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Volumn 44, Issue 42, 2005, Pages 13807-13819

Altered APP processing in PDAPP (Val717 → Phe) transgenic mice yields extended-length Aβ peptides

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN; MASS SPECTROMETRY; PROTEINS; TISSUE;

EID: 27144553121     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051213+     Document Type: Article
Times cited : (27)

References (83)
  • 1
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer, R., Gray, S., and Kawas, C. (1998) Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset, Am. J. Public Health 88, 1337-1342.
    • (1998) Am. J. Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 2
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G., and Wong, C. W. (1984) Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein, Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A., and Higgins, G. A. (1992) Alzheimer's disease: The amyloid cascade hypothesis, Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 5
    • 0035081475 scopus 로고    scopus 로고
    • Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid β-protein
    • Selkoe, D. J. (2001) Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid β-protein, J. Alzheimers Dis. 3, 75-80.
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 75-80
    • Selkoe, D.J.1
  • 6
    • 0034183020 scopus 로고    scopus 로고
    • Elevated Aβ and apolipoprotein E in AβPP transgenic mice and its relationship to amyloid accumulation in Alzheimer's disease
    • Kuo, Y. M., Crawford, F., Mullan, M., Kokjohn, T. A., Emmerling, M. R., Weller, R. O., and Roher, A. E. (2000) Elevated Aβ and apolipoprotein E in AβPP transgenic mice and its relationship to amyloid accumulation in Alzheimer's disease, Mol. Med. 6, 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
  • 10
    • 2942611429 scopus 로고    scopus 로고
    • Transgenic mice overexpressing amyloid β protein are an incomplete model of Alzheimer disease
    • Schwab, C., Hosokawa, M., and McGeer, P. L. (2004) Transgenic mice overexpressing amyloid β protein are an incomplete model of Alzheimer disease, Exp. Neurol. 188, 52-64.
    • (2004) Exp. Neurol. , vol.188 , pp. 52-64
    • Schwab, C.1    Hosokawa, M.2    McGeer, P.L.3
  • 11
    • 27144535248 scopus 로고    scopus 로고
    • Appraisal of AβPP transgenic mice as models for Alzheimer's disease
    • Roher, A. E., and Kokjohn, T. A. (2003) Appraisal of AβPP transgenic mice as models for Alzheimer's disease, Curr. Med. Chem. 3, 85-90.
    • (2003) Curr. Med. Chem. , vol.3 , pp. 85-90
    • Roher, A.E.1    Kokjohn, T.A.2
  • 13
    • 0035689651 scopus 로고    scopus 로고
    • Behavioral assessment of Alzheimer's transgenic mice following long-term Aβ vaccination: Task specificity and correlations between Aβ deposition and spatial memory
    • Arendash, G. W., Gordon, M. N., Diamond, D. M., Austin, L. A., Hatcher, J. M., Jantzen, P., DiCarlo, G., Wilcock, D., and Morgan, D. (2001) Behavioral assessment of Alzheimer's transgenic mice following long-term Aβ vaccination: Task specificity and correlations between Aβ deposition and spatial memory, DNA Cell Biol. 20, 737-744.
    • (2001) DNA Cell Biol. , vol.20 , pp. 737-744
    • Arendash, G.W.1    Gordon, M.N.2    Diamond, D.M.3    Austin, L.A.4    Hatcher, J.M.5    Jantzen, P.6    Dicarlo, G.7    Wilcock, D.8    Morgan, D.9
  • 14
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report
    • Nicoll, J. A., Wilkinson, D., Holmes, C., Steart, P., Markham, H., and Weller, R. O. (2003) Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report, Nat. Med. 9, 448-452.
    • (2003) Nat. Med. , vol.9 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 15
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyloid-β immunization in Alzheimer's disease
    • Ferrer, I., Boada, R. M., Sanchez Guerra, M. L., Rey, M. J., and Costa-Jussa, F. (2004) Neuropathology and pathogenesis of encephalitis following amyloid-β immunization in Alzheimer's disease, Brain Pathol. 14, 11-20.
