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Volumn 25, Issue 2, 1999, Pages 81-97

The amyloid precursor protein of Alzheimer's disease and the Aβ peptide

Author keywords

Aggregation; Genetic transmission; Heparin binding; Neurotoxicity; Oxidative stress

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; COPPER; HEPARIN BINDING PROTEIN; MEMBRANE PROTEIN; PRESENILIN 1; PRESENILIN 2; TAU PROTEIN; ZINC;

EID: 0032902647     PISSN: 03051846     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2990.1999.00164.x     Document Type: Review
Times cited : (144)

References (202)
  • 1
    • 0028984919 scopus 로고
    • Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells
    • 1 Asami-Odaka A, Ishibashi Y, Kikuchi T, Kitada C, Suzuki N. Long amyloid β-protein secreted from wild-type human neuroblastoma IMR-32 cells. Biochemistry 1995; 34: 10272-8
    • (1995) Biochemistry , vol.34 , pp. 10272-10278
    • Asami-Odaka, A.1    Ishibashi, Y.2    Kikuchi, T.3    Kitada, C.4    Suzuki, N.5
  • 2
    • 0028912956 scopus 로고
    • Role of cyclic GMP in the regulation of neuronal calcium and survival by secreted forms of b-amyloid precursor
    • 2 Barger SW, Fiscus RR, Ruth P, Hofmann F, Mattson MP. Role of cyclic GMP in the regulation of neuronal calcium and survival by secreted forms of b-amyloid precursor. J Neurochem 1995; 64: 2087-96
    • (1995) J Neurochem , vol.64 , pp. 2087-2096
    • Barger, S.W.1    Fiscus, R.R.2    Ruth, P.3    Hofmann, F.4    Mattson, M.P.5
  • 3
    • 0030222080 scopus 로고    scopus 로고
    • Induction of neuroprotective kB-dependent transcription by secreted forms of the Alzheimers b-amyloid precursor
    • 3 Barger SW, Mattson MP. Induction of neuroprotective kB-dependent transcription by secreted forms of the Alzheimers b-amyloid precursor. Mol Brain Res 1996; 40: 116-26
    • (1996) Mol Brain Res , vol.40 , pp. 116-126
    • Barger, S.W.1    Mattson, M.P.2
  • 4
    • 0030030005 scopus 로고    scopus 로고
    • Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I
    • 4 Beher D, Hesse L, Masters CL, Multhaup G. Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I. J Biol Chem 1996; 271: 13-20
    • (1996) J Biol Chem , vol.271 , pp. 13-20
    • Beher, D.1    Hesse, L.2    Masters, C.L.3    Multhaup, G.4
  • 5
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • 5 Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 1994; 77: 817-27
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 6
    • 0029988367 scopus 로고    scopus 로고
    • Regulation of APP expression, biogenesis and metabolism by extracellular matrix and cytokines
    • 6 Beyreuther K, Multhaup G, Monning U et al. Regulation of APP expression, biogenesis and metabolism by extracellular matrix and cytokines. Ann NY Acad Sci 1996; 777: 74-6
    • (1996) Ann NY Acad Sci , vol.777 , pp. 74-76
    • Beyreuther, K.1    Multhaup, G.2    Monning, U.3
  • 7
    • 0023731159 scopus 로고
    • Familial Alzheimer's disease in American descendants of the Volga Germans: Probable genetic founder effect
    • 7 Bird TD, Lampe TH, Nemens ET, Miner GW, Sumi SM, Schellenberg GD. Familial Alzheimer's disease in American descendants of the Volga Germans: probable genetic founder effect. Ann Neurol 1988; 23: 25-31
    • (1988) Ann Neurol , vol.23 , pp. 25-31
    • Bird, T.D.1    Lampe, T.H.2    Nemens, E.T.3    Miner, G.W.4    Sumi, S.M.5    Schellenberg, G.D.6
  • 8
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo
    • 8 Borchelt DR, Thinakaran G, Eckman CB et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 1996; 17: 1005-13
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 9
    • 0029894227 scopus 로고    scopus 로고
    • Hereditary cerebral haemorrhage with amyloidosis-Dutch type (HCHWA-D): I - A review of clinical, radiologic and genetic aspects
    • 9 Bornebrock M, Haan J, Maat-Schieman MLC, Van Duinen SG, Roos RAC. Hereditary cerebral haemorrhage with amyloidosis-Dutch type (HCHWA-D): I - a review of clinical, radiologic and genetic aspects. Brain Pathol 1996; 6: 111-4
    • (1996) Brain Pathol , vol.6 , pp. 111-114
    • Bornebrock, M.1    Haan, J.2    Maat-Schieman, M.L.C.3    Van Duinen, S.G.4    Roos, R.A.C.5
  • 10
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs
    • 10 Burdick D, Soreghan B, Kwon M et al. Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J Biol Chem 1992; 267: 546-54
