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Volumn 335, Issue 1, 2004, Pages 81-90

Alzheimer's β-peptide oligomer formation at physiologic concentrations

Author keywords

Amyloid; Antibodies; ELISA; Gel permeation chromatography; Kinetics; Thermodynamics

Indexed keywords

ANTIBODIES; CHEMICAL DETECTION; CRITICAL MICELLE CONCENTRATION; DIMETHYL SULFOXIDE; DYES; ENZYME KINETICS; EPITOPES; GEL PERMEATION CHROMATOGRAPHY; IONIC STRENGTH; MICELLES; MOLECULAR WEIGHT; PEPTIDES; PHYSIOLOGY; POTASSIUM COMPOUNDS; SOAPS (DETERGENTS); SODIUM CHLORIDE; TEMPERATURE DISTRIBUTION; THERMODYNAMICS;

EID: 7444247272     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.08.014     Document Type: Article
Times cited : (110)

References (54)
  • 1
    • 7444257603 scopus 로고    scopus 로고
    • Soluble amyloid oligomers: A common cause of neurodegeneration?
    • K. Senior Soluble amyloid oligomers: a common cause of neurodegeneration? Lancet Neurol. 2 2003 330
    • (2003) Lancet Neurol. , vol.2 , pp. 330
    • Senior, K.1
  • 2
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • W.L. Klein, G.A. Krafft, and C.E. Finch Targeting small Abeta 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
  • 4
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in parkinson's disease
    • M.J. Volles, and P.T. Lansbury Jr. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in parkinson's disease Biochemistry 42 2003 7871 7878
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 8
    • 1542268242 scopus 로고    scopus 로고
    • Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function
    • D.A. Bennett, J.A. Schneider, R.S. Wilson, J.L. Bienias, and S.E. Arnold Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function Arch. Neurol. 61 2004 378 384
    • (2004) Arch. Neurol. , vol.61 , pp. 378-384
    • Bennett, D.A.1    Schneider, J.A.2    Wilson, R.S.3    Bienias, J.L.4    Arnold, S.E.5
  • 9
    • 0030735176 scopus 로고    scopus 로고
    • The mean Abeta load in the hippocampus correlates with duration and severity of dementia in subgroups of Alzheimer disease
    • G.T. Bartoo, D. Nochlin, D. Chang, Y. Kim, and S.M. Sumi The mean Abeta load in the hippocampus correlates with duration and severity of dementia in subgroups of Alzheimer disease J. Neuropathol. Exp. Neurol. 56 1997 531 540
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 531-540
    • Bartoo, G.T.1    Nochlin, D.2    Chang, D.3    Kim, Y.4    Sumi, S.M.5
  • 12
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging
    • J. Wang, D.W. Dickson, J.Q. Trojanowski, and V.M. Lee The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging Exp. Neurol. 158 1999 328 337
    • (1999) Exp. Neurol. , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 13
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • K.N. Dahlgren, A.M. Manelli, W.B. Stine Jr., L.K. Baker, G.A. Krafft, and M.J. LaDu Oligomeric and fibrillar species of amyloid-beta 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 Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 14
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • D.M. Hartley, D.M. Walsh, C.P. Ye, T. Diehl, S. Vasquez, P.M. Vassilev, D.B. Teplow, and D.J. Selkoe Protofibrillar intermediates of amyloid beta-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.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 16
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Abeta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Y. Gong, L. Chang, K.L. Viola, P.N. Lacor, M.P. Lambert, C.E. Finch, G.A. Krafft, and W.L. Klein Alzheimer's disease-affected brain: presence of oligomeric Abeta 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    Krafft, G.A.7    Klein, W.L.8
  • 17
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • B. O'Nuallain, and R. Wetzel Conformational Abs recognizing a generic amyloid fibril epitope Proc. Natl. Acad. Sci. USA 99 2002 1485 1490
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 20
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by congo red spectral shift assay
    • W.E. Klunk, R.F. Jacob, and R.P. Mason Quantifying amyloid by congo red spectral shift assay Methods Enzymol. 309 1999 285 305
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 21