    • (2004) Brain Pathol. , vol.14 , pp. 11-20
    • Ferrer, I.1    Boada, R.M.2    Sanchez Guerra, M.L.3    Rey, M.J.4    Costa-Jussa, F.5
  • 19
    • 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. J., 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. 98, 8850-8855.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , 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
  • 20
    • 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, 2267.
    • (2002) Science , vol.295 , pp. 2267
    • Demattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 22
    • 14244255355 scopus 로고    scopus 로고
    • Passive immunotherapy against Aβ in aged APP-transgenic mice reverses cognitive deficits and depletes parenchymal amyloid deposits in spite of increased vascular amyloid and microhemorrhage
    • Wilcock, D. M., Rojiani, A., Rosenthal, A., Subbarao, S., Freeman, M. J., Gordon, M. N., and Morgan, D. (2004) Passive immunotherapy against Aβ in aged APP-transgenic mice reverses cognitive deficits and depletes parenchymal amyloid deposits in spite of increased vascular amyloid and microhemorrhage, J. Neuroinflammation 1, 24-35.
    • (2004) J. Neuroinflammation , vol.1 , pp. 24-35
    • Wilcock, D.M.1    Rojiani, A.2    Rosenthal, A.3    Subbarao, S.4    Freeman, M.J.5    Gordon, M.N.6    Morgan, D.7
  • 24
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell, J., Farlow, M., Ghetti, B., and Benson, M. D. (1991) A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease, Sci. 254, 97-99.
    • (1991) Sci. , vol.254 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 26
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of Aβ 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke, L., Masliah, E., Yu, G. Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., and McConlogue, L. (2000) High-level neuronal expression of Aβ 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation, J. Neurosci. 20, 4050-4058.
    • (2000) J. Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6    Hu, K.7    Kholodenko, D.8    Johnson-Wood, K.9    McConlogue, L.10
  • 29
    • 0028179341 scopus 로고
    • Chemical characterization of a β 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
    • Gowing, E., Roher, A. E., Woods, A. S., Cotter, R. J., Chaney, M., Little, S. P., and Ball, M. J. (1994) Chemical characterization of A β 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease, J. Biol. Chem. 269, 10987-10990.
    • (1994) J. Biol. Chem. , vol.269 , 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
  • 30
    • 0347445722 scopus 로고    scopus 로고
    • A genomic analysis of rat proteases and protease inhibitors
    • Puente, X. S., and Lopez-Otin, C. (2004) A genomic analysis of rat proteases and protease inhibitors, Genome Res. 14, 609-622.
    • (2004) Genome Res. , vol.14 , pp. 609-622
    • Puente, X.S.1    Lopez-Otin, C.2
  • 33
    • 10944259134 scopus 로고    scopus 로고
    • Identification of a new presenilin-dependent ζ-cleavage site within the transmembrane domain of amyloid precursor protein
    • Zhao, G., Mao, G., Tan, J., Dong, Y., Cui, M. Z., Kim, S. H., and Xu, X. (2004) Identification of a new presenilin-dependent ζ-cleavage site within the transmembrane domain of amyloid precursor protein, J. Biol. Chem. 279, 50647-50650.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50647-50650
    • Zhao, G.1    Mao, G.2    Tan, J.3    Dong, Y.4    Cui, M.Z.5    Kim, S.H.6    Xu, X.7
  • 34
    • 0037176727 scopus 로고    scopus 로고
    • A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann, A., Eggert, S., Reinhard, F. B., Vogel, M., Paliga, K., Baier, G., Masters, C. L., Beyreuther, K., and Evin, G. (2002) A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing, Biochemistry 41, 2825-2835.
