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Volumn 15, Issue 1, 2015, Pages

Structural differences of amyloid-β fibrils revealed by antibodies from phage display

Author keywords

Abeta; Alzheimer's disease; A ; Beta amyloid; Immune library; Phage display; scFv

Indexed keywords

AGGREGATES; BINS; CONFORMATIONS; DIAGNOSIS; EPITOPES; GLYCOPROTEINS; LIBRARIES; NEURODEGENERATIVE DISEASES; OLIGOMERS; PEPTIDES; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY;

EID: 84935850991     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/s12896-015-0146-8     Document Type: Article
Times cited : (11)

References (78)
  • 1
    • 14844336875 scopus 로고    scopus 로고
    • Survival following dementia onset: Alzheimer's disease and vascular dementia
    • Fitzpatrick AL, Kuller LH, Lopez OL, Kawas CH, Jagust W. Survival following dementia onset: Alzheimer's disease and vascular dementia. J Neurol Sci. 2005;229-230:43-9.
    • (2005) J Neurol Sci , vol.229-230 , pp. 43-49
    • Fitzpatrick, A.L.1    Kuller, L.H.2    Lopez, O.L.3    Kawas, C.H.4    Jagust, W.5
  • 2
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau
    • Goedert M, Wischik CM, Crowther RA, Walker JE, Klug A. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc Natl Acad Sci U S A. 1988;85:4051-5.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 3
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A. 1986;83:4044-8.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 4
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 1984;120:885-90.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • Masters CL, Multhaup G, Simms G, Pottgiesser J, Martins RN, Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J. 1985;4:2757-63.
    • (1985) EMBO J , vol.4 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 6
    • 0022654027 scopus 로고
    • Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease
    • Selkoe DJ, Abraham CR, Podlisny MB, Duffy LK. Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease. J Neurochem. 1986;46:1820-34.
    • (1986) J Neurochem , vol.46 , pp. 1820-1834
    • Selkoe, D.J.1    Abraham, C.R.2    Podlisny, M.B.3    Duffy, L.K.4
  • 7
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
    • Seubert P, Vigo-Pelfrey C, Esch F, Lee M, Dovey H, Davis D, et al. Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids. Nature. 1992;359:325-7.
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3    Lee, M.4    Dovey, H.5    Davis, D.6
  • 8
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury Jr PT. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem. 1997;66:385-407.
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 9
    • 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
    • Jarrett JT, Berger EP, Lansbury Jr PT. 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 (Mosc). 1993;32:4693-7.
    • (1993) Biochemistry (Mosc) , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 10
  • 11
    • 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 AE, Chaney MO, Kuo Y-M, Webster SD, Stine WB, Haverkamp LJ, et al. Morphology and toxicity of Aβ-(1-42) dimer derived from neuritic and vascular Amyloid deposits of Alzheimer's disease. J Biol Chem. 1996;271:20631-5.
    • (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
  • 14
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of Amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren KN. Oligomeric and fibrillar species of Amyloid-beta peptides differentially affect neuronal viability. J Biol Chem. 2002;277:32046-53.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1
  • 15
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesné S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature. 2006;440:352-7.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5    Yang, A.6
  • 16
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 2002;416:535-9.
    • (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
  • 17
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. Amyloid β-protein fibrillogenesis detection of a protofibrillar intermediate. J Biol Chem. 1997;272:22364-72.
    • (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
  • 18
    • 79953133327 scopus 로고    scopus 로고
    • Aβ42 Neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete A 42 species
    • Jan A, Adolfsson O, Allaman I, Buccarello A-L, Magistretti PJ, Pfeifer A, et al. Aβ42 Neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete A 42 species. J Biol Chem. 2010;286:8585-96.
    • (2010) J Biol Chem , vol.286 , pp. 8585-8596
    • Jan, A.1    Adolfsson, O.2    Allaman, I.3    Buccarello, A.-L.4    Magistretti, P.J.5    Pfeifer, A.6
  • 19
  • 20
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
    • Benilova I, Karran E, De Strooper B. The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci. 2012;15:349-57.
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    Strooper, B.3
  • 21
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol. 2007;8:101-12.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 22
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 2003;300:486-9.
