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Volumn 28, Issue 4, 2012, Pages 735-758

Methods for analysis of amyloid-β aggregates

Author keywords

ADDL; Alzheimer's disease; amyloid ; fibrils; immunoassay; microscopy; oligomers; separation techniques; spectroscopy; spectrum analysis; structural analysis

Indexed keywords

AMYLOID BETA PROTEIN ANTIBODY; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; CONGO RED; OLIGOMER; QUANTUM DOT; THIOFLAVINE;

EID: 84863393423     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-2011-111421     Document Type: Review
Times cited : (63)

References (180)
  • 1
    • 13444293174 scopus 로고    scopus 로고
    • Defining molecular targets to prevent Alzheimer disease
    • Selkoe DJ (2005) Defining molecular targets to prevent Alzheimer disease. Arch Neurol 62, 192-195.
    • (2005) Arch Neurol , vol.62 , pp. 192-195
    • Selkoe, D.J.1
  • 2
    • 77949336151 scopus 로고    scopus 로고
    • 2010 Alzheimer's disease facts and figures
    • Alzheimer's Association
    • Alzheimer's Association (2010) 2010 Alzheimer's disease facts and figures. Alzheimers Dement 6, 158-194.
    • (2010) Alzheimers Dement , vol.6 , pp. 158-194
  • 3
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • Selkoe DJ (2004) Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 6, 1054-1061.
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 5
    • 33747652958 scopus 로고    scopus 로고
    • Distinct early folding and aggregation properties of Alzheimer amyloid-beta peptides Abeta40 and Abeta42: Stable trimer or tetramer formation by Abeta42
    • Chen YR, Glabe CG (2006) Distinct early folding and aggregation properties of Alzheimer amyloid-beta peptides Abeta40 and Abeta42: Stable trimer or tetramer formation by Abeta42. J Biol Chem 281, 24414-24422.
    • (2006) J Biol Chem , vol.281 , pp. 24414-24422
    • Chen, Y.R.1    Glabe, C.G.2
  • 7
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe JD, Cohen AS (2000) Review: History of the amyloid fibril. J Struct Biol 130, 88-98.
    • (2000) J Struct Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 8
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • DOI 10.1074/jbc.M210207200
    • Stine WB Jr, Dahlgren KN, Krafft GA, LaDu MJ (2003) In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem 278, 11612-11622. (Pubitemid 36792723)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 9
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283, 29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 10
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Abeta oligomers
    • Sakono M, Zako T (2010) Amyloid oligomers: Formation and toxicity of Abeta oligomers. FEBS J 277, 1348-1358.
    • (2010) FEBS J , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 11
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8, 101-112. (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 12
  • 13
    • 45249102680 scopus 로고    scopus 로고
    • Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders
    • DOI 10.2174/156720508784533358
    • Rahimi F, Shanmugam A, Bitan G (2008) Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Curr Alzheimer Res 5, 319-341. (Pubitemid 351840280)
    • (2008) Current Alzheimer Research , vol.5 , Issue.3 , pp. 319-341
    • Rahimi, F.1    Shanmugam, A.2    Bitan, G.3
  • 15
    • 77956698237 scopus 로고    scopus 로고
    • Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research
    • Jan A, Hartley DM, Lashuel HA (2010) Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research. Nat Protoc 5, 1186-1209.
    • (2010) Nat Protoc , vol.5 , pp. 1186-1209
    • Jan, A.1    Hartley, D.M.2    Lashuel, H.A.3
  • 18
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid
    • DOI 10.1038/nsmb1345, PII NSMB1345
    • Chimon S, Shaibat MA, Jones CR, Calero DC, Aizezi B, Ishii Y (2007) Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid. Nat Struct Mol Biol 14, 1157-1164. (Pubitemid 350223342)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 19
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small A beta oligomers: The solution to an Alzheimer's disease conundrum?
    • DOI 10.1016/S0166-2236(00)01749-5, PII S0166223600017495
    • Klein WL, Krafft GA, Finch CE (2001) Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum? Trends Neurosci 24, 219-224. (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
  • 23
    • 15944363809 scopus 로고    scopus 로고
    • The contribution of microscopy to the study of Alzheimer's disease, amyloid plaques and Abeta fibrillogenesis
    • Harris JR (2005) The contribution of microscopy to the study of Alzheimer's disease, amyloid plaques and Abeta fibrillogenesis. Subcell Biochem 38, 1-44.
    • (2005) Subcell Biochem , vol.38 , pp. 1-44
    • Harris, J.R.1
  • 24
    • 0014098295 scopus 로고
    • High-resolution electron microscopic analysis of the amyloid fibril
    • Shirahama T, Cohen AS (1967) High-resolution electron microscopic analysis of the amyloid fibril. J Cell Biol 33, 679-708.
    • (1967) J Cell Biol , vol.33 , pp. 679-708
    • Shirahama, T.1    Cohen, A.S.2
  • 25
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • DOI 10.1074/jbc.272.35.22364
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB (1997) Amyloid beta-protein fibrillogenesis Detection of a protofibrillar intermediate. J Biol Chem 272, 22364-22372. (Pubitemid 27382873)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 26
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of a beta 1-40: Implications for the search for a beta fibril formation inhibitors
    • Goldsbury CS, Wirtz S, Muller SA, Sunderji S, Wicki P, Aebi U, Frey P (2000) Studies on the in vitro assembly of a beta 1-40: Implications for the search for a beta fibril formation inhibitors. J Struct Biol 130, 217-231.
    • (2000) J Struct Biol , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.2    Muller, S.A.3    Sunderji, S.4    Wicki, P.5    Aebi, U.6    Frey, P.7
  • 27
    • 0842307665 scopus 로고    scopus 로고
    • Amyloidosis of Alzheimer's Abeta peptides: Solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
    • Antzutkin ON (2004) Amyloidosis of Alzheimer's Abeta peptides: Solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies. Magn Reson Chem 42, 231-246.
    • (2004) Magn Reson Chem , vol.42 , pp. 231-246
    • Antzutkin, O.N.1
  • 28
    • 75749131596 scopus 로고    scopus 로고
    • Introduction to atomic force microscopy (AFM) in biology
    • Chapter 17, Unit 17.7
    • Goldsbury CS, Scheuring S, Kreplak L (2009) Introduction to atomic force microscopy (AFM) in biology. Curr Protoc Protein Sci Chapter 17, Unit 17.7, 1-19.