    • (1992) J Biol Chem , vol.267 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3
  • 11
    • 0028986916 scopus 로고
    • β-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • 11 Busciglio J, Lorenzo A, Yeh J, Yankner BA. β-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 1995; 14: 879-88
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 12
    • 0027220686 scopus 로고
    • A novel zinc (II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease
    • 12 Bush AI, Multhaup G, Moir RD et al. A novel zinc (II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease. J Biol Chem 1993; 268: 16109-12
    • (1993) J Biol Chem , vol.268 , pp. 16109-16112
    • Bush, A.I.1    Multhaup, G.2    Moir, R.D.3
  • 13
    • 0027980901 scopus 로고
    • Rapid induction of Alzheimer Aβ amyloid formation by Zinc
    • 13 Bush AI, Pettingell WH, Multhaup G et al. Rapid induction of Alzheimer Aβ amyloid formation by Zinc. Science 1994; 265: 1464-7
    • (1994) Science , vol.265 , pp. 1464-1467
    • Bush, A.I.1    Pettingell, W.H.2    Multhaup, G.3
  • 14
    • 0028171064 scopus 로고
    • The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily
    • 14 Bush AI, Pettingell WJ, de Paradis M, Tanzi RE, Wasco W. The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. J Biol Chem 1994; 269: 26618-21
    • (1994) J Biol Chem , vol.269 , pp. 26618-26621
    • Bush, A.I.1    Pettingell, W.J.2    De Paradis, M.3    Tanzi, R.E.4    Wasco, W.5
  • 15
    • 0028178837 scopus 로고
    • β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-sperific fashion: Implications to Alzheimer's disease
    • 15 Butterfield DA, Hensley K, Harris M, Mattson M, Carney J. β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-sperific fashion: implications to Alzheimer's disease. Biochem Biophys Res Commun 1994; 200: 710-5
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.5
  • 16
    • 0025296205 scopus 로고
    • Processing of Alzheimer β/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation
    • 16 Buxbaum JD, Gandy SE, Cicehetti P et al. Processing of Alzheimer β/A4 amyloid precursor protein: modulation by agents that regulate protein phosphorylation. Proc Natl Acad Sci USA 1990; 87: 6003-6
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6003-6006
    • Buxbaum, J.D.1    Gandy, S.E.2    Cicehetti, P.3
  • 17
    • 0029983525 scopus 로고    scopus 로고
    • Regulation of APP processing by intra-and intercellular signals
    • 17 Buxbaum JD, Greengard P. Regulation of APP processing by intra-and intercellular signals. Ann NY Acad Sci 1996; 777: 327-31
    • (1996) Ann NY Acad Sci , vol.777 , pp. 327-331
    • Buxbaum, J.D.1    Greengard, P.2
  • 18
    • 0028207004 scopus 로고
    • Calcium regulates processing of the Alzheimer amyloid protein precursor in a protein kinase C-independent manner
    • 18 Buxbaum JD, Ruefli AA, Parker CA, Cypess AM, Greengard P. Calcium regulates processing of the Alzheimer amyloid protein precursor in a protein kinase C-independent manner. Proc Natl Acad Sci USA 1994; 91: 4489-93
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4489-4493
    • Buxbaum, J.D.1    Ruefli, A.A.2    Parker, C.A.3    Cypess, A.M.4    Greengard, P.5
  • 19
    • 0027526419 scopus 로고
    • Release of excess amyloid β protein from a mutant amyloid β protein precursor
    • 19 Cai X-D, Golde TE, Younkin SG. Release of excess amyloid β protein from a mutant amyloid β protein precursor. Science 1993; 259: 514-6
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.-D.1    Golde, T.E.2    Younkin, S.G.3
  • 20
    • 19244363543 scopus 로고    scopus 로고
    • No founder effect in three novel Alzheimer's disease families with APP. 717 Valα(r) Ile mutation
    • 20 Campion D, Brice A, Hannequin D et al. No founder effect in three novel Alzheimer's disease families with APP. 717 Valα(r) Ile mutation. J Med Genet 1996; 33: 661-4
    • (1996) J Med Genet , vol.33 , pp. 661-664
    • Campion, D.1    Brice, A.2    Hannequin, D.3
  • 21
    • 0026589836 scopus 로고
    • Chloroquine inhibits intracellular degradation but not secretion of Alzheimer β/A4 amyloid precursor protein
    • 21 Caporaso GL, Gandy SE, Buxbaum JD, Greengard P. Chloroquine inhibits intracellular degradation but not secretion of Alzheimer β/A4 amyloid precursor protein. Proc Natl Acad Sci USA 1992; 89: 2252-6
