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Volumn 9, Issue , 2009, Pages 909-919

Immunotherapeutic strategies for Alzheimer's disease treatment

Author keywords

Alzheimer's disease; Amyloid plaque; Amyloid ; Immunotherapy; Inflammation; Neuropathology

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; AMYLOID BETA PROTEIN[1-30]; AMYLOID BETA PROTEIN[1-42]; HISTIDYLARGINYLPHENYLALANYLGLUTAMIC ACID; IMMUNOGLOBULIN; IMMUNOGLOBULIN G; INFLUENZA VACCINE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 266; MONOCLONAL ANTIBODY BC05; PEPTIDE; UNCLASSIFIED DRUG;

EID: 70350755721     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1100/tsw.2009.99     Document Type: Review
Times cited : (13)

References (76)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D.J. (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 2
    • 0025899041 scopus 로고    scopus 로고
    • Hardy, J. and Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12(10), 383-388.
    • Hardy, J. and Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12(10), 383-388.
  • 6
    • 0035964312 scopus 로고    scopus 로고
    • Immune hypo-responsiveness to amyloid β-peptide in amyloid precursor protein transgenic mice: Implications for the pathogenesis and treatment of Alzheimer's disease
    • Monsonego, A., Maron, R., Zota, V., Selkoe, D.J., and Weiner, H.L. (2001) Immune hypo-responsiveness to amyloid β-peptide in amyloid precursor protein transgenic mice: implications for the pathogenesis and treatment of Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 98, 10273-10278.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 10273-10278
    • Monsonego, A.1    Maron, R.2    Zota, V.3    Selkoe, D.J.4    Weiner, H.L.5
  • 7
    • 0041886776 scopus 로고    scopus 로고
    • Increased T cell reactivity to amyloid β-protein in older humans and patients with Alzheimer disease
    • Monsonego, A., Zota, V., Karni, A., Krieger, J.I., Bar-Or, A., Bitan, G., et al. (2003) Increased T cell reactivity to amyloid β-protein in older humans and patients with Alzheimer disease. J. Clin. Invest. 112(3), 415-422.
    • (2003) J. Clin. Invest , vol.112 , Issue.3 , pp. 415-422
    • Monsonego, A.1    Zota, V.2    Karni, A.3    Krieger, J.I.4    Bar-Or, A.5    Bitan, G.6
  • 8
    • 0037203825 scopus 로고    scopus 로고
    • Nerve inflammation halts trial for Alzheimer's drug
    • Check, E. (2002) Nerve inflammation halts trial for Alzheimer's drug. Nature 415, 462.
    • (2002) Nature , vol.415 , pp. 462
    • Check, E.1
  • 10
    • 0037073558 scopus 로고    scopus 로고
    • The generation and characterization of potentially therapeutic Abeta antibodies in mice: Differences according to strain and immunization protocol
    • Spooner, E.T., Desai, R.V., Mori, C., Leverone, J.F., and Lemere, C.A. (2002) The generation and characterization of potentially therapeutic Abeta antibodies in mice: differences according to strain and immunization protocol. Vaccine 21, 290-297.
    • (2002) Vaccine , vol.21 , pp. 290-297
    • Spooner, E.T.1    Desai, R.V.2    Mori, C.3    Leverone, J.F.4    Lemere, C.A.5
  • 11
    • 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, M.E., Tian, X., Phinney, A.L., Manea, M., et al. (2002) Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4-10 and inhibit cytotoxicity and fibrillogenesis. Nat. Med. 8, 1263-1269.
    • (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
  • 12
    • 20444459853 scopus 로고    scopus 로고
    • Autoantibodies to redox-modified oligomeric Abeta are attenuated in the plasma of Alzheimer's disease patients
    • Moir, R.D., Tseitlin, K.A., Soscia, S., Hyman, B.T., Irizarry, M.C., and Tanzi, R.E. (2005) Autoantibodies to redox-modified oligomeric Abeta are attenuated in the plasma of Alzheimer's disease patients. J. Biol. Chem. 280(17), 17458-17463.
    • (2005) J. Biol. Chem , vol.280 , Issue.17 , pp. 17458-17463
    • Moir, R.D.1    Tseitlin, K.A.2    Soscia, S.3    Hyman, B.T.4    Irizarry, M.C.5    Tanzi, R.E.6
  • 13
    • 0036085702 scopus 로고    scopus 로고
    • Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals
    • Weksler, M.E., Relkin, N., Turkenich, R., LaRusse, S., Zhou, L., and Szabo, P. (2002) Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals. Exp. Gerontol. 37, 943-948.