    • (2009) Curr Protoc Protein Sci , pp. 1-19
    • Goldsbury, C.S.1    Scheuring, S.2    Kreplak, L.3
  • 31
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: Genes, proteins, and therapy. Physiol Rev 81, 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 32
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353-356. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 33
    • 33747182874 scopus 로고    scopus 로고
    • Ex situ atomic force microscopy analysis of beta-amyloid self-assembly and deposition on a synthetic template
    • DOI 10.1021/la0601511
    • Ha C, Park CB (2006) Ex situ atomic force microscopy analysis of beta-amyloid self-assembly and deposition on a synthetic template. Langmuir 22, 6977-6985. (Pubitemid 44231442)
    • (2006) Langmuir , vol.22 , Issue.16 , pp. 6977-6985
    • Ha, C.1    Park, C.B.2
  • 34
    • 18044401691 scopus 로고    scopus 로고
    • Visualizing the growth of Alzheimer's A beta amyloid-like fibrils
    • Goldsbury C, Aebi U, Frey P (2001) Visualizing the growth of Alzheimer's A beta amyloid-like fibrils. Trends Mol Med 7, 582.
    • (2001) Trends Mol Med , vol.7 , pp. 582
    • Goldsbury, C.1    Aebi, U.2    Frey, P.3
  • 35
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • Harper JD, Wong SS, Lieber CM, Lansbury PT Jr (1999) Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease. Biochemistry 38, 8972-8980.
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 36
    • 0037168446 scopus 로고    scopus 로고
    • Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance
    • DOI 10.1021/bi0204185
    • Antzutkin ON, Leapman RD, Balbach JJ, Tycko R (2002) Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41, 15436-15450. (Pubitemid 36008156)
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15436-15450
    • Antzutkin, O.N.1    Leapman, R.D.2    Balbach, J.J.3    Tycko, R.4
  • 38
    • 25844493112 scopus 로고    scopus 로고
    • Capturing intermediate structures of Alzheimer's beta-amyloid, Abeta(1-40), by solid-state NMR spectroscopy
    • DOI 10.1021/ja054039l
    • Chimon S, Ishii Y (2005) Capturing intermediate structures of Alzheimer's beta-amyloid, Abeta(1-40), by solid-state NMR spectroscopy. J Am Chem Soc 127, 13472-13473. (Pubitemid 41401181)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.39 , pp. 13472-13473
    • Chimon, S.1    Ishii, Y.2
  • 39
    • 27644527691 scopus 로고    scopus 로고
    • Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR
    • DOI 10.1016/j.bmc.2005.07.071, PII S096808960500725X
    • Masuda Y, Irie K, Murakami K, Ohigashi H, Ohashi R, Takegoshi K, Shimizu T, Shirasawa T (2005) Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR. Bioorg Med Chem 13, 6803-6809. (Pubitemid 41571226)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.24 , pp. 6803-6809
    • Masuda, Y.1    Irie, K.2    Murakami, K.3    Ohigashi, H.4    Ohashi, R.5    Takegoshi, K.6    Shimizu, T.7    Shirasawa, T.8
  • 40
    • 0027379395 scopus 로고
    • Characterization of beta-amyloid peptide from human cerebrospinal fluid
    • DOI 10.1111/j.1471-4159.1993.tb09841.x
    • Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I, Schenk DB (1993) Characterization of beta-amyloid peptide from human cerebrospinal fluid. J Neurochem 61, 1965-1968. (Pubitemid 23317227)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.5 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 41
    • 71449105844 scopus 로고    scopus 로고
    • Structural characterization of beta-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy
    • Ionut IM, Cozma C, Tomczyk N, Rontree J, Desor M, Drescher M, Przybylski M (2009) Structural characterization of beta-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy. Anal Bioanal Chem 395, 2509-2519.
    • (2009) Anal Bioanal Chem , vol.395 , pp. 2509-2519
    • Ionut, I.M.1    Cozma, C.2    Tomczyk, N.3    Rontree, J.4    Desor, M.5    Drescher, M.6    Przybylski, M.7
  • 42
    • 0026708694 scopus 로고
    • Kinetics of aggregation of synthetic beta-amyloid peptide
    • Tomski SJ, Murphy RM (1992) Kinetics of aggregation of synthetic beta-amyloid peptide. Arch Biochem Biophys 294, 630-638.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 630-638
    • Tomski, S.J.1    Murphy, R.M.2
  • 43
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow CJ, Zagorski MG (1991) Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition. Science 253, 179-182. (Pubitemid 21917135)
    • (1991) Science , vol.253 , Issue.5016 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 45
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of amyloid beta (1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action
    • DOI 10.1002/cbic.200700427
    • Bartolini M, Bertucci C, Bolognesi ML, Cavalli A, Melchiorre C, Andrisano V (2007) Insight into the kinetic of amyloid beta (1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action. Chembiochem 8, 2152-2161. (Pubitemid 350220767)
    • (2007) ChemBioChem , vol.8 , Issue.17 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 46
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PT, Zagorski MG (1992) Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease Analysis of circular dichroism spectra. J Mol Biol 225, 1075-1093.
    • (1992) J Mol Biol , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 47
    • 0347753786 scopus 로고    scopus 로고
    • Two Types of Alzheimer's beta-Amyloid (1-40) Peptide Membrane Interactions: Aggregation Preventing Transmembrane Anchoring Versus Accelerated Surface Fibril Formation
    • DOI 10.1016/j.jmb.2003.11.046
    • Bokvist M, Lindstrom F, Watts A, Grobner G (2004) Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J Mol Biol 335, 1039-1049. (Pubitemid 38091609)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 1039-1049
    • Bokvist, M.1    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 48
    • 14644390240 scopus 로고    scopus 로고
    • Structural role of glycine in amyloid fibrils formed from transmembrane alpha-helices
    • DOI 10.1021/bi047827g
    • Liu W, Crocker E, Zhang W, Elliott JI, Luy B, Li H, Aimoto S, Smith SO (2005) Structural role of glycine in amyloid fibrils formed from transmembrane alpha-helices. Biochemistry 44, 3591-3597. (Pubitemid 40322028)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3591-3597
    • Liu, W.1    Crocker, E.2    Zhang, W.3    Elliott, J.I.4    Luy, B.5    Li, H.6    Aimoto, S.7    Smith, S.O.8
  • 49
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity
    • Hung LW, Ciccotosto GD, Giannakis E, Tew DJ, Perez K, Masters CL, Cappai R, Wade JD, Barnham KJ (2008) Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity. J Neurosci 28, 11950-11958.