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2252-2256
    • Caporaso, G.L.1    Gandy, S.E.2    Buxbaum, J.D.3    Greengard, P.4
  • 22
    • 0026745610 scopus 로고
    • Mutation of the β-amyloid protein in familial Alzheimer's disease increases β-protein production
    • 22 Citron M, Oltersdorf T, Haass C et al. Mutation of the β-amyloid protein in familial Alzheimer's disease increases β-protein production. Nature 1992; 360: 672-4
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3
  • 23
    • 0028924248 scopus 로고
    • Generation of amyloid beta protein from its precursor is sequence specific
    • 23 Citron M, Teplow DB, Selkoe DJ. Generation of amyloid beta protein from its precursor is sequence specific. Neuron 1995; 14: 661-70
    • (1995) Neuron , vol.14 , pp. 661-670
    • Citron, M.1    Teplow, D.B.2    Selkoe, D.J.3
  • 24
    • 0030199986 scopus 로고    scopus 로고
    • Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF
    • 24 Citron M, Diehl TS, Capell A, Haass C, Teplow DB, Selkoe DJ. Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF. Neuron 1996; 17: 171-9
    • (1996) Neuron , vol.17 , pp. 171-179
    • Citron, M.1    Diehl, T.S.2    Capell, A.3    Haass, C.4    Teplow, D.B.5    Selkoe, D.J.6
  • 25
    • 0029803744 scopus 로고    scopus 로고
    • Evidence that the 42-and 40-amino acid forms of amyloid β protein are generated from the β-amyloid precursor protein by different protease activities
    • 25 Citron M, Diehl TS, Gordon G, Biere AL, Seubert P, Selkoe DJ. Evidence that the 42-and 40-amino acid forms of amyloid β protein are generated from the β-amyloid precursor protein by different protease activities. Proc Natl Acad Sci USA 1996; 93: 13170-5
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13170-13175
    • Citron, M.1    Diehl, T.S.2    Gordon, G.3    Biere, A.L.4    Seubert, P.5    Selkoe, D.J.6
  • 26
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • 26 Citron M, Westaway D, Xia W et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat Med 1997; 3: 67-72
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 27
    • 0031026779 scopus 로고    scopus 로고
    • Identification of heparin-binding domains in the amyloid precursor protein of Alzheimer's disease by deletion mutagenesis and peptide mapping
    • 27 Clarris HJ, Cappai R, Heffernan D, Beyreuther K, Masters CL, Small DH. Identification of heparin-binding domains in the amyloid precursor protein of Alzheimer's disease by deletion mutagenesis and peptide mapping. J Neurochem 1997; 68: 1164-72
    • (1997) J Neurochem , vol.68 , pp. 1164-1172
    • Clarris, H.J.1    Cappai, R.2    Heffernan, D.3    Beyreuther, K.4    Masters, C.L.5    Small, D.H.6
  • 28
    • 0022569856 scopus 로고
    • A heparin-binding domain from N-CAM is involved in neural cell-substratum adhesion
    • 28 Cole GJ, Glaser L. A heparin-binding domain from N-CAM is involved in neural cell-substratum adhesion. J Cell Biol 1986; 102: 403-12
    • (1986) J Cell Biol , vol.102 , pp. 403-412
    • Cole, G.J.1    Glaser, L.2
  • 29
    • 0029812077 scopus 로고    scopus 로고
    • Expression and analysis of presenilin 1 in a human neuronal system: Localization in cell bodies and dendrites
    • 29 Cook DG, Sung JC, Golde TE et al. Expression and analysis of presenilin 1 in a human neuronal system: localization in cell bodies and dendrites. Proc Natl Acad Sci USA 1996; 93: 9223-8
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9223-9228
    • Cook, D.G.1    Sung, J.C.2    Golde, T.E.3
  • 30
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • 30 Cook DG, Forman MS, Sung JC et al. Alzheimer's Aβ (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Med 1997; 3: 1021-3
    • (1997) Nature Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3
  • 31
    • 0031949628 scopus 로고    scopus 로고
    • A variant of Alzheimer's disease with spastic paraparesis and unusual plaques due to deletion of exon 9 of presenilin 1
    • 31 Crook R, Verkkoniemi A, Perez-Tur J et al. A variant of Alzheimer's disease with spastic paraparesis and unusual plaques due to deletion of exon 9 of presenilin 1. Nature Med 1998; 4: 452-5
    • (1998) Nature Med , vol.4 , pp. 452-455
    • Crook, R.1    Verkkoniemi, A.2    Perez-Tur, J.3
  • 32
    • 0027360352 scopus 로고
