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Volumn 2, Issue 8, 2002, Pages 907-917

Immunological approaches as therapy for Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid plaques; Anti aggregating antibodies; Conformation; Immunisation

Indexed keywords

ALZHEIMER DISEASE VACCINE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-30]; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; FC RECEPTOR; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 10D5; MONOCLONAL ANTIBODY 266; MONOCLONAL ANTIBODY 3D6; POLYCLONAL ANTIBODY; UNCLASSIFIED DRUG;

EID: 0036914592     PISSN: 14712598     EISSN: None     Source Type: Journal    
DOI: 10.1517/14712598.2.8.907     Document Type: Review
Times cited : (16)

References (85)
  • 1
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell RW, Lomas DA: Conformational disease. Lancet (1997) 35:134-138.
    • (1997) Lancet , vol.35 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 2
    • 0033621398 scopus 로고    scopus 로고
    • Aberrant protein deposition and neurological disease
    • Kaytor MD, Warren ST: Aberrant protein deposition and neurological disease. J. Biol. Chem. (1999) 274:37507-37510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37507-37510
    • Kaytor, M.D.1    Warren, S.T.2
  • 3
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • Wetzel R: Mutations and off-pathway aggregation of proteins. Trends Biotechnol. (1994) 12:193-198.
    • (1994) Trends Biotechnol. , vol.12 , pp. 193-198
    • Wetzel, R.1
  • 4
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly JW: Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases. Structure (1997) 5:595-600.
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 6
    • 0019970006 scopus 로고
    • Computer graphics in drug design: Molecular modeling of thyroid hormone-prealbumin interactions
    • Blaney JM, Jorgensen EC, Connolly ML et al.: Computer graphics in drug design: Molecular modeling of thyroid hormone-prealbumin interactions. J. Med. Chem. (1982) 25:785-790.
    • (1982) J. Med. Chem. , vol.25 , pp. 785-790
    • Blaney, J.M.1    Jorgensen, E.C.2    Connolly, M.L.3
  • 7
    • 0018793861 scopus 로고
    • Temperature-dependent x-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder H, Petsko GA, Tsernoglou D: Temperature-dependent x-ray diffraction as a probe of protein structural dynamics. Nature (1979) 280:558-563.
    • (1979) Nature , vol.280 , pp. 558-563
    • Frauenfelder, H.1    Petsko, G.A.2    Tsernoglou, D.3
  • 8
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus M, Petsko GA: Molecular dynamics simulations in biology. Nature (1990) 347:632-639.
    • (1990) Nature , vol.347 , pp. 632-639
    • Karplus, M.1    Petsko, G.A.2
  • 9
    • 0026233196 scopus 로고
    • Thermostabilization of Carboxypeptidase A by interaction with its monoclonal antibodies
    • Solomon B, Balas N: Thermostabilization of Carboxypeptidase A by interaction with its monoclonal antibodies. Biotechnol. and Appl. Biochem. (1991) 14:202-211.
    • (1991) Biotechnol. and Appl. Biochem. , vol.14 , pp. 202-211
    • Solomon, B.1    Balas, N.2
  • 10
    • 0029887388 scopus 로고    scopus 로고
    • Effect of monoclonal antibodies in preventing Carboxypeptidase A aggregation
    • Katzav T, Hanan E, Solomon B: Effect of monoclonal antibodies in preventing Carboxypeptidase A aggregation. Appl. Biochem. Biotechnol. (1996) 2:227-230.
    • (1996) Appl. Biochem. Biotechnol. , vol.2 , pp. 227-230
    • Katzav, T.1    Hanan, E.2    Solomon, B.3
  • 11
    • 0004381305 scopus 로고
    • Partly native epitopes are already present on early intermediates in the folding of tryptophan synthase
    • Blond S, Goldberg M: Partly native epitopes are already present on early intermediates in the folding of tryptophan synthase. Proc. Natl. Acad. Sci. USA (1987) 84:1147-1151.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1147-1151
    • Blond, S.1    Goldberg, M.2
  • 12
    • 0026527693 scopus 로고
    • Antibody assisted protein refolding
    • Carlson JD, Yarmush ML: Antibody assisted protein refolding. Biol Technology (1992) 10:86-91.