    • (2002) Exp. Gerontol , vol.37 , pp. 943-948
    • Weksler, M.E.1    Relkin, N.2    Turkenich, R.3    LaRusse, S.4    Zhou, L.5    Szabo, P.6
  • 14
    • 0030925824 scopus 로고    scopus 로고
    • Increased incidence of anti-beta-amyloid autoantibodies secreted by Epstein-Barr virus transformed B cell lines from patients with Alzheimer's disease
    • Xu, S. and Gaskin, F. (1997) Increased incidence of anti-beta-amyloid autoantibodies secreted by Epstein-Barr virus transformed B cell lines from patients with Alzheimer's disease. Mech. Ageing Dev. 94(1-3), 213-222.
    • (1997) Mech. Ageing Dev , vol.94 , Issue.1-3 , pp. 213-222
    • Xu, S.1    Gaskin, F.2
  • 16
    • 0029895147 scopus 로고    scopus 로고
    • Brain amyloid-a physicochemical perspective
    • Maggio, J.E. and Mantyh, P.W. (1996) Brain amyloid-a physicochemical perspective. Brain Pathol. 6, 147-162.
    • (1996) Brain Pathol , vol.6 , pp. 147-162
    • Maggio, J.E.1    Mantyh, P.W.2
  • 17
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C.J. and Zagorski, M.G. (1991) Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition. Science 253, 179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 18
    • 0028980362 scopus 로고
    • The a-helical to b-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto, C., Castano, E.M., Frangione, B., and Inestrosa, N.C. (1995) The a-helical to b-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. 270, 3063.
    • (1995) J. Biol. Chem , vol.270 , pp. 3063
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 19
    • 0029015766 scopus 로고
    • pH-dependent conformations of the amyloid beta(1-28) peptide fragment explored using molecular dynamics
    • Kirschenbaum, K. and Daggett, V. (1995) pH-dependent conformations of the amyloid beta(1-28) peptide fragment explored using molecular dynamics. Biochemistry 34(23), 7629-7639.
    • (1995) Biochemistry , vol.34 , Issue.23 , pp. 7629-7639
    • Kirschenbaum, K.1    Daggett, V.2
  • 20
    • 0018793861 scopus 로고
    • Temperature dependent x-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder, H., Petsko, G.A., and Tsernoglou, D. (1979) Temperature dependent x-ray diffraction as a probe of protein structural dynamics. Nature 280, 558.
    • (1979) Nature , vol.280 , pp. 558
    • Frauenfelder, H.1    Petsko, G.A.2    Tsernoglou, D.3
  • 21
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus, M. and Petsko, G.A. (1990) Molecular dynamics simulations in biology. Nature 347, 632.
    • (1990) Nature , vol.347 , pp. 632
    • Karplus, M.1    Petsko, G.A.2
  • 22
    • 0004381305 scopus 로고
    • Partly native epitopes are already present on early intermediates in the folding of tryptophan synthase
    • Blond, S. and Goldberg, M. (1987) Partly native epitopes are already present on early intermediates in the folding of tryptophan synthase. Proc. Natl. Acad. Sci. U. S. A. 84, 1147.
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 1147
    • Blond, S.1    Goldberg, M.2
  • 24
    • 0026233196 scopus 로고
    • Thermostabilization of carboxypeptidase A by interaction with its monoclonal antibodies
    • Solomon, B. and Balas, N. (1991) Thermostabilization of carboxypeptidase A by interaction with its monoclonal antibodies. Biotechnol. Appl. Biochem. 14, 202.
    • (1991) Biotechnol. Appl. Biochem , vol.14 , pp. 202
    • Solomon, B.1    Balas, N.2
  • 25
    • 0029201345 scopus 로고
    • Chaperone-like effect of monoclonal antibodies on refolding of heat-denatured carboxypeptidase A
    • Solomon, B. and Schwartz, F. (1995) Chaperone-like effect of monoclonal antibodies on refolding of heat-denatured carboxypeptidase A. J. Mol. Recogn. 8, 72-76.