    • Regulated cleavage of Alzheimer β-amyloid precursor protein in the absence of the cytoplasmic tail
    • 32 da Cruz e Silva OA, Iverfeldt K, Oltersdorf T et al. Regulated cleavage of Alzheimer β-amyloid precursor protein in the absence of the cytoplasmic tail. Neuroscience 1993; 57: 873-7
    • (1993) Neuroscience , vol.57 , pp. 873-877
    • Da Cruz E Silva, O.A.1    Iverfeldt, K.2    Oltersdorf, T.3
  • 33
    • 0027333449 scopus 로고
    • apl-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor
    • 33 Daigle I, Li C. apl-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor. Proc Natl Acad Sci USA 1993; 90: 12045-9
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 12045-12049
    • Daigle, I.1    Li, C.2
  • 34
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • 34 De Strooper B, Saftig P, Craessaerts K et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 1998; 391: 387-90
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3
  • 35
    • 0030293854 scopus 로고    scopus 로고
    • Protein topology of presenilin 1
    • 35 Doan A, Thinakaran G, Borchelt DR et al. Protein topology of presenilin 1. Neuron 1996; 17: 1023-30
    • (1996) Neuron , vol.17 , pp. 1023-1030
    • Doan, A.1    Thinakaran, G.2    Borchelt, D.R.3
  • 36
    • 16044366039 scopus 로고    scopus 로고
    • Increased Amyloid-β in brains of mice expressing mutant presenilin 1
    • 36 Duff K, Eckman C, Zehr C et al. Increased Amyloid-β in brains of mice expressing mutant presenilin 1. Nature 1996; 42: 710-3
    • (1996) Nature , vol.42 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3
  • 37
    • 0031900476 scopus 로고    scopus 로고
    • Transgenic models for Alzheimer's disease
    • 37 Duff K. Transgenic models for Alzheimer's disease. Neuropathol Appl Neurobiol 1998; 24: 101-3
    • (1998) Neuropathol Appl Neurobiol , vol.24 , pp. 101-103
    • Duff, K.1
  • 38
    • 9844261165 scopus 로고    scopus 로고
    • A new pathogenic mutation in the APP gene (1716V) increases the relative proportion of A β 42 (43)
    • 38 Eckman CB, Mehta ND, Crook R et al. A new pathogenic mutation in the APP gene (1716V) increases the relative proportion of A β 42 (43). Hum Mol Genet 1997; 6: 2087-9
    • (1997) Hum Mol Genet , vol.6 , pp. 2087-2089
    • Eckman, C.B.1    Mehta, N.D.2    Crook, R.3
  • 39
    • 0025295039 scopus 로고
    • Cleavage of amyloid β peptide during constitutive processing of its precursor
    • 39 Esch FS, Keim PS, Beattie EC et al. Cleavage of amyloid β peptide during constitutive processing of its precursor. Science 1990; 248: 1122-4
    • (1990) Science , vol.248 , pp. 1122-1124
    • Esch, F.S.1    Keim, P.S.2    Beattie, E.C.3
  • 40
    • 0026522375 scopus 로고
    • Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor
    • 40 Estus S, Golde TE, Kunishita T et al. Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor. Science 1992; 255: 726-8
    • (1992) Science , vol.255 , pp. 726-728
    • Estus, S.1    Golde, T.E.2    Kunishita, T.3
  • 41
    • 0023880109 scopus 로고
    • Oral zinc supplementation in Down's syndrome: Restoration of thymic endocrine activity and of some immune defects
    • 41 Franceschi C, Chiricolo M, Licastro F et al. Oral zinc supplementation in Down's syndrome: restoration of thymic endocrine activity and of some immune defects. J Ment Defic Res 1988; 32: 169-81
    • (1988) J Ment Defic Res , vol.32 , pp. 169-181
    • Franceschi, C.1    Chiricolo, M.2    Licastro, F.3
  • 42
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • 42 Fraser PE, Nguyen JT, Chin DT, Kirschner DA. Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. J Neurochem 1992; 59: 1531-40
    • (1992) J Neurochem , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 43
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • 43 Frederickson CJ. Neurobiology of zinc and zinc-containing neurons. Int Rev Neurobiol 1989; 31: 145-238
    • (1989) Int Rev Neurobiol , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 44
    • 0030064140 scopus 로고    scopus 로고
    • Amyloid β-protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance Aβ and association of Aβ40 with cored plaques
    • 44 Fukumoto H, Asami-Odaka A, Suzuki N, Shimada H, Ihara Y, Iwatsubo T. Amyloid β-protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance Aβ and association of Aβ40 with cored plaques. Am J Path 1996; 148: 259-65