    • (1992) Biol Technology , vol.10 , pp. 86-91
    • Carlson, J.D.1    Yarmush, M.L.2
  • 13
    • 0029201345 scopus 로고
    • Chaperone-like effect of monoclonal antibodies on refolding of heat-denatured Carboxypeptidase A
    • Solomon B, Schwartz F: Chaperone-like effect of monoclonal antibodies on refolding of heat-denatured Carboxypeptidase A. J. Mol. Recognit. (1995) 8:72-76.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 72-76
    • Solomon, B.1    Schwartz, F.2
  • 14
    • 0024425004 scopus 로고
    • The alpha-lyric protease pro-region does not require a physical linkage to activate the protease domain in vivo
    • Silen JL, Agard DA: The alpha-lyric protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature (1989) 341:462-464.
    • (1989) Nature , vol.341 , pp. 462-464
    • Silen, J.L.1    Agard, D.A.2
  • 15
    • 0035209308 scopus 로고    scopus 로고
    • Annual incidence of Alzheimer's disease in the United States projected to the years 2000 through 2050
    • Hebert LE, Beckett LA, Scherr PA, Evans DA: Annual incidence of Alzheimer's disease in the United States projected to the years 2000 through 2050. Alzheimer Dis. Assoc. Disord. (2001)15:169-173.
    • (2001) Alzheimer Dis. Assoc. Disord. , vol.15 , pp. 169-173
    • Hebert, L.E.1    Beckett, L.A.2    Scherr, P.A.3    Evans, D.A.4
  • 16
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe DJ: The molecular pathology of Alzheimer's disease. Neuron (1991) 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 17
    • 0028986916 scopus 로고
    • β-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J, Lorenzo A, Yeh J, Yankner BA: β-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron (1995) 14:879-888. Evidence of involvement of amyloid plaques in neurofibrillary tangle formation.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 18
    • 0028965635 scopus 로고
    • Somatodentritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz J, Probst A, Spillantini MG et al.: Somatodentritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. (1995) 14:1304-1313. Evidence of involvement of amyloid plaques in neurofibrillary tangles formation.
    • (1995) EMBO J. , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3
  • 19
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL et al.: Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science (2001) 293:1487-1491. Evidence of involvement of amytoid plaques in neurofibrillary tangle formation.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 20
    • 0032150877 scopus 로고    scopus 로고
    • Genetic dissection of Alzheimer's disease and related dementias: Amyloid and its relationship to tau
    • Hardy J, Duff K. & Hardy KG, Perez-Tur J, Hutton M: Genetic dissection of Alzheimer's disease and related dementias: Amyloid and its relationship to tau. Nat. Neurosci. (1998) 1:355-358. Evidence of involvement of amyloid plaques in neurofibrillary tangle formation.
    • (1998) Nat. Neurosci. , vol.1 , pp. 355-358
    • Hardy, J.1    Duff, K.2    Hardy, K.G.3    Perez-Tur, J.4    Hutton, M.5
  • 21
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J, Allsop D: Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. (1991) 12:383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 22
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β protein and the genetics of Alzheimer's disease
    • Selkoe DJ: Amyloid β protein and the genetics of Alzheimer's disease. J. Biol. Chem. (1996) 271:18295-18298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 23
    • 0032150877 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J: Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. (1998) 1:355-358.
    • (1998) Trends Neurosci. , vol.1 , pp. 355-358
    • Hardy, J.1
  • 24
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ: The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science (2002) 297:353-356. This is an excellent updated review which provides comprehensive and timely information on therapeutics based on amyloid hypothesis.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 25
    • 0026075602 scopus 로고
    • Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene
    • Chartier-Harlin MC, Crawford F, Houlden H et al.: Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene. Nature (1991) 353:844-846.
    • (1991) Nature , vol.353 , pp. 844-846
    • Chartier-Harlin, M.C.1    Crawford, F.2    Houlden, H.3
  • 26
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M et al.: Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature (1991) 349:704-706.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 27
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of betaamyloid
    • Mullan M, Crawford F, Axelman K et al.: A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of betaamyloid. Nat. Genet. (1992a) 1:345-347.
    • (1992) Nat. Genet. , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 28
    • 0027024651 scopus 로고
    • A locus for familial early-onset Alzheimer's disease on the long arm of chromosome 15, proximal to the alpha-1-antichymotrypsin gene
    • Mullan M, Houlden H, Windelspecht M et al.: A locus for familial early-onset Alzheimer's disease on the long arm of chromosome 15, proximal to the alpha-1-antichymotrypsin gene. Nat. Genet. (1992b) 2:340-342.