    • (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
  • 23
    • 84884630099 scopus 로고    scopus 로고
    • Human LilrB2 Is a β-Amyloid Receptor and Its Murine Homolog PirB Regulates Synaptic Plasticity in an Alzheimer's Model.
    • Kim T, Vidal GS, Djurisic M, William CM, Birnbaum ME, Garcia KC, et al. Human LilrB2 Is a β-Amyloid Receptor and Its Murine Homolog PirB Regulates Synaptic Plasticity in an Alzheimer's Model. Science. 2013;341:1399-1404.
    • (2013) Science. , vol.341 , pp. 1399-1404
    • Kim, T.1    Vidal, G.S.2    Djurisic, M.3    William, C.M.4    Birnbaum, M.E.5    Garcia, K.C.6
  • 24
  • 26
    • 64049098761 scopus 로고    scopus 로고
    • Neuropathology and cognitive impairment in Alzheimer disease: a complex but coherent relationship
    • Nelson PT, Braak H, Markesbery WR. Neuropathology and cognitive impairment in Alzheimer disease: a complex but coherent relationship. J Neuropathol Exp Neurol. 2009;68:1-14.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 1-14
    • Nelson, P.T.1    Braak, H.2    Markesbery, W.R.3
  • 27
    • 0030582181 scopus 로고    scopus 로고
    • Visualisation and quantification of rates of atrophy in Alzheimer's disease
    • Fox NC, Freeborough PA, Rossor MN. Visualisation and quantification of rates of atrophy in Alzheimer's disease. Lancet. 1996;348:94-7.
    • (1996) Lancet , vol.348 , pp. 94-97
    • Fox, N.C.1    Freeborough, P.A.2    Rossor, M.N.3
  • 31
    • 79960343358 scopus 로고    scopus 로고
    • Perspective: in search of biomarkers
    • Buckholtz NS. Perspective: in search of biomarkers. Nature. 2011;475:S8.
    • (2011) Nature , vol.475 , pp. S8
    • Buckholtz, N.S.1
  • 32
    • 0003960039 scopus 로고    scopus 로고
    • Davidson's principles and practice of medicine
    • Edinburgh; New York: Churchill Livingstone/Elsevier
    • Colledge NR, Walker BR, Ralston S, Davidson S. Davidson's principles and practice of medicine. Edinburgh; New York: Churchill Livingstone/Elsevier; 2010.
    • (2010)
    • Colledge, N.R.1    Walker, B.R.2    Ralston, S.3    Davidson, S.4
  • 33
    • 0033217323 scopus 로고    scopus 로고
    • Therapeutic standards in Alzheimer disease
    • Doody RS. Therapeutic standards in Alzheimer disease. Alzheimer Dis Assoc Disord. 1999;13 Suppl 2:S20-6.
    • (1999) Alzheimer Dis Assoc Disord , vol.13 , pp. S20-S26
    • Doody, R.S.1
  • 34
    • 0345735594 scopus 로고    scopus 로고
    • Evaluation of memantine for the treatment of Alzheimer's disease
    • Ferris SH. Evaluation of memantine for the treatment of Alzheimer's disease. Expert Opin Pharmacother. 2003;4:2305-13.
    • (2003) Expert Opin Pharmacother , vol.4 , pp. 2305-2313
    • Ferris, S.H.1
  • 35
    • 67849092221 scopus 로고    scopus 로고
    • Isolation of a human-like antibody fragment (scFv) that neutralizes ricin biological activity
    • Pelat T, Hust M, Hale M, Lefranc M-P, Dübel S, Thullier P. Isolation of a human-like antibody fragment (scFv) that neutralizes ricin biological activity. BMC Biotechnol. 2009;9:60.