    • (1995) J. Mol. Recogn , vol.8 , pp. 72-76
    • Solomon, B.1    Schwartz, F.2
  • 26
    • 77957045803 scopus 로고    scopus 로고
    • Activity of monoclonal antibodies in prevention of in vitro aggregation of their antigens
    • Ballesteros, A, Plou, F.J, Iborra, J.L, and Halling, P.J, Eds. Elsevier, Amsterdam. pp
    • Solomon, B., Gozanski-Katzav, T., Koppel, R., and Hanan-Aharon, E. (1998) Activity of monoclonal antibodies in prevention of in vitro aggregation of their antigens. In Stability and Stabilization of Biocatalysts. Ballesteros, A., Plou, F.J., Iborra, J.L., and Halling, P.J., Eds. Elsevier, Amsterdam. pp. 183-188.
    • (1998) Stability and Stabilization of Biocatalysts , pp. 183-188
    • Solomon, B.1    Gozanski-Katzav, T.2    Koppel, R.3    Hanan-Aharon, E.4
  • 27
    • 0029887388 scopus 로고    scopus 로고
    • Effect of monoclonal antibodies in preventing carboxypeptidase A aggregation
    • Katzav, T., Hanan, E., and Solomon, B. (1996) Effect of monoclonal antibodies in preventing carboxypeptidase A aggregation. Appl. Biochem. Biotechnol. 2, 227.
    • (1996) Appl. Biochem. Biotechnol , vol.2 , pp. 227
    • Katzav, T.1    Hanan, E.2    Solomon, B.3
  • 28
    • 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., and Katzav, T. (1996) Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer's β-amyloid peptide. Proc. Natl. Acad. Sci. U. S. A. 93(1), 452-455.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , Issue.1 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 29
    • 0000650806 scopus 로고    scopus 로고
    • Protective effect of monoclonal antibodies against Alzheimer's β-amyloid aggregation
    • Hanan, E. and Solomon, B. (1996) Protective effect of monoclonal antibodies against Alzheimer's β-amyloid aggregation. Amyloid 3, 130-133.
    • (1996) Amyloid , vol.3 , pp. 130-133
    • Hanan, E.1    Solomon, B.2
  • 31
    • 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., and Solomon, B. (1998) N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregating antibodies. J. Neuroimmunol. 88, 85-90.
    • (1998) J. Neuroimmunol , vol.88 , pp. 85-90
    • Frenkel, D.1    Balass, M.2    Solomon, B.3
  • 32
    • 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., Kachalsky-Katzir, E., and Solomon, B. (1999) High affinity binding of monoclonal antibodies to the sequential epitope EFRH of β-amyloid peptide is essential for modulation of fibrillar aggregation. J. Neuroimmunol. 95, 136.
    • (1999) J. Neuroimmunol , vol.95 , pp. 136
    • Frenkel, D.1    Balass, M.2    Kachalsky-Katzir, E.3    Solomon, B.4
  • 33
    • 0034014950 scopus 로고    scopus 로고
    • Single and multiple transgenic mice as models for Alzheimer's disease
    • Van Leuven, F. (2000) Single and multiple transgenic mice as models for Alzheimer's disease. Prog. Neurobiol. 61(3), 305-312.
    • (2000) Prog. Neurobiol , vol.61 , Issue.3 , pp. 305-312
    • Van Leuven, F.1
  • 34
    • 0036914592 scopus 로고    scopus 로고
    • Immunological approaches as therapy for Alzheimer's disease
    • Solomon, B. (2002) Immunological approaches as therapy for Alzheimer's disease. Exp. Opin. Biol. Ther. 2(8), 907-917.
    • (2002) Exp. Opin. Biol. Ther , vol.2 , Issue.8 , pp. 907-917
    • Solomon, B.1
  • 35
    • 0036595125 scopus 로고    scopus 로고
    • β-Amyloid immunization approaches for Alzheimer's disease
    • Imbimbo, B.P. (2002) β-Amyloid immunization approaches for Alzheimer's disease. Drug Dev. Res. 56, 150-162.