    • (1992) Nat. Genet. , vol.2 , pp. 340-342
    • Mullan, M.1    Houlden, H.2    Windelspecht, M.3
  • 29
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad E, Wasco W, Poorkaj P et al.: Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science (1995) 269:973-977.
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 30
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset Alzheimer's disease
    • Sherrington R, Rogaev EI, Liang Y et al.: Cloning of a gene bearing missense mutations in early-onset Alzheimer's disease. Nature (1995) 375:754-760.
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 31
    • 0001772459 scopus 로고    scopus 로고
    • β-amyloid and treatment opportunities for Alzheimer's disease
    • Sabbagh MN, Galasko D, Thal LJ: β-amyloid and treatment opportunities for Alzheimer's disease. Alzheimer's Dis. Rev. (1998) 3:1-19.
    • (1998) Alzheimer's Dis. Rev. , vol.3 , pp. 1-19
    • Sabbagh, M.N.1    Galasko, D.2    Thal, L.J.3
  • 32
    • 0029895147 scopus 로고    scopus 로고
    • Brain amyloid - A physicochemical perspective
    • Maggio JE, Mantyh PW: Brain amyloid - A physicochemical perspective. Brain Pathol. (1996) 6:147-162. This study suggests in vitro modulation of β-amyloid formation by various external factors.
    • (1996) Brain Pathol. , vol.6 , pp. 147-162
    • Maggio, J.E.1    Mantyh, P.W.2
  • 33
    • 0029015766 scopus 로고
    • pH-dependent conformations of the amyloid β (1-28) peptide fragment explored using molecular dynamics
    • Kirshenbaum K, Daggett V: pH-dependent conformations of the amyloid β (1-28) peptide fragment explored using molecular dynamics. Biochemistry (1995) 34:7629-7639.
    • (1995) Biochemistry , vol.34 , pp. 7629-7639
    • Kirshenbaum, K.1    Daggett, V.2
  • 34
    • 0025779179 scopus 로고
    • Solution structures of β-peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow CJ, Zagorski MG: Solution structures of β-peptide and its constituent fragments: Relation to amyloid deposition. Science (1991) 253:179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 35
    • 0028980362 scopus 로고
    • The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto C, Castano EM, Frangione B, Inestrosa, NC: The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. (1995) 270:3063-3067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 36
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation
    • Soto C, Kindy MS, Baumann M, Frangione B: Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem. Biophys. Res. Commun. (1996) 226(3):672-680.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , Issue.3 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 37
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A, Yankner BA: Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. USA (1994) 1:12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.1 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 38
    • 0029034927 scopus 로고
    • Aggregation state and neurotoxic properties of Alzheimer beta-amyloid peptide
    • Howlett, DR, Jennings KH, Lee DC et al.: Aggregation state and neurotoxic properties of Alzheimer beta-amyloid peptide. Neurodegeneration (1995) 4:23-32.
    • (1995) Neurodegeneration , vol.4 , pp. 23-32
    • Howlett, D.R.1    Jennings, K.H.2    Lee, D.C.3
  • 39
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • Wisniewski T, Castano EM, Golabek A, Vogel T, Frangione B: Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am. J. Pathol. (1994) 145(5):1030-1035.
    • (1994) Am. J. Pathol. , vol.145 , Issue.5 , pp. 1030-1035
    • Wisniewski, T.1    Castano, E.M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 40
    • 0030058382 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer's β-amyloid peptide
    • Solomon B, Koppel R, Hanan E, Katzav T: Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer's β-amyloid peptide. Proc. Natl. Acad. Sci. USA (1996) 93(1):452-455. This is the first demonstration that mAbs can prevent amyloid formation.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.1 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 41
    • 0030971789 scopus 로고    scopus 로고
    • Disaggregation of Alzheimer β-amyloid by site-directed mAb
    • Solomon B, Koppel R, Frankel D, Hanan-Aharon E: Disaggregation of Alzheimer β-amyloid by site-directed mAb. Proc. Natl. Acad. Sci. USA (1997) 94:4109-4112. This is the first demonstration that site-directed antibodies dissolve already formed amyloid fibrils.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4109-4112
    • Solomon, B.1    Koppel, R.2    Frankel, D.3    Hanan-Aharon, E.4
  • 42
    • 0000650806 scopus 로고    scopus 로고
    • Protective effect of monoclonal antibodies against Alzheimer's β-amyloid aggregation
    • Hanan E, Solomon B: Protective effect of monoclonal antibodies against Alzheimer's β-amyloid aggregation. Amyloid: Int. J. Exp. Clin. Invest. (1996) 3:130-133.