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.9
  • 36
    • 2442592973 scopus 로고    scopus 로고
    • The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and ε-like cleavages: Modulation of APLP-1 processing by N-glycosylation
    • Eggert, S., Paliga, K., Soba, P., Evin, G., Masters, C. L., Weidemann, A., and Beyreuther, K. (2004) The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and ε-like cleavages: Modulation of APLP-1 processing by N-glycosylation, J. Biol. Chem. 279, 18146-18156.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18146-18156
    • Eggert, S.1    Paliga, K.2    Soba, P.3    Evin, G.4    Masters, C.L.5    Weidemann, A.6    Beyreuther, K.7
  • 37
    • 3142536464 scopus 로고    scopus 로고
    • Secretion of long Aβ-related peptides processed at e-cleavage site is dependent on the α-secretase precutting
    • Kametani, F. (2004) Secretion of long Aβ-related peptides processed at e-cleavage site is dependent on the α-secretase precutting, FEBS Lett. 570, 73-76.
    • (2004) FEBS Lett. , vol.570 , pp. 73-76
    • Kametani, F.1
  • 38
    • 1542543460 scopus 로고    scopus 로고
    • Intracellular domain generation of amyloid precursor protein by ε-cleavage depends on C-terminal fragment by α-secretase cleavage
    • Kume, H., Maruyama, H., and Kametani, F. (2004) Intracellular domain generation of amyloid precursor protein by ε-cleavage depends on C-terminal fragment by α-secretase cleavage, Int. J. Mol. Med. 13, 121-125.
    • (2004) Int. J. Mol. Med. , vol.13 , pp. 121-125
    • Kume, H.1    Maruyama, H.2    Kametani, F.3
  • 39
    • 6344265522 scopus 로고    scopus 로고
    • Truncated carboxyl-terminal fragments of β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42
    • Funamoto, S., Morishima-Kawashima, M., Tanimura, Y., Hirotani, N., Saido, T. C., and Ihara, Y. (2004) Truncated carboxyl-terminal fragments of β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42, Biochemistry 43, 13532-13540.
    • (2004) Biochemistry , vol.43 , pp. 13532-13540
    • Funamoto, S.1    Morishima-Kawashima, M.2    Tanimura, Y.3    Hirotani, N.4    Saido, T.C.5    Ihara, Y.6
  • 42
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modeling of the Aβ-42 peptide from Alzheimer's disease
    • Chaney, M. O., Webster, S. D., Kuo, Y. M., and Roher, A. E. (1998) Molecular modeling of the Aβ-42 peptide from Alzheimer's disease, Protein Eng. 11, 761-767.
    • (1998) Protein Eng. , vol.11 , pp. 761-767
    • Chaney, M.O.1    Webster, S.D.2    Kuo, Y.M.3    Roher, A.E.4
  • 44
    • 0028980163 scopus 로고
    • Early amyloid-β deposits show different immunoreactivity to the amino-and carboxy-terminal regions of β-peptide in Alzheimer's disease and Down's syndrome brain
    • Kida, E., Wisniewski, K. E., and Wisniewski, H. M. (1995) Early amyloid-β deposits show different immunoreactivity to the amino-and carboxy-terminal regions of β-peptide in Alzheimer's disease and Down's syndrome brain, Neurosci. Lett. 193, 105-108.
    • (1995) Neurosci. Lett. , vol.193 , pp. 105-108
    • Kida, E.1    Wisniewski, K.E.2    Wisniewski, H.M.3
  • 45
    • 0030035922 scopus 로고    scopus 로고
    • P3 β-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain
    • Higgins, L. S., Murphy, G. M., Jr., Forno, L. S., Catalano, R., and Cordell, B. (1996) P3 β-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain, Am. J. Pathol. 149, 585-596.
    • (1996) Am. J. Pathol. , vol.149 , pp. 585-596
    • Higgins, L.S.1    Murphy Jr., G.M.2    Forno, L.S.3    Catalano, R.4    Cordell, B.5
  • 48
    • 0035085610 scopus 로고    scopus 로고
    • Amyloid-β peptide fragments p3 and p4 induce pro-inflammatory cytokine and chemokine production in vitro and in vivo
    • Szczepanik, A. M., Rampe, D., and Ringheim, G. E. (2001) Amyloid-β peptide fragments p3 and p4 induce pro-inflammatory cytokine and chemokine production in vitro and in vivo, J. Neurochem. 77, 304-317.