    • (2008) J Neurosci , vol.28 , pp. 11950-11958
    • Hung, L.W.1    Ciccotosto, G.D.2    Giannakis, E.3    Tew, D.J.4    Perez, K.5    Masters, C.L.6    Cappai, R.7    Wade, J.D.8    Barnham, K.J.9
  • 51
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid beta-protein fibril assembly Differential effects of alpha-helix stabilization
    • Fezoui Y, Teplow DB (2002) Kinetic studies of amyloid beta-protein fibril assembly Differential effects of alpha-helix stabilization. J Biol Chem 277, 36948-36954.
    • (2002) J Biol Chem , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 52
    • 48849097629 scopus 로고    scopus 로고
    • Circular dichroism to study protein interactions
    • UNIT 20
    • Kelly SM, Price NC (2006) Circular dichroism to study protein interactions. Curr Protoc Protein Sci, UNIT 20.10.
    • (2006) Curr Protoc Protein Sci , pp. 10
    • Kelly, S.M.1    Price, N.C.2
  • 54
    • 33750594531 scopus 로고    scopus 로고
    • Simultaneous electrophoretic analysis of proteins of very high and low molecular weights using low-percentage acrylamide gel and a gradient SDS-PAGE gel
    • DOI 10.1002/elps.200600141
    • Casas-Terradellas E, Garcia-Gonzalo FR, Hadjebi O, Bartrons R, Ventura F, Rosa JL (2006) Simultaneous electrophoretic analysis of proteins of very high and low molecular weights using low-percentage acrylamide gel and a gradient SDS-PAGE gel. Electrophoresis 27, 3935-3938. (Pubitemid 44680803)
    • (2006) Electrophoresis , vol.27 , Issue.20 , pp. 3935-3938
    • Casas-Terradellas, E.1    Garcia-Gonzalo, F.R.2    Hadjebi, O.3    Bartrons, R.4    Ventur, F.5    Rosa, J.L.6
  • 55
    • 78651153791 scopus 로고
    • Disc Electrophoresis II. Method and Application to human serum proteins
    • Davis BJ (1964) Disc Electrophoresis II. Method and Application to human serum proteins. Ann N Y Acad Sci 121, 404-427.
    • (1964) Ann N Y Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 56
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 58
    • 75549089646 scopus 로고    scopus 로고
    • Apolipoprotein E protects cultured pericytes and astrocytes from D-Abeta(1-40)-mediated cell death
    • Bruinsma IB, Wilhelmus MM, Kox M, Veerhuis R, de Waal RM, Verbeek MM (2010) Apolipoprotein E protects cultured pericytes and astrocytes from D-Abeta(1-40)-mediated cell death. Brain Res 1315, 169-180.
    • (2010) Brain Res , vol.1315 , pp. 169-180
    • Bruinsma, I.B.1    Wilhelmus, M.M.2    Kox, M.3    Veerhuis, R.4    De Waal, R.M.5    Verbeek, M.M.6
  • 61
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers - What you see is not always what you get
    • DOI 10.1080/13506120500106958
    • Bitan G, Fradinger EA, Spring SM, Teplow DB (2005) Neurotoxic protein oligomers-what you see is not always what you get. Amyloid 12, 88-95. (Pubitemid 40978716)
    • (2005) Amyloid , vol.12 , Issue.2 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 62
    • 77954835300 scopus 로고    scopus 로고
    • High-molecular-weight {beta}-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients
    • Fukumoto H, Tokuda T, Kasai T, Ishigami N, Hidaka H, Kondo M, Allsop D, Nakagawa M (2010) High-molecular-weight {beta}-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. FASEB J 24, 2716-2726.
    • (2010) FASEB J , vol.24 , pp. 2716-2726
    • Fukumoto, H.1    Tokuda, T.2    Kasai, T.3    Ishigami, N.4    Hidaka, H.5    Kondo, M.6    Allsop, D.7    Nakagawa, M.8
  • 64
    • 73249127170 scopus 로고    scopus 로고
    • Native electrophoretic techniques to identify protein-protein interactions
    • Wittig I, Schagger H (2009) Native electrophoretic techniques to identify protein-protein interactions. Proteomics 9, 5214-5223.
    • (2009) Proteomics , vol.9 , pp. 5214-5223
    • Wittig, I.1    Schagger, H.2
  • 65
    • 0242362596 scopus 로고    scopus 로고
    • Beta-Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
    • DOI 10.1046/j.1432-1033.2003.03815.x
    • Klug GM, Losic D, Subasinghe SS, Aguilar MI, Martin LL, Small DH (2003) Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH. Eur J Biochem 270, 4282-4293. (Pubitemid 37340346)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.21 , pp. 4282-4293
    • Klug, G.M.J.A.1    Losic, D.2    Subasinghe, S.S.3    Aguilar, M.-I.4    Martin, L.L.5    Small, D.H.6
  • 66
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • DOI 10.1073/pnas.96.11.6020
    • Fancy DA, Kodadek T (1999) Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light. Proc Natl Acad Sci U S A 96, 6020-6024. (Pubitemid 29256612)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.11 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 67
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan G, Lomakin A, Teplow DB (2001) Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276, 35176-35184.
    • (2001) J Biol Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 68
    • 77954039898 scopus 로고    scopus 로고
    • Real-time imaging and quantification of amyloid-beta peptide aggregates by novel quantum-dot nanoprobes
    • Tokuraku K, Marquardt M, Ikezu T (2009) Real-time imaging and quantification of amyloid-beta peptide aggregates by novel quantum-dot nanoprobes. PLoS One 4, e8492.
    • (2009) PLoS One , vol.4
    • Tokuraku, K.1    Marquardt, M.2    Ikezu, T.3
  • 69
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von JG (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von, J.G.2
  • 71
    • 33646036173 scopus 로고    scopus 로고
    • Adventures in the matrix
    • Eisenstein M (2006) Adventures in the matrix. Nat Protoc 3, 410.