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • H. LeVine III Quantification of beta-sheet amyloid fibril structures with thioflavin T Methods Enzymol. 309 1999 274 284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 22
    • 0028832472 scopus 로고
    • Soluble multimeric Alzheimer beta(1-40) pre-amyloid complexes in dilute solution
    • H. LeVine III Soluble multimeric Alzheimer beta(1-40) pre-amyloid complexes in dilute solution Neurobiol. Aging 16 1995 755 764
    • (1995) Neurobiol. Aging , vol.16 , pp. 755-764
    • LeVine III, H.1
  • 24
    • 0028298620 scopus 로고
    • Transglutaminase facilitates the formation of polymers of the beta-amyloid peptide
    • S.M. Dudek, and G.V. Johnson Transglutaminase facilitates the formation of polymers of the beta-amyloid peptide Brain Res. 651 1994 129 133
    • (1994) Brain Res. , vol.651 , pp. 129-133
    • Dudek, S.M.1    Johnson, G.V.2
  • 25
    • 0034647786 scopus 로고    scopus 로고
    • Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease
    • O.M. El Agnaf, D.S. Mahil, B.P. Patel, and B.M. Austen Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease Biochem. Biophys. Res. Commun. 273 2000 1003 1007
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 1003-1007
    • El Agnaf, O.M.1    Mahil, D.S.2    Patel, B.P.3    Austen, B.M.4
  • 26
    • 0030778396 scopus 로고    scopus 로고
    • Hemin and related porphyrins inhibit beta-amyloid aggregation
    • D. Howlett, P. Cutler, S. Heales, and P. Camilleri Hemin and related porphyrins inhibit beta-amyloid aggregation FEBS Lett. 417 1997 249 251
    • (1997) FEBS Lett. , vol.417 , pp. 249-251
    • Howlett, D.1    Cutler, P.2    Heales, S.3    Camilleri, P.4
  • 28
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and dissociation using surface plasmon resonance
    • K. Hasegawa, K. Ono, M. Yamada, and H. Naiki Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and dissociation using surface plasmon resonance Biochemistry 41 2002 13489 13498
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 29
    • 0033955085 scopus 로고    scopus 로고
    • A stable and highly sensitive 3,3′,5,5′-tetramethylbenzidine- based substrate reagent for enzyme-linked immunosorbent assays
    • A. Frey, B. Meckelein, D. Externest, and M.A. Schmidt A stable and highly sensitive 3,3′,5,5′-tetramethylbenzidine-based substrate reagent for enzyme-linked immunosorbent assays J. Immunol. Methods 233 2000 47 56
    • (2000) J. Immunol. Methods , vol.233 , pp. 47-56
    • Frey, A.1    Meckelein, B.2    Externest, D.3    Schmidt, M.A.4
  • 30
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • G. Bitan, A. Lomakin, and D.B. Teplow Amyloid beta-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
  • 31
    • 0033975837 scopus 로고    scopus 로고
    • Plasma and cerebrospinal fluid levels of amyloid beta proteins 1-40 and 1-42 in Alzheimer disease
    • P.D. Mehta, T. Pirttila, S.P. Mehta, E.A. Sersen, P.S. Aisen, and H.M. Wisniewski Plasma and cerebrospinal fluid levels of amyloid beta proteins 1-40 and 1-42 in Alzheimer disease Arch. Neurol. 57 2000 100 105
    • (2000) Arch. Neurol. , vol.57 , pp. 100-105
    • Mehta, P.D.1    Pirttila, T.2    Mehta, S.P.3    Sersen, E.A.4    Aisen, P.S.5    Wisniewski, H.M.6
  • 34
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants
    • A. Lomakin, D.S. Chung, G.B. Benedek, D.A. Kirschner, and D.B. Teplow On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants Proc. Natl. Acad. Sci. USA 93 1996 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
  • 35
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • J.T. Jarrett, E.P. Berger, and P.T. Lansbury Jr. The carboxy terminus of the beta 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
  • 36
    • 0021527508 scopus 로고
    • Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway
    • M.F. Bishop, and F.A. Ferrone Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway Biophys. J. 46 1984 631 644
    • (1984) Biophys. J. , vol.46 , pp. 631-644
    • Bishop, M.F.1    Ferrone, F.A.2
  • 37
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation
    • A.J. Modler, K. Gast, G. Lutsch, and G. Damaschun Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation J. Mol. Biol. 325 2003 135 148