    • (2002) Drug Dev. Res , vol.56 , pp. 150-162
    • Imbimbo, B.P.1
  • 38
    • 0035964312 scopus 로고    scopus 로고
    • Immune hyporesponsiveness to amyloid β-peptide in amyloid precursor protein transgenic mice: Implications for the pathogenesis and treatment of Alzheimer's disease
    • Monsonego, A., Maron, R., Zota, V., Selkoe, D.J., and Weiner, H.L. (2001) Immune hyporesponsiveness to amyloid β-peptide in amyloid precursor protein transgenic mice: implications for the pathogenesis and treatment of Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 98, 10273-10278.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 10273-10278
    • Monsonego, A.1    Maron, R.2    Zota, V.3    Selkoe, D.J.4    Weiner, H.L.5
  • 39
    • 0034884382 scopus 로고    scopus 로고
    • Immunization with a nontoxic/nonfibrillar amyloid-beta homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice
    • Sigurdsson, E.M., Scholtzova, H., Mehta, P.D., Frangione, B., and Wisniewski, T. (2001) Immunization with a nontoxic/nonfibrillar amyloid-beta homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice. Am. J. Pathol. 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
  • 40
    • 0037133324 scopus 로고    scopus 로고
    • A liposome-based therapeutic vaccine against β-amyloid plaques on the pancreas of transgenic NORBA mice
    • Nicolau, C., Greferath, R., Balaban, T.S., Lazarte, J.E., and Hopkins, R.J. (2002) A liposome-based therapeutic vaccine against β-amyloid plaques on the pancreas of transgenic NORBA mice. Proc. Natl. Acad. Sci. U. S. A. 99, 2332-2337.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 2332-2337
    • Nicolau, C.1    Greferath, R.2    Balaban, T.S.3    Lazarte, J.E.4    Hopkins, R.J.5
  • 41
    • 0037424110 scopus 로고    scopus 로고
    • Reduction of beta-amyloid plaques in brain of transgenic mouse model of Alzheimer's disease by EFRH-phage immunization
    • Frenkel, D., Dewachter, I., Van Leuven, F., and Solomon, B. (2003) Reduction of beta-amyloid plaques in brain of transgenic mouse model of Alzheimer's disease by EFRH-phage immunization. Vaccine 21, 1060-1065.
    • (2003) Vaccine , vol.21 , pp. 1060-1065
    • Frenkel, D.1    Dewachter, I.2    Van Leuven, F.3    Solomon, B.4
  • 42
    • 13544277841 scopus 로고    scopus 로고
    • EFRH-phage immunization of Alzheimer's disease animal model improves behavioral performance in Morris Water Maze trials
    • Lavie, V., Becker, M., Cohen-Kupiec, R., Yacoby, I., Koppel, R., Wedenig, M., Hutter-Paier, B., and Solomon, B. (2004) EFRH-phage immunization of Alzheimer's disease animal model improves behavioral performance in Morris Water Maze trials. J. Mol. Neurosci. 24, 105-113.
    • (2004) J. Mol. Neurosci , vol.24 , pp. 105-113
    • Lavie, V.1    Becker, M.2    Cohen-Kupiec, R.3    Yacoby, I.4    Koppel, R.5    Wedenig, M.6    Hutter-Paier, B.7    Solomon, B.8
  • 43
    • 33646066257 scopus 로고    scopus 로고
    • Amyloid-β immunotherapy for the prevention and treatment of Alzheimer disease: Lessons from mice, monkeys, and humans
    • Lemere, C.A., Maier, M., Jiang, L., Peng, Y., and Seabrook, T.J. (2006) Amyloid-β immunotherapy for the prevention and treatment of Alzheimer disease: lessons from mice, monkeys, and humans. Rejuvenation Res. 9, 77-84.
    • (2006) Rejuvenation Res , vol.9 , pp. 77-84
    • Lemere, C.A.1    Maier, M.2    Jiang, L.3    Peng, Y.4    Seabrook, T.J.5
  • 44
    • 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 disease
    • Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (2000) Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 6(8), 916-920.
    • (2000) Nat. Med , vol.6 , Issue.8 , pp. 916-920
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.-L.4    Games, D.5    Grajeda, H.6    Guido, T.7    Hu, K.8    Huang, J.9    Johnson-Wood, K.10    Khan, K.11
  • 46
    • 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, R.B., Bales, K.R., Cummins, D.I., Dodart, J.C., Paul, S.M., and Holtzman, D.M. (2001) 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. U. S. A. 17, 8850-8855.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.17 , pp. 8850-8855
    • Demattos, R.B.1    Bales, K.R.2    Cummins, D.I.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 48
    • 33745111586 scopus 로고    scopus 로고
    • Intracranial administration of deglycosylated C-terminal-specific anti-Aβ antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice
    • Carty, N.C., Wilcock, D.M., Rosenthal, A., Grimm, J., Pons, J., Ronan, V., Gottschall, P.E., Gordon, M.N., and Morgan, D. (2006) Intracranial administration of deglycosylated C-terminal-specific anti-Aβ antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice. J. Neuroinflammation 10, 3.
