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Volumn 4, Issue 5, 2002, Pages 431-434

Of mice and men: The relevance of transgenic mice Aβ immunizations to Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN;

EID: 0036813085     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2002-4509     Document Type: Note
Times cited : (10)

References (25)
  • 1
    • 0034837627 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease
    • C. Janus and D. Westaway, Transgenic mouse models of Alzheimer's disease, Physiol Behavior 73 (2001), 873-886.
    • (2001) Physiol Behavior , vol.73 , pp. 873-886
    • Janus, C.1    Westaway, D.2
  • 3
    • 0035132326 scopus 로고    scopus 로고
    • Amyloid β vaccination: Reduced plaques and improved cognition
    • S.G. Younkin, Amyloid β vaccination: Reduced plaques and improved cognition, Nat Med 7 (2001), 18-19.
    • (2001) Nat Med , vol.7 , pp. 18-19
    • Younkin, S.G.1
  • 4
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • K. Hsiao, P. Chapman, S. Nilsen, C. Eckman, Y. Harigaya, S. Younkin, F. Yang and G. Cole, Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice, Sci 274 (1996), 99-102.
    • (1996) Sci , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 9
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plaque core proteins purified form Alzheimer disease brain
    • A.E. Roher, K.C. Palmer, E.C. Yurewicz, M.J. Ball and B.D. Greenberg. Morphological and biochemical analyses of amyloid plaque core proteins purified form Alzheimer disease brain, J Neurochem 61 (1993), 1916-1926.
    • (1993) J Neurochem , vol.61 , pp. 1916-1926
    • Roher, A.E.1    Palmer, K.C.2    Yurewicz, E.C.3    Ball, M.J.4    Greenberg, B.D.5
  • 10
    • 0027332081 scopus 로고
    • β-amyloid 1-42 is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • A.E. Roher, J.D. Lowenson, S. Clarke, A.S. Woods, R.J. Cotter, E. Gowing and M.J. Ball, β-amyloid 1-42 is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease, Proc Natl Acad Sci USA 90 (1993), 10836-10840.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 11
    • 0028179341 scopus 로고
    • Chemical characterization of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
    • E. Gowing, A.E. Roher, A.S. Woods, R.J. Cotter, M. Chaney, S.P. Little and M.J. Ball, Chemical characterization of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease, J Biol Chem 296 (1994), 10987-10990.
    • (1994) J Biol Chem , vol.296 , pp. 10987-10990
    • Gowing, E.1    Roher, A.E.2    Woods, A.S.3    Cotter, R.J.4    Chaney, M.5    Little, S.P.6    Ball, M.J.7
  • 14
    • 0031559602 scopus 로고    scopus 로고
    • Isolation, chemical characterization, and quantitation of Aβ 3-pyroglutamyl peptides from neuritic plaques and vascular amyloid deposits
    • Y.M. Kuo, M.R. Emmerling, A.S. Woods, R.J. Cotter and A.E. Roher, Isolation, chemical characterization, and quantitation of Aβ 3-pyroglutamyl peptides from neuritic plaques and vascular amyloid deposits, Biochem Biophys Res Comm 237 (1997), 188-191.
    • (1997) Biochem Biophys Res Comm , vol.237 , pp. 188-191
    • Kuo, Y.M.1    Emmerling, M.R.2    Woods, A.S.3    Cotter, R.J.4    Roher, A.E.5
  • 15
    • 0031862969 scopus 로고    scopus 로고
    • Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease
    • Y.M. Kuo, S. Webster, M.R. Emmerling, N. DeLima and A.E. Roher, Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease, Biochim Biophys Acta 1406 (1998), 291-298.
    • (1998) Biochim Biophys Acta , vol.1406 , pp. 291-298