    • (2006) Nat Protoc , vol.3 , pp. 410
    • Eisenstein, M.1
  • 72
    • 71549121663 scopus 로고    scopus 로고
    • Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking Implications for deducing the structure of endogenous amyloid-beta oligomers
    • Moore BD, Rangachari V, Tay WM, Milkovic NM, Rosenberry TL (2009) Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking Implications for deducing the structure of endogenous amyloid-beta oligomers. Biochemistry 48, 11796-11806.
    • (2009) Biochemistry , vol.48 , pp. 11796-11806
    • Moore, B.D.1    Rangachari, V.2    Tay, W.M.3    Milkovic, N.M.4    Rosenberry, T.L.5
  • 73
    • 35648986681 scopus 로고    scopus 로고
    • Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate
    • DOI 10.1021/bi701213s
    • Rangachari V, Moore BD, Reed DK, Sonoda LK, Bridges AW, Conboy E, Hartigan D, Rosenberry TL (2007) Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. Biochemistry 46, 12451-12462. (Pubitemid 350027406)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12451-12462
    • Rangachari, V.1    Moore, B.D.2    Reed, D.K.3    Sonoda, L.K.4    Bridges, A.W.5    Conboy, E.6    Hartigan, D.7    Rosenberry, T.L.8
  • 74
    • 34447255463 scopus 로고    scopus 로고
    • Formation of Toxic Fibrils of Alzheimer's Amyloid beta-Protein-(1-40) by Monosialoganglioside GM1, a Neuronal Membrane Component
    • DOI 10.1016/j.jmb.2007.05.069, PII S0022283607007176
    • Okada T, Wakabayashi M, Ikeda K, Matsuzaki K (2007) Formation of toxic fibrils of Alzheimer's amyloid betaprotein-(1-40) by monosialoganglioside GM1, a neuronal membrane component. J Mol Biol 371, 481-489. (Pubitemid 47048280)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.2 , pp. 481-489
    • Okada, T.1    Wakabayashi, M.2    Ikeda, K.3    Matsuzaki, K.4
  • 76
    • 0033624283 scopus 로고    scopus 로고
    • Differences in the Abeta40/Abeta42 ratio associated with cerebrospinal fluid lipoproteins as a function of apolipoprotein E genotype
    • DOI 10.1002/1531-8249(200008)48:2<201::AID-ANA10>3.0.CO;2-X
    • Fagan AM, Younkin LH, Morris JC, Fryer JD, Cole TG, Younkin SG, Holtzman DM (2000) Differences in the Abeta40/Abeta42 ratio associated with cerebrospinal fluid lipoproteins as a function of apolipoprotein E genotype. Ann Neurol 48, 201-210. (Pubitemid 30617039)
    • (2000) Annals of Neurology , vol.48 , Issue.2 , pp. 201-210
    • Fagan, A.M.1    Younkin, L.H.2    Morris, J.C.3    Fryer, J.D.4    Cole, T.G.5    Younkin, S.G.6    Holtzman, D.M.7
  • 77
    • 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
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL (2007) 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, 2866-2875. (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , 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
  • 78
    • 34247145107 scopus 로고    scopus 로고
    • Attenuated amyloid-beta aggregation and neurotoxicity owing to methionine oxidation
    • DOI 10.1097/WNR.0b013e3280b07c21, PII 0000175620070416000007
    • Johansson AS, Bergquist J, Volbracht C, Paivio A, Leist M, Lannfelt L, Westlind-Danielsson A (2007) Attenuated amyloid-beta aggregation and neurotoxicity owing to methionine oxidation. Neuroreport 18, 559-563. (Pubitemid 46594915)
    • (2007) NeuroReport , vol.18 , Issue.6 , pp. 559-563
    • Johansson, A.-S.1    Bergquist, J.2    Volbracht, C.3    Paivio, A.4    Leist, M.5    Lannfelt, L.6    Westlind-Danielsson, A.7
  • 79
    • 0035846576 scopus 로고    scopus 로고
    • Spontaneous in vitro formation of supramolecular beta-amyloid structures, "betaamy balls", by beta-amyloid 1-40 peptide
    • DOI 10.1021/bi010375c
    • Westlind-Danielsson A, Arnerup G (2001) Spontaneous in vitro formation of supramolecular beta-amyloid structures, "betaamy balls", by beta-amyloid 1-40 peptide. Biochemistry 40, 14736-14743. (Pubitemid 33136093)
    • (2001) Biochemistry , vol.40 , Issue.49 , pp. 14736-14743
    • Westlind-Danielsson, A.1    Arnerup, G.2
  • 80
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores
    • DOI 10.1016/S0022-2836(03)00927-6
    • Lashuel HA, Hartley DM, Petre BM, Wall JS, Simon MN, Walz T, Lansbury PT Jr (2003) Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores. J Mol Biol 332, 795-808. (Pubitemid 37101368)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.4 , 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
  • 81
    • 0345060507 scopus 로고    scopus 로고
    • Abeta Protofibrils Possess a Stable Core Structure Resistant to Hydrogen Exchange
    • DOI 10.1021/bi0357816
    • Kheterpal I, Lashuel HA, Hartley DM, Walz T, Lansbury PT Jr, Wetzel R (2003) Abeta protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry 42, 14092-14098. (Pubitemid 37499405)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14092-14098
    • Kheterpal, I.1    Lashuel, H.A.2    Hartley, D.M.3    Walz, T.4    Lansbury Jr., P.T.5    Wetzel, R.6
  • 82
    • 33748742268 scopus 로고    scopus 로고
    • Is any measurement method optimal for all aggregate sizes and types?
    • Philo JS (2006) Is any measurement method optimal for all aggregate sizes and types? AAPS J 8, E564-E571.
    • (2006) AAPS J , vol.8
    • Philo, J.S.1
  • 85
    • 22844445895 scopus 로고    scopus 로고
    • Preparation of aggregate-free, low molecular weight amyloid-beta for assembly and toxicity assays
    • Bitan G, Teplow DB (2005) Preparation of aggregate-free, low molecular weight amyloid-beta for assembly and toxicity assays. Methods Mol Biol 299, 3-9.
    • (2005) Methods Mol Biol , vol.299 , pp. 3-9
    • Bitan, G.1    Teplow, D.B.2
  • 86
    • 22844438853 scopus 로고    scopus 로고
    • Quasielastic light scattering for protein assembly studies
    • Lomakin A, Teplow DB, Benedek GB (2005) Quasielastic light scattering for protein assembly studies. Methods Mol Biol 299, 153-174.