    • (2006) J. Neuroinflammation , vol.10 , pp. 3
    • Carty, N.C.1    Wilcock, D.M.2    Rosenthal, A.3    Grimm, J.4    Pons, J.5    Ronan, V.6    Gottschall, P.E.7    Gordon, M.N.8    Morgan, D.9
  • 51
    • 0021713342 scopus 로고
    • Production of functional chimaeric mouse/human antibody
    • Boulianne, G.L., Hozumi, N., and Shulman, M.J. (1984) Production of functional chimaeric mouse/human antibody. Nature 312, 643-646.
    • (1984) Nature , vol.312 , pp. 643-646
    • Boulianne, G.L.1    Hozumi, N.2    Shulman, M.J.3
  • 52
    • 0022558297 scopus 로고
    • Replacing the complementary-determining regions in a human antibody with those from a mouse
    • Jones, P.T., Dear, P.H., Foote, J., Neuberger, M.S., and Winter, G. (1986) Replacing the complementary-determining regions in a human antibody with those from a mouse. Nature 321, 522-525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 53
    • 0036085702 scopus 로고    scopus 로고
    • Patients with Alzheimer's disease have lower levels of serum anti-amyloid peptide antibodies than healthy individuals
    • Weksler, M.E., Relkin, N., Turkenich, R., LaRusse, S., Zhou, L., and Szabo, P. (2002) Patients with Alzheimer's disease have lower levels of serum anti-amyloid peptide antibodies than healthy individuals. Exp. Gerontol. 37(7), 943-948.
    • (2002) Exp. Gerontol , vol.37 , Issue.7 , pp. 943-948
    • Weksler, M.E.1    Relkin, N.2    Turkenich, R.3    LaRusse, S.4    Zhou, L.5    Szabo, P.6
  • 55
    • 0041320819 scopus 로고    scopus 로고
    • Human anti-beta-amyloid antibodies block beta-amyloid fibril formation and prevent beta-amyloid-induced neurotoxicity
    • Du, Y., Wei, X., Dodel, R., Sommer, N., Hampel, H., Gao, F., Ma, Z., Zhao, L., Oertel, W.H., and Farlow, M. (2003) Human anti-beta-amyloid antibodies block beta-amyloid fibril formation and prevent beta-amyloid-induced neurotoxicity. Brain 126(Pt 9), 1935-1939.
    • (2003) Brain , vol.126 , Issue.PART 9 , pp. 1935-1939
    • Du, Y.1    Wei, X.2    Dodel, R.3    Sommer, N.4    Hampel, H.5    Gao, F.6    Ma, Z.7    Zhao, L.8    Oertel, W.H.9    Farlow, M.10
  • 56
    • 0037168786 scopus 로고    scopus 로고
    • Mechanisms of action of IVIg and therapeutic considerations in the treatment of acute and chronic demyelinating neuropathies
    • Dalakas, M.C. (2002) Mechanisms of action of IVIg and therapeutic considerations in the treatment of acute and chronic demyelinating neuropathies. Neurology 59(12 Suppl 6), S13-21.
    • (2002) Neurology , vol.59 , Issue.12 SUPPL. 6
    • Dalakas, M.C.1
  • 57
    • 33746419618 scopus 로고    scopus 로고
    • Intravenous immunoglobulin enhances the clearance of fibrillar amyloid-beta peptide
    • Istrin, G., Bosis, E., and Solomon, B. (2006) Intravenous immunoglobulin enhances the clearance of fibrillar amyloid-beta peptide. J. Neurosci. Res. 84(2), 434-443.
    • (2006) J. Neurosci. Res , vol.84 , Issue.2 , pp. 434-443
    • Istrin, G.1    Bosis, E.2    Solomon, B.3
  • 58
    • 38449088277 scopus 로고    scopus 로고
    • Antibody-based approaches in Alzheimer's research: Safety, pharmacokinetics, metabolism, and analytical tools
    • Mohajeri, M.H. and Lichtlen, P. (2008) Antibody-based approaches in Alzheimer's research: safety, pharmacokinetics, metabolism, and analytical tools. J. Neurochem. 104, 859-874.