    • (2001) J. Neurochem. , vol.77 , pp. 304-317
    • Szczepanik, A.M.1    Rampe, D.2    Ringheim, G.E.3
  • 49
    • 0036707528 scopus 로고    scopus 로고
    • Aβ 17-42 in Alzheimer's disease activates JNK and caspase-8 leading to neuronal apoptosis
    • Wei, W., Norton, D. D., Wang, X., and Kusiak, J. W. (2002) Aβ 17-42 in Alzheimer's disease activates JNK and caspase-8 leading to neuronal apoptosis, Brain 125, 2036-2043.
    • (2002) Brain , vol.125 , pp. 2036-2043
    • Wei, W.1    Norton, D.D.2    Wang, X.3    Kusiak, J.W.4
  • 52
    • 0031559602 scopus 로고    scopus 로고
    • Isolation, chemical characterization, and quantitation of Aβ 3-pyroglutamyl peptides from neuritic plaques and vascular amyloid deposits
    • Kuo, Y. M., Emmerling, M. R., Woods, A. S., Cotter, R. J., and Roher, A. E. (1997) Isolation, chemical characterization, and quantitation of Aβ 3-pyroglutamyl peptides from neuritic plaques and vascular amyloid deposits, Biochem. Biophys. Res. Commun. 237, 188-191.
    • (1997) Biochem. Biophys. Res. Commun. , 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
  • 53
    • 0031862969 scopus 로고    scopus 로고
    • Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease
    • Kuo, Y. M., Webster, S., Emmerling, M. R., DeLima, N., and Roher, A. E. (1998) Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease, Biochim. Biophys. Acta 1406, 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
  • 55
    • 0036903299 scopus 로고    scopus 로고
    • Molecular imaging of amyloid β peptides in mouse brain sections using mass spectrometry
    • Stoeckli, M., Staab, D., Staufenbiel, M., Wiederhold, K. H., and Signer, L. (2002) Molecular imaging of amyloid β peptides in mouse brain sections using mass spectrometry, Anal Biochem. 311, 33-39.
    • (2002) Anal Biochem. , vol.311 , pp. 33-39
    • Stoeckli, M.1    Staab, D.2    Staufenbiel, M.3    Wiederhold, K.H.4    Signer, L.5
  • 57
    • 0032981558 scopus 로고    scopus 로고
    • Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
    • Lichtenthaler, S. F., Wang, R., Grimm, H., Uljon, S. N., Masters, C. L., and Beyreuther, K. (1999) Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein, Proc. Natl. Acad. Sci. U.S.A. 96, 3053-3058.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3053-3058
    • Lichtenthaler, S.F.1    Wang, R.2    Grimm, H.3    Uljon, S.N.4    Masters, C.L.5    Beyreuther, K.6
  • 58
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase
    • Nunan, J., Shearman, M. S., Checler, F., Cappai, R., Evin, G., Beyreuther, K., Masters, C. L., and Small, D. H. (2001) The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase, Eur. J. Biochem. 268, 5329-5336.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3    Cappai, R.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 59
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor β-secretase in Alzheimer's disease
    • Holsinger, R. M., McLean, C. A., Beyreuther, K., Masters, C. L., and Evin, G. (2002) Increased expression of the amyloid precursor β-secretase in Alzheimer's disease, Ann. Neurol. 51, 783-786.
    • (2002) Ann. Neurol. , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 60
    • 0036718272 scopus 로고    scopus 로고
    • β-secretase protein and activity are increased in the neocortex in Alzheimer disease
    • Fukumoto, H., Cheung, B. S., Hyman, B. T., and Irizarry, M. C. (2002) β-Secretase protein and activity are increased in the neocortex in Alzheimer disease, Arch. Neurol. 59, 1381-1389.