    • (2009) BMC Biotechnol , vol.9 , pp. 60
    • Pelat, T.1    Hust, M.2    Hale, M.3    Lefranc, M.-P.4    Dübel, S.5    Thullier, P.6
  • 36
    • 23044503900 scopus 로고    scopus 로고
    • Selection of a Macaque Fab with framework regions like those in humans, high affinity, and ability to neutralize the Protective Antigen (PA) of Bacillus anthracis by binding to the segment of PA between residues 686 and 694
    • Laffly E, Danjou L, Condemine F, Vidal D, Drouet E, Lefranc M-P, et al. Selection of a Macaque Fab with framework regions like those in humans, high affinity, and ability to neutralize the Protective Antigen (PA) of Bacillus anthracis by binding to the segment of PA between residues 686 and 694. Antimicrob Agents Chemother. 2005;49:3414-20.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3414-3420
    • Laffly, E.1    Danjou, L.2    Condemine, F.3    Vidal, D.4    Drouet, E.5    Lefranc, M.-P.6
  • 37
    • 34547646543 scopus 로고    scopus 로고
    • High-affinity, human antibody-like antibody fragment (Single-Chain Variable Fragment) neutralizing the Lethal Factor (LF) of Bacillus anthracis by inhibiting protective Antigen-LF complex formation
    • Pelat T, Hust M, Laffly E, Condemine F, Bottex C, Vidal D, et al. High-affinity, human antibody-like antibody fragment (Single-Chain Variable Fragment) neutralizing the Lethal Factor (LF) of Bacillus anthracis by inhibiting protective Antigen-LF complex formation. Antimicrob Agents Chemother. 2007;51:2758-64.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2758-2764
    • Pelat, T.1    Hust, M.2    Laffly, E.3    Condemine, F.4    Bottex, C.5    Vidal, D.6
  • 38
    • 68949150896 scopus 로고    scopus 로고
    • Identification of a putative Crf splice variant and generation of recombinant antibodies for the specific detection of Aspergillus fumigatus
    • Schütte M, Thullier P, Pelat T, Wezler X, Rosenstock P, Hinz D, et al. Identification of a putative Crf splice variant and generation of recombinant antibodies for the specific detection of Aspergillus fumigatus. PLoS One. 2009;4:e6625.
    • (2009) PLoS One , vol.4
    • Schütte, M.1    Thullier, P.2    Pelat, T.3    Wezler, X.4    Rosenstock, P.5    Hinz, D.6
  • 39
    • 84872752809 scopus 로고    scopus 로고
    • Isolation and characterisation of a human-like antibody fragment (scFv) that inactivates VEEV in vitro and in vivo
    • Rülker T, Voß L, Thullier P, O' Brien LM, Pelat T, Perkins SD, et al. Isolation and characterisation of a human-like antibody fragment (scFv) that inactivates VEEV in vitro and in vivo. PLoS One. 2012;7, e37242.
    • (2012) PLoS One , vol.7
    • Rülker, T.1    Voß, L.2    Thullier, P.3    O' Brien, L.M.4    Pelat, T.5    Perkins, S.D.6
  • 41
    • 84896499135 scopus 로고    scopus 로고
    • Development of neutralizing scFv-Fc against botulinum neurotoxin A light chain from a macaque immune library
    • Miethe S, Rasetti-Escargueil C, Liu Y, Chahboun S, Pelat T, Avril A, et al. Development of neutralizing scFv-Fc against botulinum neurotoxin A light chain from a macaque immune library. mAbs. 2014;6:446-59.
    • (2014) mAbs , vol.6 , pp. 446-459
    • Miethe, S.1    Rasetti-Escargueil, C.2    Liu, Y.3    Chahboun, S.4    Pelat, T.5    Avril, A.6
  • 43
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: the power of in vitro display technologies
    • Bradbury ARM, Sidhu S, Dübel S, McCafferty J. Beyond natural antibodies: the power of in vitro display technologies. Nat Biotechnol. 2011;29:245-54.
    • (2011) Nat Biotechnol , vol.29 , pp. 245-254
    • Bradbury, A.R.M.1    Sidhu, S.2    Dübel, S.3    McCafferty, J.4
  • 45
    • 84879446443 scopus 로고    scopus 로고
    • High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells
    • Jäger V, Büssow K, Wagner A, Weber S, Hust M, Frenzel A, et al. High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells. BMC Biotechnol. 2013;13:52.