    • Kuo, Y.M.1    Webster, S.2    Emmerling, M.R.3    DeLima, N.4    Roher, A.E.5
  • 17
    • 0029862137 scopus 로고
    • Age-dependent neuronal and synaptic degeneration in mice transgenic for the C-terminus of amyloid precursor protein
    • M.L. Oster-Granite, D.L. McPhie, J. Greenan and R.L. Neve, Age-dependent neuronal and synaptic degeneration in mice transgenic for the C-terminus of amyloid precursor protein, J Neurosci 16 (1966), 6732-6741.
    • (1966) J Neurosci , vol.16 , pp. 6732-6741
    • Oster-Granite, M.L.1    McPhie, D.L.2    Greenan, J.3    Neve, R.L.4
  • 18
    • 0033586449 scopus 로고    scopus 로고
    • Impairments in learning and memory accompanied by neurodegeneration in mice transgenic for the carboxyl-terminus of the amyloid precursor protein
    • J. Berger-Sweeney, D.L. McPhie, J.A. Arters, J. Greenan, M.L. Oster-Granite and R.L. Neve, Impairments in learning and memory accompanied by neurodegeneration in mice transgenic for the carboxyl-terminus of the amyloid precursor protein, Mol Brain Res 66 (1999), 150-162.
    • (1999) Mol Brain Res , vol.66 , pp. 150-162
    • Berger-Sweeney, J.1    McPhie, D.L.2    Arters, J.A.3    Greenan, J.4    Oster-Granite, M.L.5    Neve, R.L.6
  • 19
    • 0034183020 scopus 로고    scopus 로고
    • Elevated Aβ and apolipoprotein E in AβPP transgenic mice and its relationship to amyloid accumulation in Alzheimer's disease
    • Y.M. Kuo, F. Crawford, M. Mullan, T.A. Kokjohn, M.R. Emmerling, R.O. Weller and A.E. Roher, Elevated Aβ and apolipoprotein E in AβPP transgenic mice and its relationship to amyloid accumulation in Alzheimer's disease, Mol Med 6 (2000), 430-439.
    • (2000) Mol Med , vol.6 , pp. 430-439
    • Kuo, Y.M.1    Crawford, F.2    Mullan, M.3    Kokjohn, T.A.4    Emmerling, M.R.5    Weller, R.O.6    Roher, A.E.7
  • 21
    • 0035106780 scopus 로고    scopus 로고
    • Imaging of amyloid-β deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy
    • B.J. Bacskai, S.T. Kajdacz, R.H. Christie, C. Carter, D. Games, P. Seubert, D. Schenk and B.T. Hyman, Imaging of amyloid-β deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy, Nat Med 7 (2001), 369-372.
    • (2001) Nat Med , vol.7 , pp. 369-372
    • Bacskai, B.J.1    Kajdacz, S.T.2    Christie, R.H.3    Carter, C.4    Games, D.5    Seubert, P.6    Schenk, D.7    Hyman, B.T.8
  • 22
    • 0034746897 scopus 로고    scopus 로고
    • Reduced effectiveness of Aβ 1-42 immunization in APP transgenic mice with significant amyloid deposition
    • P. Das, M.P. Murphy, L.H. Younkin, S.G. Younkin and T.E. Golde, Reduced effectiveness of Aβ 1-42 immunization in APP transgenic mice with significant amyloid deposition, Neurobiol Aging 22 (2001), 721-727.
    • (2001) Neurobiol Aging , vol.22 , pp. 721-727
    • Das, P.1    Murphy, M.P.2    Younkin, L.H.3    Younkin, S.G.4    Golde, T.E.5
  • 24
    • 0030664076 scopus 로고    scopus 로고
    • Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells
    • D.M. Paresce, H. Chung and F.R. Maxfield, Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells, J Biol Chem 272 (1997), 29390-29397.
    • (1997) J Biol Chem , vol.272 , pp. 29390-29397
    • Paresce, D.M.1    Chung, H.2    Maxfield, F.R.3
  • 25
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid β-peptide by microglial cells
    • H. Chung, M.I. Brazil, T.T. Soe and F.R. Maxfield, Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid β-peptide by microglial cells, J Biol Chem 274 (1999), 32301-32308.
    • (1999) J Biol Chem , vol.274 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.