    • (2002) Arch. Neurol. , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 62
    • 0033605252 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases
    • Weidemann, A., Paliga, K., Durrwang, U., Reinhard, F. B., Schuckert, O., Evin, G., and Masters, C. L. (1999) Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases, J. Biol. Chem. 274, 5823-5829.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5823-5829
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3    Reinhard, F.B.4    Schuckert, O.5    Evin, G.6    Masters, C.L.7
  • 63
    • 0033597884 scopus 로고    scopus 로고
    • Alternative, non-secretase processing of Alzheimer's β-amyloid precursor protein during apoptosis by caspase-6 and -8
    • Pellegrini, L., Passer, B. J., Tabaton, M., Ganjei, J. K., and D'Adamio, L. (1999) Alternative, non-secretase processing of Alzheimer's β-amyloid precursor protein during apoptosis by caspase-6 and -8, J. Biol. Chem. 274, 21011-21016.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21011-21016
    • Pellegrini, L.1    Passer, B.J.2    Tabaton, M.3    Ganjei, J.K.4    D'Adamio, L.5
  • 64
    • 0033551738 scopus 로고    scopus 로고
    • Caspase-6 role in apoptosis of human neurons, amyloidogenesis, and Alzheimer's disease
    • LeBlanc, A., Liu, H., Goodyer, C., Bergeron, C., and Hammond, J. (1999) Caspase-6 role in apoptosis of human neurons, amyloidogenesis, and Alzheimer's disease, J. Biol. Chem. 274, 23426-23436.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23426-23436
    • Leblanc, A.1    Liu, H.2    Goodyer, C.3    Bergeron, C.4    Hammond, J.5
  • 66
    • 0142179222 scopus 로고    scopus 로고
    • Caspase cleavage of the amyloid precursor protein modulates amyloid β-protein toxicity
    • Lu, D. C., Soriano, S., Bredesen, D. E., and Koo, E. H. (2003) Caspase cleavage of the amyloid precursor protein modulates amyloid β-protein toxicity, J. Neurochem. 87, 733-741.
    • (2003) J. Neurochem. , vol.87 , pp. 733-741
    • Lu, D.C.1    Soriano, S.2    Bredesen, D.E.3    Koo, E.H.4
  • 67
    • 0022550027 scopus 로고
    • Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
    • Roher, A., Wolfe, D., Palutke, M., and KuKuruga, D. (1986) Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein, Proc. Natl. Acad. Sci. U.S.A. 83, 2662-2666.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2662-2666
    • Roher, A.1    Wolfe, D.2    Palutke, M.3    Kukuruga, D.4
  • 68
    • 0024231238 scopus 로고
    • Isolation and chemical characterization of Alzheimer's disease paired helical filament cytoskeletons: Differentiation from amyloid plaque core protein
    • Roher, A. E., Palmer, K. C., Chau, V., and Ball, M. J. (1988) Isolation and chemical characterization of Alzheimer's disease paired helical filament cytoskeletons: Differentiation from amyloid plaque core protein, J. Cell Biol. 107, 2703-2716.
    • (1988) J. Cell Biol. , vol.107 , pp. 2703-2716
    • Roher, A.E.1    Palmer, K.C.2    Chau, V.3    Ball, M.J.4
  • 69
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue
    • Roher, A. E., Palmer, K. C., Yurewicz, E. C., Ball, M. J., and Greenberg, B. D. (1993) Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue, J. Neurochem. 61, 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
  • 73
    • 0036813085 scopus 로고    scopus 로고
    • Of mice and men: The relevance of transgenic mice Aβ immunizations to Alzheimer's disease
    • Roher, A. E., and Kokjohn, T. A. (2002) Of mice and men: The relevance of transgenic mice Aβ immunizations to Alzheimer's disease, J. Alzheimer's Dis. 4, 431-434.