    • (2013) BMC Biotechnol , vol.13 , pp. 52
    • Jäger, V.1    Büssow, K.2    Wagner, A.3    Weber, S.4    Hust, M.5    Frenzel, A.6
  • 46
    • 24644458809 scopus 로고    scopus 로고
    • Aβ42 immunization in Alzheimer's disease generates Aβ N-terminal antibodies
    • Lee M, Bard F, Johnson-Wood K, Lee C, Hu K, Griffith SG, et al. Aβ42 immunization in Alzheimer's disease generates Aβ N-terminal antibodies. Ann Neurol. 2005;58:430-5.
    • (2005) Ann Neurol , vol.58 , pp. 430-435
    • Lee, M.1    Bard, F.2    Johnson-Wood, K.3    Lee, C.4    Hu, K.5    Griffith, S.G.6
  • 47
    • 3042692322 scopus 로고    scopus 로고
    • Alzheimer's disease Aβ vaccine reduces central nervous system Aβ levels in a non-human primate, the Caribbean Vervet
    • Lemere CA, Beierschmitt A, Iglesias M, Spooner ET, Bloom JK, Leverone JF, et al. Alzheimer's disease Aβ vaccine reduces central nervous system Aβ levels in a non-human primate, the Caribbean Vervet. Am J Pathol. 2004;165:283-97.
    • (2004) Am J Pathol , vol.165 , pp. 283-297
    • Lemere, C.A.1    Beierschmitt, A.2    Iglesias, M.3    Spooner, E.T.4    Bloom, J.K.5    Leverone, J.F.6
  • 48
    • 77954957153 scopus 로고    scopus 로고
    • Linear and conformation specific antibodies in aged beagles after prolonged vaccination with aggregated Abeta
    • Vasilevko V, Pop V, Kim HJ, Saing T, Glabe CC, Milton S, et al. Linear and conformation specific antibodies in aged beagles after prolonged vaccination with aggregated Abeta. Neurobiol Dis. 2010;39:301-10.
    • (2010) Neurobiol Dis , vol.39 , pp. 301-310
    • Vasilevko, V.1    Pop, V.2    Kim, H.J.3    Saing, T.4    Glabe, C.C.5    Milton, S.6
  • 49
    • 0037452779 scopus 로고    scopus 로고
    • Epitope and isotype specificities of antibodies to beta -amyloid peptide for protection against Alzheimer's disease-like neuropathology
    • Bard F, Barbour R, Cannon C, Carretto R, Fox M, Games D, et al. Epitope and isotype specificities of antibodies to beta -amyloid peptide for protection against Alzheimer's disease-like neuropathology. Proc Natl Acad Sci U S A. 2003;100:2023-8.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2023-2028
    • Bard, F.1    Barbour, R.2    Cannon, C.3    Carretto, R.4    Fox, M.5    Games, D.6
  • 52
    • 84875455396 scopus 로고    scopus 로고
    • Characterization of a single-chain variable fragment recognizing a linear epitope of Aβ: a biotechnical tool for studies on Alzheimer's disease?
    • Dornieden S, Müller-Schiffmann A, Sticht H, Jiang N, Cinar Y, Wördehoff M, et al. Characterization of a single-chain variable fragment recognizing a linear epitope of Aβ: a biotechnical tool for studies on Alzheimer's disease? PLoS ONE. 2013;8:e59820.
    • (2013) PLoS ONE , vol.8
    • Dornieden, S.1    Müller-Schiffmann, A.2    Sticht, H.3    Jiang, N.4    Cinar, Y.5    Wördehoff, M.6
  • 54
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N, Hartmann T, Pantel J, Schröder J, Zerfass R, Förstl H, et al. Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J Biol Chem. 1996;271:22908-14.
    • (1996) J Biol Chem , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schröder, J.4    Zerfass, R.5    Förstl, H.6
  • 55
    • 0031020909 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease
    • Johnson-Wood K, Lee M, Motter R, Hu K, Gordon G, Barbour R, et al. Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease. Proc Natl Acad Sci U S A. 1997;94:1550-5.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1550-1555
    • Johnson-Wood, K.1    Lee, M.2    Motter, R.3    Hu, K.4    Gordon, G.5    Barbour, R.6
  • 56
    • 59649110455 scopus 로고    scopus 로고
    • Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils
    • Meinhardt J, Sachse C, Hortschansky P, Grigorieff N, Fändrich M. Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol. 2009;386(3):869-77.