    • (2003) J. Mol. Biol. , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 39
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis
    • M.D. Kirkitadze, M.M. Condron, and D.B. Teplow Identification and characterization of key kinetic intermediates in amyloid beta-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
  • 41
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • M. Pitschke, R. Prior, M. Haupt, and D. Riesner Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy Nat. Med. 4 1998 832 834 (see comments)
    • (1998) Nat. Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 43
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh, I. Klyubin, J.V. Fadeeva, W.K. Cullen, R. Anwyl, M.S. Wolfe, M.J. Rowan, and D.J. Selkoe 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    Rowan, M.J.7    Selkoe, D.J.8
  • 44
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • D.M. Walsh, A. Lomakin, G.B. Benedek, M.M. Condron, and D.B. Teplow Amyloid beta-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
  • 45
    • 0030611858 scopus 로고    scopus 로고
    • Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations
    • W. Garzon-Rodriguez, M. Sepulveda-Becerra, S. Milton, and C.G. Glabe Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations J. Biol. Chem. 272 1997 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
  • 46
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores
    • H.A. Lashuel, D.M. Hartley, B.M. Petre, J.S. Wall, M.N. Simon, T. Walz, and P.T. Lansbury Jr. Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores J. Mol. Biol. 332 2003 795 808
    • (2003) J. Mol. Biol. , vol.332 , pp. 795-808
    • Lashuel, H.A.1    Hartley, D.M.2    Petre, B.M.3    Wall, J.S.4    Simon, M.N.5    Walz, T.6    Lansbury Jr., P.T.7
  • 47
    • 0033830819 scopus 로고    scopus 로고
    • Scope, limitations and mechanistic aspects of the photo-induced cross-linking of proteins by water-soluble metal complexes
    • D.A. Fancy, C. Denison, K. Kim, Y. Xie, T. Holdeman, F. Amini, and T. Kodadek 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.4    Holdeman, T.5    Amini, F.6    Kodadek, T.7
  • 48
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • D.A. Fancy, and T. Kodadek Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light Proc. Natl. Acad. Sci. USA 96 1999 6020 6024
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 50
    • 0142227240 scopus 로고    scopus 로고
    • Nucleation-elongation: A mechanism for cooperative supramolecular polymerization
    • D. Zhao, and J.S. Moore Nucleation-elongation: a mechanism for cooperative supramolecular polymerization Org. Biomol. Chem. 1 2003 3471 3491
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3471-3491
    • Zhao, D.1    Moore, J.S.2
  • 51
    • 0346434111 scopus 로고    scopus 로고
    • Nucleation-elongation polymerization under imbalanced stoichiometry
    • D. Zhao, and J.S. Moore Nucleation-elongation polymerization under imbalanced stoichiometry J. Am. Chem. Soc. 125 2003 16294 16299
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16294-16299
    • Zhao, D.1    Moore, J.S.2
  • 52
    • 0035907123 scopus 로고    scopus 로고
    • Amyloid beta protein 1-40 and 1-42 levels in matched cerebrospinal fluid and plasma from patients with Alzheimer disease
    • P.D. Mehta, T. Pirttila, B.A. Patrick, M. Barshatzky, and S.P. Mehta Amyloid beta protein 1-40 and 1-42 levels in matched cerebrospinal fluid and plasma from patients with Alzheimer disease Neurosci. Lett. 304 2001 102 106
    • (2001) Neurosci. Lett. , vol.304 , pp. 102-106
    • Mehta, P.D.1    Pirttila, T.2    Patrick, B.A.3    Barshatzky, M.4    Mehta, S.P.5
  • 54
    • 0242412140 scopus 로고    scopus 로고
    • Plasma Abeta40 and Abeta42 and Alzheimer's disease: Relation to age, mortality, and risk
    • R. Mayeux, L.S. Honig, M.X. Tang, J. Manly, Y. Stern, N. Schupf, and P.D. Mehta Plasma Abeta40 and Abeta42 and Alzheimer's disease: relation to age, mortality, and risk Neurology 61 2003 1185 1190
    • (2003) Neurology , vol.61 , pp. 1185-1190
    • Mayeux, R.1    Honig, L.S.2    Tang, M.X.3    Manly, J.4    Stern, Y.5    Schupf, N.6    Mehta, P.D.7


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