    • (1996) Amyloid: Int. J. Exp. Clin. Invest. , vol.3 , pp. 130-133
    • Hanan, E.1    Solomon, B.2
  • 43
    • 0034237142 scopus 로고    scopus 로고
    • Modulation of Alzheimer's β-amyloid neurotoxicity by site-directed single-chain antibody
    • Frenkel D, Solomon B, Benhar I: Modulation of Alzheimer's β-amyloid neurotoxicity by site-directed single-chain antibody. J. Neuroimmunol. (2000) 106:23-31. Antibodies devoid of Fc region exhibit anti-aggregating properties preventing Aβ neurotoxicity.
    • (2000) J. Neuroimmunol. , vol.106 , pp. 23-31
    • Frenkel, D.1    Solomon, B.2    Benhar, I.3
  • 44
    • 0032145617 scopus 로고    scopus 로고
    • N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregating antibodies
    • Frenkel D, Balass M, Solomon B: N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregating antibodies. J. Neuroimmunol. (1998) 8:85-90.
    • (1998) J. Neuroimmunol. , vol.8 , pp. 85-90
    • Frenkel, D.1    Balass, M.2    Solomon, B.3
  • 45
    • 0033103657 scopus 로고    scopus 로고
    • High affinity binding of monoclonal antibodies to the sequential epitope EFRH of β-amyloid peptide is essential for modulation of fibrillar aggregation
    • Frenkel D, Balass M, KachalskyKatzir E, Solomon B: High affinity binding of monoclonal antibodies to the sequential epitope EFRH of β-amyloid peptide is essential for modulation of fibrillar aggregation. J. Neuroimmunol. (1999) 95:136-142. The study emphasises the key role of EFRH sequence in modulation of AβP conformation.
    • (1999) J. Neuroimmunol. , vol.95 , pp. 136-142
    • Frenkel, D.1    Balass, M.2    KachalskyKatzir, E.3    Solomon, B.4
  • 46
    • 0034014950 scopus 로고    scopus 로고
    • Single and multiple transgenic mice as models for Alzheimer's disease
    • Van Leuven F: Single and multiple transgenic mice as models for Alzheimer's disease. Prog. Neurobiol. (2000) 61(3):305-312.
    • (2000) Prog. Neurobiol. , vol.61 , Issue.3 , pp. 305-312
    • Van Leuven, F.1
  • 47
    • 0032930444 scopus 로고    scopus 로고
    • Inhibition of β-amyloid formation as a therapeutic strategy
    • Moore CL, Wolfe MS: Inhibition of β-amyloid formation as a therapeutic strategy. Expert Opin. Ther. Patents (1999) 9(2):135-146.
    • (1999) Expert Opin. Ther. Patents , vol.9 , Issue.2 , pp. 135-146
    • Moore, C.L.1    Wolfe, M.S.2
  • 48
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein
    • Games D, Adams D, Alessandrini R et al.: Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein. Nature (1995) 373:523-527.
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 49
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer's disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W et al.: Immunization with amyloid-β attenuates Alzheimer's disease-like pathology in the PDAPP mouse. Nature (1999) 400:173-177. First in vivo demonstration that anti-β-amyloid antibodies reduce amyloid plaque in transgenic mice.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 50
    • 0033801852 scopus 로고    scopus 로고
    • Nasal administration of amyloid-beta peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease
    • Weiner HL, Lemere CA, Maron R et al.: Nasal administration of amyloid-beta peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease. Ann. Neurol. (2000) 48:567-579.
    • (2000) Ann. Neurol. , vol.48 , pp. 567-579
    • Weiner, H.L.1    Lemere, C.A.2    Maron, R.3
  • 51
    • 0034530636 scopus 로고    scopus 로고
    • Nasal A beta treatment induces anti-A beta antibody production and decreases cerebral amyloid burden in PDAPP mice
    • Lemere CA, Maron R, Spooner ET et al.: Nasal A beta treatment induces anti-A beta antibody production and decreases cerebral amyloid burden in PDAPP mice. Ann. NY Acad. Sci. (2000) 920:328-331.