    • (2005) Methods Mol Biol , vol.299 , pp. 153-174
    • Lomakin, A.1    Teplow, D.B.2    Benedek, G.B.3
  • 87
    • 68549110182 scopus 로고    scopus 로고
    • In vitro amyloid Abeta(1-42) peptide aggregation monitoring by asymmetrical flow field-flow fractionation with multi-angle light scattering detection
    • Rambaldi DC, Zattoni A, Reschiglian P, Colombo R, De LE (2009) In vitro amyloid Abeta(1-42) peptide aggregation monitoring by asymmetrical flow field-flow fractionation with multi-angle light scattering detection. Anal Bioanal Chem 394, 2145-2149.
    • (2009) Anal Bioanal Chem , vol.394 , pp. 2145-2149
    • Rambaldi, D.C.1    Zattoni, A.2    Reschiglian, P.3    Colombo, R.4    De, L.E.5
  • 88
    • 0014085985 scopus 로고
    • Observation of the spectrum of light scattered by solutions of biological macromolecules
    • Dubin SB, Lunacek JH, Benedek GB (1967) Observation of the spectrum of light scattered by solutions of biological macromolecules. Proc Natl Acad Sci U S A 57, 1164-1171.
    • (1967) Proc Natl Acad Sci U S A , vol.57 , pp. 1164-1171
    • Dubin, S.B.1    Lunacek, J.H.2    Benedek, G.B.3
  • 89
    • 0034728443 scopus 로고    scopus 로고
    • Turbidity as a useful optical parameter to predict protein crystallization by dynamic light scattering
    • Moreno A, Mas-Oliva J, Soriano-Garcia M, Salvador CO, Bolanos-Garcia VM (2000) Turbidity as a useful optical parameter to predict protein crystallization by dynamic light scattering. J Mol Struct 519, 243-256.
    • (2000) J Mol Struct , vol.519 , pp. 243-256
    • Moreno, A.1    Mas-Oliva, J.2    Soriano-Garcia, M.3    Salvador, C.O.4    Bolanos-Garcia, V.M.5
  • 90
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism
    • DOI 10.1074/jbc.M500052200
    • Carrotta R, Manno M, Bulone D, Martorana V, San Biagio PL (2005) Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. J Biol Chem 280, 30001-30008. (Pubitemid 41216175)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San, B.P.L.5
  • 93
    • 0029157531 scopus 로고
    • Solvent ef fects on self-assembly of beta-amyloid peptide
    • Shen CL, Murphy RM (1995) Solvent ef fects on self-assembly of beta-amyloid peptide. Biophys J 69, 640-651.
    • (1995) Biophys J , vol.69 , pp. 640-651
    • Shen, C.L.1    Murphy, R.M.2
  • 94
    • 0016740820 scopus 로고
    • Immunoassay by light scattering spectroscopy
    • Cohen RJ, Benedek GB (1975) Immunoassay by light scattering spectroscopy. Immunochemistry 12, 349-351.
    • (1975) Immunochemistry , vol.12 , pp. 349-351
    • Cohen, R.J.1    Benedek, G.B.2
  • 96
    • 33749506729 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of amyloid oligomers and fibrils
    • Mok YF, Howlett GJ (2006) Sedimentation velocity analysis of amyloid oligomers and fibrils. Methods Enzymol 413, 199-217.
    • (2006) Methods Enzymol , vol.413 , pp. 199-217
    • Mok, Y.F.1    Howlett, G.J.2
  • 97
    • 77950552292 scopus 로고    scopus 로고
    • Modulation of aggregate size- and shape-distributions of the amyloid-beta peptide by a designed beta-sheet breaker
    • Nagel-Steger L, Demeler B, Meyer-Zaika W, Hochdorffer K, Schrader T, Willbold D (2010) Modulation of aggregate size- and shape-distributions of the amyloid-beta peptide by a designed beta-sheet breaker. Eur Biophys J 39, 415-422.
    • (2010) Eur Biophys J , vol.39 , pp. 415-422
    • Nagel-Steger, L.1    Demeler, B.2    Meyer-Zaika, W.3    Hochdorffer, K.4    Schrader, T.5    Willbold, D.6
  • 99
    • 79955627838 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of amyloid oligomers and fibrils using fluorescence detection
    • Mok YF, Ryan TM, Yang S, Hatters DM, Howlett GJ, Griffin MD (2011) Sedimentation velocity analysis of amyloid oligomers and fibrils using fluorescence detection. Methods 54, 67-75.
    • (2011) Methods , vol.54 , pp. 67-75
    • Mok, Y.F.1    Ryan, T.M.2    Yang, S.3    Hatters, D.M.4    Howlett, G.J.5    Griffin, M.D.6
  • 100
    • 33750294048 scopus 로고    scopus 로고
    • Direct Observation of Oligomeric Species formed in the Early Stages of Amyloid Fibril Formation using Electrospray Ionisation Mass Spectrometry
    • DOI 10.1016/j.jmb.2006.08.081, PII S0022283606011399
    • Smith AM, Jahn TR, Ashcroft AE, Radford SE (2006) Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J Mol Biol 364, 9-19. (Pubitemid 44634528)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.1 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 101
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems. Biophys J 82, 1096-1111. (Pubitemid 34111246)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Hewlett, G.J.4    Schubert, D.5
  • 102
    • 0037380769 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of flexible macromolecules: Self-association and tangling of amyloid fibrils
    • MacRaild CA, Hatters DM, Lawrence LJ, Howlett GJ (2003) Sedimentation velocity analysis of flexible macromolecules: Self-association and tangling of amyloid fibrils. Biophys J 84, 2562-2569. (Pubitemid 36373576)
    • (2003) Biophysical Journal , vol.84 , Issue.4 , pp. 2562-2569
    • MacRaild, C.A.1    Hatters, D.M.2    Lawrence, L.J.3    Howlett, G.J.4
  • 103
    • 79960990652 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of amyloid fibrils
    • Pham CL, Mok YF, Howlett GJ (2011) Sedimentation velocity analysis of amyloid fibrils. Methods Mol Biol 752, 179-196.
