메뉴 건너뛰기




Volumn 8, Issue 33, 2013, Pages 3107-3115

Construction of human Fab library and screening of a single-domain antibody of amyloid-beta 42 oligomers

Author keywords

Alpha synuclein; Alzheimer's disease; Amyloid beta; Antibody library construction; Grants supported paper; Humanized antibody; Immunotherapy; Neural regeneration; Neuroregeneration; Oligomer; Parkinson's disease; Phage display; Single domain antibody

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN [1-42]; IMMUNOGLOBULIN F (AB) FRAGMENT; UNCLASSIFIED DRUG;

EID: 84889873963     PISSN: 16735374     EISSN: 18767958     Source Type: Journal    
DOI: 10.3969/j.issn.1673-5374.2013.33.004     Document Type: Article
Times cited : (5)

References (29)
  • 1
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol. 2007;8(2):101-12.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 2
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein WL, Krafft GA, Finch CE. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 2001;24(4):219-224.
    • (2001) Trends Neurosci , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 3
    • 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, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 2002; 416(6880):535-539.
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 4
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y, Chang L, Viola KL, et al. Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci U S A. 2003;100(18):10417-10422.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.18 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3
  • 5
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary JP, Walsh DM, Hofmeister JJ, et al. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci. 2005;8(1):79-84.
    • (2005) Nat Neurosci , vol.8 , Issue.1 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3
  • 6
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L, et al. A specific amyloid-beta protein assembly in the brain impairs memory. Nature. 2006;440(7082):352-357.
    • (2006) Nature , vol.440 , Issue.7082 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 7
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH, et al. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med. 2008;14(8): 837-842.
    • (2008) Nat Med , vol.14 , Issue.8 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3
  • 8
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature. 1999;400(6740):173-177.
    • (1999) Nature , vol.400 , Issue.6740 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 9
    • 77955924937 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease
    • Solomon B, Frenkel D. Immunotherapy for Alzheimer's disease. Neuropharmacology. 2010;59(4-5):303-309.
    • (2010) Neuropharmacology , vol.59 , Issue.4-5 , pp. 303-309
    • Solomon, B.1    Frenkel, D.2
  • 10
    • 0036127580 scopus 로고    scopus 로고
    • Set back to Alzheimer vaccine studies
    • Birmingham K, Frantz S. Set back to Alzheimer vaccine studies. Nat Med. 2002;8(3):199-200.
    • (2002) Nat Med , vol.8 , Issue.3 , pp. 199-200
    • Birmingham, K.1    Frantz, S.2
  • 11
    • 0036780877 scopus 로고    scopus 로고
    • Amyloid-beta immunotherapy for Alzheimer's disease: The end of the beginning
    • Schenk D. Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning. Nat Rev Neurosci. 2002;3(10):824-828.
    • (2002) Nat Rev Neurosci , vol.3 , Issue.10 , pp. 824-828
    • Schenk, D.1
  • 12
    • 0038100154 scopus 로고    scopus 로고
    • Antibodies against beta-amyloid slow cognitive decline in Alzheimer's disease
    • Hock C, Konietzko U, Streffer JR, et al. Antibodies against beta-amyloid slow cognitive decline in Alzheimer's disease. Neuron. 2003;38(4):547-554.
    • (2003) Neuron , vol.38 , Issue.4 , pp. 547-554
    • Hock, C.1    Konietzko, U.2    Streffer, J.R.3
  • 13
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo JM, Gilman S, Dartigues JF, et al. Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology. 2003;61(1):46-54.
    • (2003) Neurology , vol.61 , Issue.1 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3
  • 14
    • 33646384419 scopus 로고    scopus 로고
    • Immunology and immunotherapy of Alzheimer's disease
    • Weiner HL, Frenkel D. Immunology and immunotherapy of Alzheimer's disease. Nat Rev Immunol. 2006;6(5):404-416.
    • (2006) Nat Rev Immunol , vol.6 , Issue.5 , pp. 404-416
    • Weiner, H.L.1    Frenkel, D.2
  • 15
    • 0027963484 scopus 로고
    • Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs
    • Green LL, Hardy MC, Maynard-Currie CE, et al. Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs. Nat Genet. 1994;7(1):13-21.
    • (1994) Nat Genet , vol.7 , Issue.1 , pp. 13-21