    • (2000) Ann. NY Acad. Sci. , vol.920 , pp. 328-331
    • Lemere, C.A.1    Maron, R.2    Spooner, E.T.3
  • 52
    • 0035689690 scopus 로고    scopus 로고
    • Nasal vaccination with β-amyloid peptide for the treatment of Alzheimer's disease
    • Lemere CA, Maron R, Selkoe DJ, Weiner H: Nasal vaccination with β-amyloid peptide for the treatment of Alzheimer's disease. DNA Cell Biol. (2001) 20:705-711.
    • (2001) DNA Cell Biol. , vol.20 , pp. 705-711
    • Lemere, C.A.1    Maron, R.2    Selkoe, D.J.3    Weiner, H.4
  • 53
    • 0035471222 scopus 로고    scopus 로고
    • Immunization for Alzheimer's disease: Yet closer to clinical trials
    • Gurwitz D: Immunization for Alzheimer's disease: Yet closer to clinical trials. Trends Immunol. (2001) 22(10):542-543.
    • (2001) Trends Immunol. , vol.22 , Issue.10 , pp. 542-543
    • Gurwitz, D.1
  • 54
    • 0034884382 scopus 로고    scopus 로고
    • Immunization with a nontoxic/nonfibrillar amyloid-beta homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice
    • Sigurdsson EM, Scholtzova H, Mehta PD, Frangione B, Wisniewski T: Immunization with a nontoxic/nonfibrillar amyloid-beta homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice. Am. J. Pathol. (2001) 159:439-447.
    • (2001) Am. J. Pathol. , vol.159 , pp. 439-447
    • Sigurdsson, E.M.1    Scholtzova, H.2    Mehta, P.D.3    Frangione, B.4    Wisniewski, T.5
  • 55
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • Hsiao K, Chapman P, Nilsen S et al.: Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science (1996) 274:99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 56
    • 0034633632 scopus 로고    scopus 로고
    • Immunization against Alzheimer's beta-amyloid plaques via EFRH phage administration
    • Frenkel D, Katz O, Solomon B: Immunization against Alzheimer's beta-amyloid plaques via EFRH phage administration. Proc. Natl. Acad. Sci. USA (2000) 97:11455-11459.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11455-11459
    • Frenkel, D.1    Katz, O.2    Solomon, B.3
  • 57
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott JK, Smith GP: Searching for peptide ligands with an epitope library. Science (1990) 249:386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 58
    • 0026654781 scopus 로고
    • Discovering peptide ligands using epitope libraries
    • Scott JK: Discovering peptide ligands using epitope libraries. Trends Biochem Sci (1992) 17(7):241-245.
    • (1992) Trends Biochem Sci. , vol.17 , Issue.7 , pp. 241-245
    • Scott, J.K.1
  • 59
    • 0025899542 scopus 로고
    • Multiple display of foreign peptides on a filamentous bacteriophage
    • Greenwood J, Willis EA, Perham NR: Multiple display of foreign peptides on a filamentous bacteriophage. J. Mol. Biol. (1991) 220:821-827.
    • (1991) J. Mol. Biol. , vol.220 , pp. 821-827
    • Greenwood, J.1    Willis, E.A.2    Perham, N.R.3
  • 60
    • 0027287468 scopus 로고
    • Immunological properties of foreign peptides in multiple display on a filamentous bacteriophage
    • Willis EA, Perham NR, Wraith D: Immunological properties of foreign peptides in multiple display on a filamentous bacteriophage. Gene (1993) 128:79-83.
    • (1993) Gene , vol.128 , pp. 79-83
    • Willis, E.A.1    Perham, N.R.2    Wraith, D.3
  • 61
    • 0031582621 scopus 로고    scopus 로고
    • Protective immune responses induced by the immunization of mice with recombinant bacteriophage displaying an epitope of the human respiratory syncytial virus
    • Bastein N, Trude M, Simard C: Protective immune responses induced by the immunization of mice with recombinant bacteriophage displaying an epitope of the human respiratory syncytial virus. Virology (1997) 234:118-122.