    • (2011) Methods Mol Biol , vol.752 , pp. 179-196
    • Pham, C.L.1    Mok, Y.F.2    Howlett, G.J.3
  • 104
    • 75649105423 scopus 로고    scopus 로고
    • A prochelator activated by hydrogen peroxide prevents metal-induced amyloid Beta aggregation
    • Dickens MG, Franz KJ (2010) A prochelator activated by hydrogen peroxide prevents metal-induced amyloid Beta aggregation. Chembiochem 11, 59-62.
    • (2010) Chembiochem , vol.11 , pp. 59-62
    • Dickens, M.G.1    Franz, K.J.2
  • 105
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula M, Kayed R, Milton S, Glabe CG (2007) Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282, 10311-10324. (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 106
    • 36348989570 scopus 로고    scopus 로고
    • Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-beta-peptide aggregation
    • DOI 10.1016/j.neulet.2007.09.068, PII S0304394007010774
    • Santa-Maria I, Hernandez F, Moreno FJ, Avila J (2007) Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-beta-peptide aggregation. Neurosci Lett 429, 91-94. (Pubitemid 350161113)
    • (2007) Neuroscience Letters , vol.429 , Issue.2-3 , pp. 91-94
    • Santa-Maria, I.1    Hernandez, F.2    Moreno, F.J.3    Avila, J.4
  • 107
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • Jarrett JT, Lansbury PT Jr (1993) Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058. (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 108
    • 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
    • DOI 10.1021/bi00069a001
    • Jarrett JT, Berger EP, Lansbury PT Jr (1993) 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, 4693-4697. (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 109
    • 0028872558 scopus 로고
    • Apolipoprotein e is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease
    • Evans KC, Berger EP, Cho CG, Weisgraber KH, Lansbury PT Jr (1995) Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease. Proc Natl Acad Sci U S A 92, 763-767.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.G.3    Weisgraber, K.H.4    Lansbury Jr., P.T.5
  • 111
    • 0035257136 scopus 로고    scopus 로고
    • "Congo" red: Out of Africa?
    • Steensma DP (2001) "Congo" red: Out of Africa? Arch Pathol Lab Med 125, 250-252.
    • (2001) Arch Pathol Lab Med , vol.125 , pp. 250-252
    • Steensma, D.P.1
  • 112
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A, Sutter M, Jiskoot W (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25, 1487-1499.
    • (2008) Pharm Res , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 114
    • 68949163262 scopus 로고    scopus 로고
    • Preparation of fluorescently-labeled amyloid-beta peptide assemblies: The effect of fluorophore conjugation on structure and function
    • Jungbauer LM, Yu C, Laxton KJ, LaDu MJ (2009) Preparation of fluorescently-labeled amyloid-beta peptide assemblies: The effect of fluorophore conjugation on structure and function. J Mol Recognit 22, 403-413.
    • (2009) J Mol Recognit , vol.22 , pp. 403-413
    • Jungbauer, L.M.1    Yu, C.2    Laxton, K.J.3    LaDu, M.J.4
  • 115
    • 33845192482 scopus 로고    scopus 로고
    • Congo red and protein aggregation in neurodegenerative diseases
    • DOI 10.1016/j.brainresrev.2006.08.001, PII S0165017306001019
    • Frid P, Anisimov SV, Popovic N (2007) Congo red and protein aggregation in neurodegenerative diseases. Brain Res Rev 53, 135-160. (Pubitemid 44854214)
    • (2007) Brain Research Reviews , vol.53 , Issue.1 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 116
    • 0000930795 scopus 로고
    • Etude histochimique des plaques seniles
    • Divry P (1927) Etude histochimique des plaques seniles. J Belg Neurol Psychiatrie 27, 643-657.
    • (1927) J Belg Neurol Psychiatrie , vol.27 , pp. 643-657
    • Divry, P.1
  • 118
    • 0028588694 scopus 로고
    • Congo red protects against toxicity of beta-amyloid peptides on rat hippocampal neurones
    • Burgevin MC, Passat M, Daniel N, Capet M, Doble A (1994) Congo red protects against toxicity of beta-amyloid peptides on rat hippocampal neurones. Neuroreport 5, 2429-2432.
    • (1994) Neuroreport , vol.5 , pp. 2429-2432
    • Burgevin, M.C.1    Passat, M.2    Daniel, N.3    Capet, M.4    Doble, A.5
  • 122
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • DOI 10.1021/bi972029u
    • Podlisny MB, Walsh DM, Amarante P, Ostaszewski BL, Stimson ER, Maggio JE, Teplow DB, Selkoe DJ (1998) Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 37, 3602-3611. (Pubitemid 28162915)
    • (1998) Biochemistry , vol.37 , Issue.11 , 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    Teplow, D.B.7    Selkoe, D.J.8
  • 123
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser PE, Nguyen JT, Chin DT, Kirschner DA (1992) Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions. J Neurochem 59, 1531-1540.
    • (1992) J Neurochem , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 124
    • 0000464103 scopus 로고
    • Fluorescent stains, with special reference to amyloid and connective tissues
    • Vassar PS, Culling CF (1959) Fluorescent stains, with special reference to amyloid and connective tissues. Arch Pathol 68, 487-498.
    • (1959) Arch Pathol , vol.68 , pp. 487-498
    • Vassar, P.S.1    Culling, C.F.2
  • 125
    • 0032855076 scopus 로고    scopus 로고
    • Staining methods for identification of amyloid in tissue
    • DOI 10.1016/S0076-6879(99)09003-5
    • Westermark GT, Johnson KH, Westermark P (1999) Staining methods for identification of amyloid in tissue. Methods Enzymol 309, 3-25. (Pubitemid 29446438)
    • (1999) Methods in Enzymology , vol.309 , pp. 3-25
    • Westermark, G.T.1    Johnson, K.H.2    Westermark, P.3
  • 126
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
    • DOI 10.1016/0003-2697(89)90046-8
    • Naiki H, Higuchi K, Hosokawa M, Takeda T (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 177, 244-249. (Pubitemid 19088253)
    • (1989) Analytical Biochemistry , vol.177 , Issue.2 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 127
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H, III (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 2, 404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 128
    • 34248670403 scopus 로고    scopus 로고
    • Study on the binding of Thioflavin T to beta-sheet-rich and non-beta-sheet cavities
    • DOI 10.1016/j.jsb.2006.12.010, PII S1047847706003923
    • Groenning M, Olsen L, van de Weert M, Flink JM, Frokjaer S, Jorgensen FS (2007) Study on the binding of Thioflavin T to beta-sheet-rich and non-beta-sheet cavities. J Struct Biol 158, 358-369. (Pubitemid 46766672)
    • (2007) Journal of Structural Biology , vol.158 , Issue.3 , pp. 358-369
    • Groenning, M.1    Olsen, L.2    Van De, W.M.3    Flink, J.M.4    Frokjaer, S.5    Jorgensen, F.S.6
  • 129
    • 70349481513 scopus 로고    scopus 로고
    • The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds
    • Hudson SA, Ecroyd H, Kee TW, Carver JA (2009) The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds. FEBS J 276, 5960-5972.