    • (2009) J Mol Biol , vol.386 , Issue.3 , pp. 869-877
    • Meinhardt, J.1    Sachse, C.2    Hortschansky, P.3    Grigorieff, N.4    Fändrich, M.5
  • 57
    • 37649019187 scopus 로고    scopus 로고
    • Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils
    • Habicht G, Haupt C, Friedrich RP, Hortschansky P, Sachse C, Meinhardt J, et al. Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils. Proc Natl Acad Sci. 2007;104:19232-7.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 19232-19237
    • Habicht, G.1    Haupt, C.2    Friedrich, R.P.3    Hortschansky, P.4    Sachse, C.5    Meinhardt, J.6
  • 58
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, Necula M, et al. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener. 2007;2:18.
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5    Necula, M.6
  • 59
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R. Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci. 2002;99:1485-90.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 60
    • 0034633632 scopus 로고    scopus 로고
    • Immunization against Alzheimer's β-amyloid plaques via EFRH phage administration
    • Frenkel D, Katz O, Solomon B. Immunization against Alzheimer's β-amyloid plaques via EFRH phage administration. Proc Natl Acad Sci U S A. 2000;97:11455-9.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11455-11459
    • Frenkel, D.1    Katz, O.2    Solomon, B.3
  • 61
    • 0345862278 scopus 로고    scopus 로고
    • Effect of different Anti-Aβ antibodies on Aβ Fibrillogenesis as assessed by atomic force microscopy
    • Legleiter J, Czilli DL, Gitter B, DeMattos RB, Holtzman DM, Kowalewski T. Effect of different Anti-Aβ antibodies on Aβ Fibrillogenesis as assessed by atomic force microscopy. J Mol Biol. 2004;335:997-1006.
    • (2004) J Mol Biol , vol.335 , pp. 997-1006
    • Legleiter, J.1    Czilli, D.L.2    Gitter, B.3    DeMattos, R.B.4    Holtzman, D.M.5    Kowalewski, T.6
  • 62
    • 0036852750 scopus 로고    scopus 로고
    • Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4-10 and inhibit cytotoxicity and fibrillogenesis
    • McLaurin J, Cecal R, Kierstead ME, Tian X, Phinney AL, Manea M, et al. Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4-10 and inhibit cytotoxicity and fibrillogenesis. Nat Med. 2002;8:1263-9.
    • (2002) Nat Med , vol.8 , pp. 1263-1269
    • McLaurin, J.1    Cecal, R.2    Kierstead, M.E.3    Tian, X.4    Phinney, A.L.5    Manea, M.6
  • 63
    • 60749093075 scopus 로고    scopus 로고
    • Engineered antibody intervention strategies for Alzheimer's disease and related dementias by targeting amyloid and toxic oligomers
    • Robert R, Dolezal O, Waddington L, Hattarki MK, Cappai R, Masters CL, et al. Engineered antibody intervention strategies for Alzheimer's disease and related dementias by targeting amyloid and toxic oligomers. Protein Eng Des Sel. 2009;22:199-208.
    • (2009) Protein Eng Des Sel , vol.22 , pp. 199-208
    • Robert, R.1    Dolezal, O.2    Waddington, L.3    Hattarki, M.K.4    Cappai, R.5    Masters, C.L.6
  • 64
    • 0030058382 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide
    • Solomon B, Koppel R, Hanan E, Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide. Proc Natl Acad Sci U S A. 1996;93:452-5.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 65
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K. Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. J Mol Biol. 1992;228:460-73.
    • (1992) J Mol Biol , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 66
    • 84877254025 scopus 로고    scopus 로고
    • Passive anti-amyloid immunotherapy in Alzheimer's disease: What are the most promising targets?
    • Moreth J, Mavoungou C, Schindowski K. Passive anti-amyloid immunotherapy in Alzheimer's disease: What are the most promising targets? Immun Ageing A. 2013;10:18.
    • (2013) Immun Ageing A , vol.10 , pp. 18
    • Moreth, J.1    Mavoungou, C.2    Schindowski, K.3
  • 67
    • 84887973227 scopus 로고    scopus 로고
    • Treating Alzheimer's disease with monoclonal antibodies: current status and outlook for the future
    • Prins ND, Scheltens P. Treating Alzheimer's disease with monoclonal antibodies: current status and outlook for the future. Alzheimers Res Ther. 2013;5:56.