    • (1997) Virology , vol.234 , pp. 118-122
    • Bastein, N.1    Trude, M.2    Simard, C.3
  • 62
    • 0033783730 scopus 로고    scopus 로고
    • Vaccination towards prevention and treatment of Alzheimer's disease
    • Solomon B, Frenkel D: Vaccination towards prevention and treatment of Alzheimer's disease. Drugs of Today (2000) 36(9):655-663.
    • (2000) Drugs of Today , vol.36 , Issue.9 , pp. 655-663
    • Solomon, B.1    Frenkel, D.2
  • 63
    • 0035925634 scopus 로고    scopus 로고
    • Generation of auto-antibodies towards Alzheimer's disease vaccination
    • Frenkel D, Kariv N, Solomon B: Generation of auto-antibodies towards Alzheimer's disease vaccination. Vaccine Elsevier (2001) 19:2615-2619.
    • (2001) Vaccine Elsevier , vol.19 , pp. 2615-2619
    • Frenkel, D.1    Kariv, N.2    Solomon, B.3
  • 64
    • 0035702068 scopus 로고    scopus 로고
    • Towards Alzheimer's beta-amyloid vaccination
    • Frenkel D, Solomon B: Towards Alzheimer's beta-amyloid vaccination. Biologicals (2001) 29:243-247.
    • (2001) Biologicals , vol.29 , pp. 243-247
    • Frenkel, D.1    Solomon, B.2
  • 66
    • 0033525520 scopus 로고    scopus 로고
    • Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain
    • Moechars D, Dewchter I, Lorent K et al.: Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain. J. Biol. Chem.(1999) 274:6483-6492.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6483-6492
    • Moechars, D.1    Dewchter, I.2    Lorent, K.3
  • 67
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer's disease
    • Bard F, Cannon C, Barbour R et al.: Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer's disease. Nat. Med. (2000) 6:916-920. First evidence that peripheral administration of antibodies against beta-peptide cross BBB, decorate and dissolve plaque.
    • (2000) Nat. Med. , vol.6 , pp. 916-920
    • Bard, F.1    Cannon, C.2    Barbour, R.3
  • 68
    • 0035106780 scopus 로고    scopus 로고
    • Imaging of amyloid-B deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy
    • Bacskai BJ, Kajdasz ST, Christie RH et al.: Imaging of amyloid-B deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy. Nat. Med. (2001) 7:369-372. In vivo targeting of amyloid plaques by mAb and visualisation of clearance of plaque.
    • (2001) Nat. Med. , vol.7 , pp. 369-372
    • Bacskai, B.J.1    Kajdasz, S.T.2    Christie, R.H.3
  • 69
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease
    • Demattos RB, Bales KR, CUMMINS DJ, Dodart JC, Paul SM, Holtzman DM: Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA (2001) 17:8850-8855.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.17 , pp. 8850-8855
    • Demattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 70
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, Mclaurin J et al.: A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature (2000) 408:979-982. First demonstration of correlation between improved behaviour and vaccination against AβP.
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    Mclaurin, J.3
  • 71
    • 84984755327 scopus 로고    scopus 로고
    • A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan D, Diamond DM, Gottschall PE et al.: A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature (2000) 408:982-985. First demonstration of correlation between improved behaviour and vaccination against AβP.
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1    Diamond, D.M.2    Gottschall, P.E.3
  • 72
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • Holcomb L, Gordon MN, Mcgowan E et al.: Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat. Med. (1998) 4:97-100.
    • (1998) Nat. Med. , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    Mcgowan, E.3
  • 73
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model
    • Dodart JC, Bales KR, Gannon KS et al.: Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model. Nat. Neurosci. (2002) 5(5):452-457.
    • (2002) Nat. Neurosci. , vol.5 , Issue.5 , pp. 452-457
    • Dodart, J.C.1    Bales, K.R.2    Gannon, K.S.3
  • 74
    • 0034744296 scopus 로고    scopus 로고
    • TGF-beta1 promotes microglial amyloid-beta clearance and reduces plaque burden in transgenic mice
    • Wyss-Coray T, Lin C, Yan F et al.: TGF-beta1 promotes microglial amyloid-beta clearance and reduces plaque burden in transgenic mice. Nat. Med. (2001) 7(5):612-874.