    • (2002) J. Alzheimer's Dis. , vol.4 , pp. 431-434
    • Roher, A.E.1    Kokjohn, T.A.2
  • 74
    • 15944377414 scopus 로고    scopus 로고
    • Amyloid β degradation: A challenging task for brain peptidases
    • Morelli, L., Bulloj, A., Leal, M. C., and Castano, E. M. (2005) Amyloid β degradation: A challenging task for brain peptidases, Subcell. Biochem. 38, 129-145.
    • (2005) Subcell. Biochem. , vol.38 , pp. 129-145
    • Morelli, L.1    Bulloj, A.2    Leal, M.C.3    Castano, E.M.4
  • 75
    • 13644266898 scopus 로고    scopus 로고
    • Age- and region-dependent alterations in Aβ-degrading enzymes: Implications for Aβ-induced disorders
    • Caccamo, A., Oddo, S., Sugarman, M. C., Akbari, Y., and LaFerla, F. M. (2005) Age- and region-dependent alterations in Aβ-degrading enzymes: Implications for Aβ-induced disorders, Neurobiol. Aging 26, 645-654.
    • (2005) Neurobiol. Aging , vol.26 , pp. 645-654
    • Caccamo, A.1    Oddo, S.2    Sugarman, M.C.3    Akbari, Y.4    LaFerla, F.M.5
  • 77
    • 11244276934 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in brain microvessels: Proteolysis of amyloid {β} vasculotropic variants and reduced activity in cerebral amyloid angiopathy
    • Morelli, L., Llovera, R. E., Mathov, I., Lue, L. F., Frangione, B., Ghiso, J., and Castano, E. M. (2004) Insulin-degrading enzyme in brain microvessels: Proteolysis of amyloid {β} vasculotropic variants and reduced activity in cerebral amyloid angiopathy, J. Biol. Chem. 279, 56004-56013.
    • (2004) J. Biol. Chem. , vol.279 , pp. 56004-56013
    • Morelli, L.1    Llovera, R.E.2    Mathov, I.3    Lue, L.F.4    Frangione, B.5    Ghiso, J.6    Castano, E.M.7
  • 79
    • 0141596079 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease: Phenotype and application
    • Higgins, G. A., and Jacobsen, H. (2003) Transgenic mouse models of Alzheimer's disease: Phenotype and application, Behav. Pharmacol. 14, 419-438.
    • (2003) Behav. Pharmacol. , vol.14 , pp. 419-438
    • Higgins, G.A.1    Jacobsen, H.2
  • 80
    • 0042285737 scopus 로고    scopus 로고
    • What can rodent models tell us about cognitive decline in Alzheimer's disease?
    • Davis, S., and Laroche, S. (2003) What can rodent models tell us about cognitive decline in Alzheimer's disease? Mol. Neurobiol 27, 249-276.
    • (2003) Mol. Neurobiol. , vol.27 , pp. 249-276
    • Davis, S.1    Laroche, S.2
  • 81
    • 0038632272 scopus 로고    scopus 로고
    • Learning and memory deficits in APP transgenic mouse models of amyloid deposition
    • Morgan, D. (2003) Learning and memory deficits in APP transgenic mouse models of amyloid deposition, Neurochem. Res. 28, 1029-1034.
    • (2003) Neurochem. Res. , vol.28 , pp. 1029-1034
    • Morgan, D.1
  • 82
    • 0030664076 scopus 로고    scopus 로고
    • Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells
    • Paresce, D. M., Chung, H., and Maxfield, F. R. (1997) Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells, J. Biol. Chem. 272, 29397.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29397
    • Paresce, D.M.1    Chung, H.2    Maxfield, F.R.3
  • 83
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid β-peptide by microglial cells
    • Chung, H., Brazil, M. I., Soe, T. T., and Maxfield, F. R. (1999) Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid β-peptide by microglial cells, J. Biol. Chem. 274, 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


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