    • (2013) Alzheimers Res Ther , vol.5 , pp. 56
    • Prins, N.D.1    Scheltens, P.2
  • 69
    • 57149145222 scopus 로고    scopus 로고
    • The ratio of monomeric to aggregated forms of Aβ40 and Aβ42 is an important determinant of Amyloid-β aggregation, fibrillogenesis, and toxicity
    • Jan A, Gokce O, Luthi-Carter R, Lashuel HA. The ratio of monomeric to aggregated forms of Aβ40 and Aβ42 is an important determinant of Amyloid-β aggregation, fibrillogenesis, and toxicity. J Biol Chem. 2008;283:28176-89.
    • (2008) J Biol Chem , vol.283 , pp. 28176-28189
    • Jan, A.1    Gokce, O.2    Luthi-Carter, R.3    Lashuel, H.A.4
  • 70
    • 84935913711 scopus 로고
    • USDA Animal Welfare Act (AWA). 7 U.S.C. 2131 et seq., as amended and Health Research Extension Act of 1985 ('"Animals in Research"')
    • "USDA Animal Welfare Act (AWA). 7 U.S.C. 2131 et seq., as amended and Health Research Extension Act of 1985 ('"Animals in Research"'). 1985."
    • (1985)
  • 71
    • 15644372038 scopus 로고    scopus 로고
    • Guide for the Care and Use of Laboratory Animals.
    • 8th ed. Washington (DC): National Academies Press (US)
    • National Research Council (US) Committee for the Update of the Guide for the Care and Use of Laboratory Animals. Guide for the Care and Use of Laboratory Animals. 8th ed. Washington (DC): National Academies Press (US); 2011.
    • (2011)
  • 72
    • 77949904546 scopus 로고    scopus 로고
    • Obtention and engineering of non-human primate (NHP) antibodies for therapeutics
    • Pelat T, Hust M, Thullier P. Obtention and engineering of non-human primate (NHP) antibodies for therapeutics. Mini Rev Med Chem. 2009;9:1633-8.
    • (2009) Mini Rev Med Chem , vol.9 , pp. 1633-1638
    • Pelat, T.1    Hust, M.2    Thullier, P.3
  • 73
    • 84931264473 scopus 로고    scopus 로고
    • Construction of human antibody gene libraries and selection of antibodies by phage display. Methods Mol. Biol
    • Frenzel A, Kügler J, Wilke S, Schirrmann T, Hust M. Construction of human antibody gene libraries and selection of antibodies by phage display. Methods Mol. Biol. Clifton NJ. 2014;1060:215-43.
    • (2014) Clifton NJ , vol.1060 , pp. 215-243
    • Frenzel, A.1    Kügler, J.2    Wilke, S.3    Schirrmann, T.4    Hust, M.5
  • 75
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher Y, Perret S, Kamen A. High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 2002;30:E9.
    • (2002) Nucleic Acids Res , vol.30 , pp. E9
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 76
    • 0026656122 scopus 로고
    • Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank R. Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron. 1992;48:9217-32.
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 77
    • 0036721834 scopus 로고    scopus 로고
    • The SPOT-synthesis technique: synthetic peptide arrays on membrane supports-principles and applications
    • Frank R. The SPOT-synthesis technique: synthetic peptide arrays on membrane supports-principles and applications. J Immunol Methods. 2002;267:13-26.
    • (2002) J Immunol Methods , vol.267 , pp. 13-26
    • Frank, R.1
  • 78
    • 32344451179 scopus 로고    scopus 로고
    • The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding
    • Tomaselli S, Esposito V, Vangone P, van Nuland NAJ, Bonvin AMJJ, Guerrini R, et al. The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding. Chembiochem Eur J Chem Biol. 2006;7:257-67.
    • (2006) Chembiochem Eur J Chem Biol , vol.7 , pp. 257-267
    • Tomaselli, S.1    Esposito, V.2    Vangone, P.3    Nuland, N.A.J.4    Bonvin, A.M.J.J.5    Guerrini, R.6


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