • Westlind-Danielsson A., Arnerup G. Spontaneous in vitro formation of supramolecular β-amyloid structures, "βamyballs", by β-amyloid 1-40 peptide. Biochemistry. 40:2001;14736-14743
    • (2001) Biochemistry , vol.40 , pp. 14736-14743
    • Westlind-Danielsson, A.1    Arnerup, G.2


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