    • Green, L.L.1    Hardy, M.C.2    Maynard-Currie, C.E.3
  • 16
    • 0036900286 scopus 로고    scopus 로고
    • Antibody discovery: The use of transgenic mice to generate human monoclonal antibo dies for therapeutics
    • Kellermann SA, Green LL. Antibody discovery: the use of transgenic mice to generate human monoclonal antibo dies for therapeutics. Curr Opin Biotechnol. 2002;13(6): 593-597.
    • (2002) Curr Opin Biotechnol , vol.13 , Issue.6 , pp. 593-597
    • Kellermann, S.A.1    Green, L.L.2
  • 17
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P, Hudson PJ. Engineered antibody fragments and the rise of single domains. Nat Biotechnol. 2005; 23(9):1126-1136.
    • (2005) Nat Biotechnol , vol.23 , Issue.9 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 18
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 2003;300(5618):486-489.
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 19
    • 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, 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
  • 20
    • 56249092747 scopus 로고    scopus 로고
    • Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells
    • Zameer A, Kasturirangan S, Emadi S, et al. Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells. J Mol Biol. 2008;384(4):917-928.
    • (2008) J Mol Biol , vol.384 , Issue.4 , pp. 917-928
    • Zameer, A.1    Kasturirangan, S.2    Emadi, S.3
  • 21
    • 58649093288 scopus 로고    scopus 로고
    • Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers
    • Wang XP, Zhang JH, Wang YJ, et al. Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers. FEBS Lett. 2009;583(3):579-584.
    • (2009) FEBS Lett , vol.583 , Issue.3 , pp. 579-584
    • Wang, X.P.1    Zhang, J.H.2    Wang, Y.J.3
  • 22
    • 58249104047 scopus 로고    scopus 로고
    • Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent Abeta-induced neurotoxicity and inhibit fibril formation
    • Lafaye P, Achour I, England P, et al. Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent Abeta-induced neurotoxicity and inhibit fibril formation. Mol Immunol. 2009;46(4):695-704.
    • (2009) Mol Immunol , vol.46 , Issue.4 , pp. 695-704
    • Lafaye, P.1    Achour, I.2    England, P.3
  • 23
    • 37649019187 scopus 로고    scopus 로고
    • Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils
    • Habicht G, Haupt C, Friedrich RP, et al. Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils. Proc Natl Acad Sci U S A. 2007;104(49):19232-19237.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.49 , pp. 19232-19237
    • Habicht, G.1    Haupt, C.2    Friedrich, R.P.3
  • 24
    • 77953540108 scopus 로고    scopus 로고
    • Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries
    • Medecigo M, Manoutcharian K, Vasilevko V, et al. Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries. J Neuroimmunol. 223;(1-2):104-114.
    • J Neuroimmunol , vol.223 , Issue.1-2 , pp. 104-114
    • Medecigo, M.1    Manoutcharian, K.2    Vasilevko, V.3
  • 25
    • 0023096246 scopus 로고
    • Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein
    • Hendershot L, Bole D, Kohler G, et al. Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. J Cell Biol. 1987;104(3): 761-767.
    • (1987) J Cell Biol , vol.104 , Issue.3 , pp. 761-767
    • Hendershot, L.1    Bole, D.2    Kohler, G.3
  • 26
    • 0026555251 scopus 로고
    • Franklin's disease: Ig gamma 2 H chain mutant BUR
    • Prelli F, Frangione B. Franklin's disease: Ig gamma 2 H chain mutant BUR. J Immunol. 1992;148(3):949-952.
    • (1992) J Immunol , vol.148 , Issue.3 , pp. 949-952
    • Prelli, F.1    Frangione, B.2
  • 27
    • 67749122581 scopus 로고    scopus 로고
    • Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimer's disease
    • Britschgi M, Olin CE, Johns HT, et al. Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimer's disease. Proc Natl Acad Sci U S A. 2009;106(29): 12145-12150.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.29 , pp. 12145-12150
    • Britschgi, M.1    Olin, C.E.2    Johns, H.T.3
  • 28
    • 0013783533 scopus 로고
    • Amino acid sequence studies with Bence-Jones proteins
    • Hilschmann N, Craig LC. Amino acid sequence studies with Bence-Jones proteins. Proc Natl Acad Sci U S A. 1965;53(6):1403-1409.
    • (1965) Proc Natl Acad Sci U S A , vol.53 , Issue.6 , pp. 1403-1409
    • Hilschmann, N.1    Craig, L.C.2
  • 29
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward ES, Gussow D, Griffiths AD, et al. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature. 1989;341(6242): 544-546.
    • (1989) Nature , vol.341 , Issue.6242 , pp. 544-546
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.