    • (2001) Nat. Med. , vol.7 , Issue.5 , pp. 612-874
    • Wyss-Coray, T.1    Lin, C.2    Yan, F.3
  • 75
    • 0037107177 scopus 로고    scopus 로고
    • Non-fc-mediated mechanisms are involved in clearance of amyloid-β in vivo by immunotherapy
    • Bacskai BJ, Kajdasz ST, Megan E et al.: Non-fc-mediated mechanisms are involved in clearance of amyloid-β in vivo by immunotherapy. J. Neurosci. (2002) 22(18):7873-7878.
    • (2002) J. Neurosci. , vol.22 , Issue.18 , pp. 7873-7878
    • Bacskai, B.J.1    Kajdasz, S.T.2    Megan, E.3
  • 76
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-β efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • Demattos RB, Bales KR, Cummins DJ et al.: Brain to plasma amyloid-β efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science (2002) 295:2264-2267.
    • (2002) Science , vol.295 , pp. 2264-2267
    • Demattos, R.B.1    Bales, K.R.2    Cummins, D.J.3
  • 77
    • 0032732224 scopus 로고    scopus 로고
    • Elimination of the class A scavenger receptor does not affect amyloid plaque formation or neurodegeneration in transgenic mice expressing human amyloid protein precursors
    • Huang F, Buttini M, Wyss-Coray T et al.: Elimination of the class A scavenger receptor does not affect amyloid plaque formation or neurodegeneration in transgenic mice expressing human amyloid protein precursors. Am. J. Pathol. (1999) 155:1741-1747.
    • (1999) Am. J. Pathol. , vol.155 , pp. 1741-1747
    • Huang, F.1    Buttini, M.2    Wyss-Coray, T.3
  • 78
    • 0034746387 scopus 로고    scopus 로고
    • Abeta-induced inflammatory processes in microglia cells of APP23 transgenic mice
    • Bornemann KD, Wiederhold KH, Pauli C et al.: Abeta-induced inflammatory processes in microglia cells of APP23 transgenic mice. Am. J. Pathol. (2001) 158:63-73.
    • (2001) Am. J. Pathol. , vol.158 , pp. 63-73
    • Bornemann, K.D.1    Wiederhold, K.H.2    Pauli, C.3
  • 79
  • 80
    • 0030938911 scopus 로고    scopus 로고
    • Is amyloid beta-protein glycated in Alzheimer's disease?
    • Tabaton M, Perry G, Smith M et al.: Is amyloid beta-protein glycated in Alzheimer's disease? NeuroReport. (1997) 8:907-909.
    • (1997) NeuroReport , vol.8 , pp. 907-909
    • Tabaton, M.1    Perry, G.2    Smith, M.3
  • 81
    • 0035689761 scopus 로고    scopus 로고
    • Immunotherapy with β-amyloid for Alzheimer's disease: A new frontier
    • Schenk D, Seubert P, Ciccarelli RB: Immunotherapy with β-amyloid for Alzheimer's disease: A new frontier. DNA Cell Biol. (2001) 20:679-681.
    • (2001) DNA Cell Biol. , vol.20 , pp. 679-681
    • Schenk, D.1    Seubert, P.2    Ciccarelli, R.B.3
  • 82
    • 0035695315 scopus 로고    scopus 로고
    • Imunotherapeutic strategies towards prevention and treatment of Alzheimer's disease
    • Solomon B: Imunotherapeutic strategies towards prevention and treatment of Alzheimer's disease. DNA and Cell Biology (2001) 20:697-703.
    • (2001) DNA and Cell Biology , vol.20 , pp. 697-703
    • Solomon, B.1
  • 83
    • 0036676975 scopus 로고    scopus 로고
    • Roles of Fc receptors in autoimmunity
    • Takai T: Roles of Fc receptors in autoimmunity. Nature Reviews (2002) 2:580-592.
    • (2002) Nature Reviews , vol.2 , pp. 580-592
    • Takai, T.1
  • 84
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • Samuelsson A, Towers TL, Ravetch JV: Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor. Science (2001) 291:484-486.
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 85
    • 0037117459 scopus 로고    scopus 로고
    • Filamentous phage as vector-mediated antibody delivery to the brain
    • Frenkel D, Solomon B: Filamentous phage as vector-mediated antibody delivery to the brain. Proc. Natl. Acad. Sci. USA (2002) 99:5675-5679.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5675-5679
    • Frenkel, D.1    Solomon, B.2


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