    • (2008) J. Neurochem , vol.104 , pp. 859-874
    • Mohajeri, M.H.1    Lichtlen, P.2
  • 59
    • 0038044258 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease
    • Dodel, R.C., Hampel, H., and Du, Y. (2003) Immunotherapy for Alzheimer's disease. Lancet Neurol. 2, 215-220.
    • (2003) Lancet Neurol , vol.2 , pp. 215-220
    • Dodel, R.C.1    Hampel, H.2    Du, Y.3
  • 60
    • 0036953160 scopus 로고    scopus 로고
    • Passage of amyloid β protein antibody across the blood-brain barrier in a mouse model of Alzheimer's disease
    • Banks, W.A., Terrell, B., Farr, S.A., Robinson, S.M., Nonaka, N., and Morley, J.E. (2002) Passage of amyloid β protein antibody across the blood-brain barrier in a mouse model of Alzheimer's disease. Peptides 23, 2223-2226.
    • (2002) Peptides , vol.23 , pp. 2223-2226
    • Banks, W.A.1    Terrell, B.2    Farr, S.A.3    Robinson, S.M.4    Nonaka, N.5    Morley, J.E.6
  • 61
    • 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. (2003) 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. 100(4), 2023-2028.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , Issue.4 , pp. 2023-2028
    • Bard, F.1    Barbour, R.2    Cannon, C.3    Carretto, R.4    Fox, M.5    Games, D.6
  • 62
    • 0035877075 scopus 로고    scopus 로고
    • Antibody-mediated phagocytosis of the amyloid beta-peptide in microglia is differentially modulated by C1q
    • Webster, S.D., Galvan, M.D., Ferran, E., Garzon-Rodriguez, W., Glabe, C.G., and Tenner, A.J. (2001) Antibody-mediated phagocytosis of the amyloid beta-peptide in microglia is differentially modulated by C1q. J. Immunol. 166, 7496.
    • (2001) J. Immunol , vol.166 , pp. 7496
    • Webster, S.D.1    Galvan, M.D.2    Ferran, E.3    Garzon-Rodriguez, W.4    Glabe, C.G.5    Tenner, A.J.6
  • 63
    • 0037110640 scopus 로고    scopus 로고
    • Modeling Alzheimer's disease immune therapy mechanisms: Interactions of human postmortem microglia with antibody-opsonized amyloid beta peptide
    • Lue, L.-F. and Walker, D.G. (2002) Modeling Alzheimer's disease immune therapy mechanisms: interactions of human postmortem microglia with antibody-opsonized amyloid beta peptide. J. Neurosci. Res. 70, 599-610.
    • (2002) J. Neurosci. Res , vol.70 , pp. 599-610
    • Lue, L.-F.1    Walker, D.G.2
  • 64
    • 0036852750 scopus 로고    scopus 로고
    • Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4- and inhibit cytotoxicity and fibrillogenesis
    • McLaurin, J., Cecal, R., Kierstead, M.E., Tian, X., Phinney, A.L., Manea, M., French, J.E., Lambermon, M.H.L., Darabie, A.A., Brown, M.E., et al. (2002) Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4- and inhibit cytotoxicity and fibrillogenesis. Nat. Med. 8, 1263-1269.
    • (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    French, J.E.7    Lambermon, M.H.L.8    Darabie, A.A.9    Brown, M.E.10
  • 66
    • 0035106780 scopus 로고    scopus 로고
    • Imaging of amyloid-β deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy
    • Bacskai, B.J., Kajdasz, S.T., Christie, R.H., Carter, C., Games, D., Seubert, P., Schenk, D., and Bradley, H.T. (2001) Imaging of amyloid-β deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy. Nat. Med. 7(3), 369-372.
    • (2001) Nat. Med , vol.7 , Issue.3 , pp. 369-372
    • Bacskai, B.J.1    Kajdasz, S.T.2    Christie, R.H.3    Carter, C.4    Games, D.5    Seubert, P.6    Schenk, D.7    Bradley, H.T.8
  • 67
    • 0037107177 scopus 로고    scopus 로고
    • Non-fc-mediated mechanisms are involved in clearance of amyloid-β in vivo by immunotherapy
    • Bacskai, B.J., Kajdasz, S.T., McLellan, M.E., Games, D., Seubert, P., Schenk, D., and Hyman, B.T. (2002) Non-fc-mediated mechanisms are involved in clearance of amyloid-β in vivo by immunotherapy. J. Neurosci. 15, 7873-7878.