    • (2009) FEBS J , vol.276 , pp. 5960-5972
    • Hudson, S.A.1    Ecroyd, H.2    Kee, T.W.3    Carver, J.A.4
  • 130
    • 55949096479 scopus 로고    scopus 로고
    • Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin
    • Sakono M, Zako T, Ueda H, Yohda M, Maeda M (2008) Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin. FEBS J 275, 5982-5993.
    • (2008) FEBS J , vol.275 , pp. 5982-5993
    • Sakono, M.1    Zako, T.2    Ueda, H.3    Yohda, M.4    Maeda, M.5
  • 132
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • Groenning M (2009) Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J Chem Biol 3, 1-18.
    • (2009) J Chem Biol , vol.3 , pp. 1-18
    • Groenning, M.1
  • 133
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H, III (1999) Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 309, 274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 135
    • 0036175642 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: The technique and its applications
    • Krichevsky O, Bonnet G (2002) Fluorescence correlation spectroscopy: The technique and its applications. Rep Prog Physics 65, 251-297.
    • (2002) Rep Prog Physics , vol.65 , pp. 251-297
    • Krichevsky, O.1    Bonnet, G.2
  • 136
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Novel variations of an established technique
    • DOI 10.1146/annurev.biophys.36.040306.132612
    • Haustein E, Schwille P (2007) Fluorescence correlation spectroscopy: Novel variations of an established technique. Annu Rev Biophys Biomol Struct 36, 151-169. (Pubitemid 46998114)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 137
    • 33646427228 scopus 로고    scopus 로고
    • Selective destabilization of soluble amyloid beta oligomers by divalent metal ions
    • Garai K, Sengupta P, Sahoo B, Maiti S (2006) Selective destabilization of soluble amyloid beta oligomers by divalent metal ions. Biochem Biophys Res Commun 345, 210-215.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 210-215
    • Garai, K.1    Sengupta, P.2    Sahoo, B.3    Maiti, S.4
  • 138
    • 0041817542 scopus 로고    scopus 로고
    • 1-40) is thermodynamically soluble at physiological concentrations
    • DOI 10.1021/bi0341410
    • Sengupta P, Garai K, Sahoo B, Shi Y, Callaway DJ, Maiti S (2003) The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations. Biochemistry 42, 10506-10513. (Pubitemid 37071451)
    • (2003) Biochemistry , vol.42 , Issue.35 , pp. 10506-10513
    • Sengupta, P.1    Garai, K.2    Sahoo, B.3    Shi, Y.4    Callaway, D.J.E.5    Maiti, S.6
  • 140
    • 20144379798 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for imaging, labelling and sensing
    • DOI 10.1038/nmat1390
    • Medintz IL, Uyeda HT, Goldman ER, Mattoussi H (2005) Quantum dot bioconjugates for imaging, labelling and sensing. Nat Mater 4, 435-446. (Pubitemid 40774047)
    • (2005) Nature Materials , vol.4 , Issue.6 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3    Mattoussi, H.4
  • 141
    • 0002388566 scopus 로고
    • Protein fluorescence
    • Lakowicz JR (ed.), Plenum Press, New York and London
    • Lakowicz JR (1983) Protein fluorescence. In Principles of Fluorescence Spectroscopy Lakowicz JR (ed.), Plenum Press, New York and London, p. 342.
    • (1983) Principles of Fluorescence Spectroscopy , pp. 342
    • Lakowicz, J.R.1
  • 143
    • 0015116634 scopus 로고
    • Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G
    • Engvall E, Perlmann P (1971) Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry 8, 871-874.
    • (1971) Immunochemistry , vol.8 , pp. 871-874
    • Engvall, E.1    Perlmann, P.2
  • 144
    • 70849108991 scopus 로고    scopus 로고
    • Drivers of biodiagnostic development
    • Giljohann DA, Mirkin CA (2009) Drivers of biodiagnostic development. Nature 462, 461-464.
    • (2009) Nature , vol.462 , pp. 461-464
    • Giljohann, D.A.1    Mirkin, C.A.2
  • 149
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489. (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
  • 150
    • 78649754766 scopus 로고    scopus 로고
    • Amyloid-beta oligomer specificity mediated by the IgM isotype - Implications for a specific protective mechanism exerted by endogeneous auto-antibodies
    • Linghagen-Persson M, Brannstrom K, Vestling M, Steinitz M, Olofsson A (2010) Amyloid-beta oligomer specificity mediated by the IgM isotype - implications for a specific protective mechanism exerted by endogeneous auto-antibodies. PLoS One 5, e13928.
    • (2010) PLoS One , vol.5
    • Linghagen-Persson, M.1    Brannstrom, K.2    Vestling, M.3    Steinitz, M.4    Olofsson, A.5
  • 151
    • 57649171529 scopus 로고    scopus 로고
    • Characterisation of two antibodies to oligomeric Abeta and their use in ELISAs on human brain tissue homogenates
    • van Helmond Z, Heesom K, Love S (2009) Characterisation of two antibodies to oligomeric Abeta and their use in ELISAs on human brain tissue homogenates. J Neurosci Methods 176, 206-212.
    • (2009) J Neurosci Methods , vol.176 , pp. 206-212
    • Van Helmond, Z.1    Heesom, K.2    Love, S.3
  • 155
    • 60549107033 scopus 로고    scopus 로고
    • A specific enzyme-linked immunosorbent assay for measuring beta-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease
    • Xia W, Yang T, Shankar G, Smith IM, Shen Y, Walsh DM, Selkoe DJ (2009) A specific enzyme-linked immunosorbent assay for measuring beta-amyloid protein
    • (2009) Arch Neurol , vol.66 , pp. 190-199
    • Xia, W.1    Yang, T.2    Shankar, G.3    Smith, I.M.4    Shen, Y.5    Walsh, D.M.6    Selkoe, D.J.7
  • 158
    • 80051539734 scopus 로고    scopus 로고
    • Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease
    • author reply 510-511
    • Bruggink KA, Kuiperij HP, Ekholm-Pettersson F, Verbeek MM (2011) Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 77, 510; author reply 510-511.