    • (2002) J. Neurosci , vol.15 , pp. 7873-7878
    • Bacskai, B.J.1    Kajdasz, S.T.2    McLellan, M.E.3    Games, D.4    Seubert, P.5    Schenk, D.6    Hyman, B.T.7
  • 68
    • 0034237142 scopus 로고    scopus 로고
    • Modulation of Alzheimer's β-amyloid neurotoxicity by site-directed single-chain antibody
    • Frenkel, D., Solomon, B., and Benhar, I. (2000) Modulation of Alzheimer's β-amyloid neurotoxicity by site-directed single-chain antibody. J. Neuroimmunol. 106, 23-31.
    • (2000) J. Neuroimmunol , vol.106 , pp. 23-31
    • Frenkel, D.1    Solomon, B.2    Benhar, I.3
  • 69
    • 0037117459 scopus 로고    scopus 로고
    • Filamentous phage as vector-mediated antibody delivery to the brain
    • Solomon, B. and Frenkel, D. (2002) Filamentous phage as vector-mediated antibody delivery to the brain. Proc. Natl. Acad. Sci. U. S. A. 99(8), 5675-5679.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , Issue.8 , pp. 5675-5679
    • Solomon, B.1    Frenkel, D.2
  • 70
    • 2642578354 scopus 로고    scopus 로고
    • Single chain variable fragments against beta-amyloid (Aβ) can inhibit Aβ aggregation and prevent Aβ-induced neurotoxicity
    • Liu, R., Yuan, B., Emadi, S., Zameer, A., Schulz, P., McAllister, C., Lyubchenko, Y., Goud, G., and Sierks, M. R. (2004) Single chain variable fragments against beta-amyloid (Aβ) can inhibit Aβ aggregation and prevent Aβ-induced neurotoxicity. Biochemistry 43, 6959-6967.
    • (2004) Biochemistry , vol.43 , pp. 6959-6967
    • Liu, R.1    Yuan, B.2    Emadi, S.3    Zameer, A.4    Schulz, P.5    McAllister, C.6    Lyubchenko, Y.7    Goud, G.8    Sierks, M.R.9
  • 71
    • 33751111439 scopus 로고    scopus 로고
    • Intracranial adeno-associated virus-mediated delivery of anti-pan amyloid beta, amyloid beta40, and amyloid beta42 single-chain variable fragments attenuates plaque pathology in amyloid precursor protein mice
    • Levites, Y., Jansen, K., Smithson, L.A., Dakin, R., Holloway, V.M., Das, P., and Golde, T.E. (2006) Intracranial adeno-associated virus-mediated delivery of anti-pan amyloid beta, amyloid beta40, and amyloid beta42 single-chain variable fragments attenuates plaque pathology in amyloid precursor protein mice. J. Neurosci. 26, 11923-11928.
    • (2006) J. Neurosci , vol.26 , pp. 11923-11928
    • Levites, Y.1    Jansen, K.2    Smithson, L.A.3    Dakin, R.4    Holloway, V.M.5    Das, P.6    Golde, T.E.7
  • 73
    • 0141457897 scopus 로고    scopus 로고
    • Amyloid-β immunization effectively reduces amyloid deposition in FcRγ-/- knock-out mice
    • Das, P., Howard, V., Loosbrock, N., Dickson, D., Murphy, M.P., and Golde, T.E. (2003) Amyloid-β immunization effectively reduces amyloid deposition in FcRγ-/- knock-out mice. J. Neurosci. 23, 8532-8538.
    • (2003) J. Neurosci , vol.23 , pp. 8532-8538
    • Das, P.1    Howard, V.2    Loosbrock, N.3    Dickson, D.4    Murphy, M.P.5    Golde, T.E.6
  • 74
    • 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, R.B., Bales, K.R., Cummins, D.J., Paul, S.M., and Holtzman, D.M. (2002) Brain to plasma amyloid-β efflux: a measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science 295, 2264-2267.
    • (2002) Science , vol.295 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.