    • (2011) Neurology , vol.77 , pp. 510
    • Bruggink, K.A.1    Kuiperij, H.P.2    Ekholm-Pettersson, F.3    Verbeek, M.M.4
  • 160
    • 0034087032 scopus 로고    scopus 로고
    • Human anti-mouse antibodies
    • Klee GG (2000) Human anti-mouse antibodies. Arch Pathol Lab Med 124, 921-923.
    • (2000) Arch Pathol Lab Med , vol.124 , pp. 921-923
    • Klee, G.G.1
  • 161
    • 0141868926 scopus 로고    scopus 로고
    • Nanoparticle-based bio-bar codes for the ultrasensitive detection of proteins
    • DOI 10.1126/science.1088755
    • Nam JM, Thaxton CS, Mirkin CA (2003) Nanoparticle-based bio-bar codes for the ultrasensitive detection of proteins. Science 301, 1884-1886. (Pubitemid 37221389)
    • (2003) Science , vol.301 , Issue.5641 , pp. 1884-1886
    • Nam, J.-M.1    Thaxton, C.S.2    Mirkin, C.A.3
  • 163
    • 33748926472 scopus 로고    scopus 로고
    • Protein detection using biobarcodes
    • Muller UR (2006) Protein detection using biobarcodes. Mol Biosyst 2, 470-476.
    • (2006) Mol Biosyst , vol.2 , pp. 470-476
    • Muller, U.R.1
  • 165
    • 0032504940 scopus 로고    scopus 로고
    • Light-scattering submicroscopic particles as highly fluorescent analogs and their use as tracer labels in clinical and biological applications I. Theory
    • DOI 10.1006/abio.1998.2759
    • Yguerabide J, Yguerabide EE (1998) Light-scattering submicroscopic particles as highly fluorescent analogs and their use as tracer labels in clinical and biological applications. Anal Biochem 262, 137-156. (Pubitemid 28452774)
    • (1998) Analytical Biochemistry , vol.262 , Issue.2 , pp. 137-156
    • Yguerabide, J.1    Yguerabide, E.E.2
  • 169
    • 47849098034 scopus 로고    scopus 로고
    • 1-42 and amyloid-beta oligomers in blood using magnetic beads in combination with flow cytometry and its application in the diagnostics of Alzheimer's disease
    • Santos AN, Simm A, Holthoff V, Boehm G (2008) A method for the detection of amyloid-beta1-40, amyloid-beta1-42 and amyloid-beta oligomers in blood using magnetic beads in combination with Flow cytometry and its application in the diagnostics of Alzheimer's disease. J Alzheimers Dis 14, 127-131. (Pubitemid 352040031)
    • (2008) Journal of Alzheimer's Disease , vol.14 , Issue.2 , pp. 127-131
    • Santos, A.N.1    Simm, A.2    Holthoff, V.3    Boehm, G.4
  • 171
    • 79954613385 scopus 로고    scopus 로고
    • Folding stability of amyloid-beta 40 monomer is an important determinant of the nucleation kinetics in fibrillization
    • Ni CL, Shi HP, Yu HM, Chang YC, Chen YR (2011) Folding stability of amyloid-beta 40 monomer is an important determinant of the nucleation kinetics in fibrillization. FASEB J 25, 1390-1401.
    • (2011) FASEB J , vol.25 , pp. 1390-1401
    • Ni, C.L.1    Shi, H.P.2    Yu, H.M.3    Chang, Y.C.4    Chen, Y.R.5
  • 174
    • 44849092655 scopus 로고    scopus 로고
    • Nanotechnology solutions for Alzheimer's disease: Advances in research tools, diagnostic methods and therapeutic agents
    • Nazem A, Mansoori GA (2008) Nanotechnology solutions for Alzheimer's disease: Advances in research tools, diagnostic methods and therapeutic agents. J Alzheimers Dis 13, 199-223. (Pubitemid 352038525)
    • (2008) Journal of Alzheimer's Disease , vol.13 , Issue.2 , pp. 199-223
    • Nazem, A.1    Mansoori, G.A.2
  • 175
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation
    • DOI 10.1073/pnas.96.7.3688
    • Kowalewski T, Holtzman DM (1999) In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation. Proc Natl Acad Sci U S A 96, 3688-3693. (Pubitemid 29168971)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.7 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 177
    • 0347949620 scopus 로고    scopus 로고
    • Characterization by Atomic Force Microscopy of Alzheimer Paired Helical Filaments under Physiological Conditions
    • Moreno-Herrero F, Perez M, Baro AM, Avila J (2004) Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions. Biophys J 86, 517-525. (Pubitemid 38067481)
    • (2004) Biophysical Journal , vol.86 , Issue.1 I , pp. 517-525
    • Moreno-Herrero, F.1    Perez, M.2    Baro, A.M.3    Avila, J.4
  • 178
    • 0038204160 scopus 로고    scopus 로고
    • AFM and STM study of beta -amyloid aggregation on graphite
    • DOI 10.1016/S0304-3991(03)00031-7
    • Wang Z, Zhou C, Wang C, Wan L, Fang X, Bai C (2003) AFM and STM study of beta-amyloid aggregation on graphite. Ultramicroscopy 97, 73-79. (Pubitemid 36683282)
    • (2003) Ultramicroscopy , vol.97 , Issue.1-4 , pp. 73-79
    • Wang, Z.1    Zhou, C.2    Wang, C.3    Wan, L.4    Fang, X.5    Bai, C.6
  • 179
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • Muller DJ, Engel A (1997) The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys J 73, 1633-1644. (Pubitemid 27360752)
    • (1997) Biophysical Journal , vol.73 , Issue.3 , pp. 1633-1644
    • Muller, D.J.1    Engel, A.2
  • 180
    • 22844448175 scopus 로고    scopus 로고
    • Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates
    • Goldsbury C, Green J (2005) Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates. Methods Mol Biol 299, 103-128.
    • (2005) Methods Mol Biol , vol.299 , pp. 103-128
    • Goldsbury, C.1    Green, J.2


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