    • (1996) Am J Path , vol.148 , pp. 259-265
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Shimada, H.4    Ihara, Y.5    Iwatsubo, T.6
  • 45
    • 0028980783 scopus 로고
    • Intracellular production of β5A4 amyloid of Alzheimer's disease, modulation by phosphoramidon and lack of coupling to the secretion of the amyloid precursor protein
    • 45 Fuller SJ, Storey E, Li Q-X, Smith AI, Beyreuther K, Masters CL. Intracellular production of β5A4 amyloid of Alzheimer's disease, modulation by phosphoramidon and lack of coupling to the secretion of the amyloid precursor protein. Biochemistry 1995; 34: 8091-8
    • (1995) Biochemistry , vol.34 , pp. 8091-8098
    • Fuller, S.J.1    Storey, E.2    Li, Q.-X.3    Smith, A.I.4    Beyreuther, K.5    Masters, C.L.6
  • 46
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of a-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain
    • 46 Furukawa K, Sopher BL, Rydel RE et al. Increased activity-regulating and neuroprotective efficacy of a-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain. J Neurochem 1996; 67: 1882-96
    • (1996) J Neurochem , vol.67 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.L.2    Rydel, R.E.3
  • 47
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • 47 Gabuzda D, Busciglio J, Chen LB, Mitsudaira P, Yankner BA. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J Biol Chem 1994; 269: 13623-8
    • (1994) J Biol Chem , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Mitsudaira, P.4    Yankner, B.A.5
  • 49
    • 0027082156 scopus 로고
    • A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion
    • 49 Ghiso J, Rostagno A, Gardella JE, Liem L, Gorevic PD, Frangione B. A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion. Biochem J 1992; 288: 1053-9
    • (1992) Biochem J , vol.288 , pp. 1053-1059
    • Ghiso, J.1    Rostagno, A.2    Gardella, J.E.3    Liem, L.4    Gorevic, P.D.5    Frangione, B.6
  • 50
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • 50 Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984; 120: 885-90
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 51
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • 51 Goate A, Chartier-Harlin M-C, Mullan M et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991; 349: 704-6
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.-C.2    Mullan, M.3
  • 52
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • 52 Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 1996; 383: 550-3
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 53
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • 53 Golde TE, Estus S, Younkin LH, Selkoe DJ, Younkin SG. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 1992; 255: 728-30
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 54
    • 0028169905 scopus 로고
    • Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury
    • 54 Goodman Y, Mattson MP. Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury. Exp Neurol 1994; 128: 1-12
    • (1994) Exp Neurol , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 55
    • 0028179341 scopus 로고
    • Chemical characterization of Aβ 17 42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
    • 55 Gowing E, Roher AE, Woods AS et al. Chemical characterization of Aβ 17 42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. J Biol Chem 1994; 269: 10987-90
    • (1994) J Biol Chem , vol.269 , pp. 10987-10990
    • Gowing, E.1    Roher, A.E.2    Woods, A.S.3
  • 56
    • 0028915895 scopus 로고
    • Amyloid beta protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Aβ40 or Aβ
    • 56 Gravina SA, Ho L, Eckman CB et al. Amyloid beta protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Aβ40 or Aβ. J Biol Chem 1995;270: 7013-6
    • (1995) J Biol Chem , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3
  • 57
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • 57 Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ. Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 1992; 357: 500-3
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 58
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • 58 Haass C, Schlossmacher MG, Hung AY et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 1992; 359: 322-5
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1    Schlossmacher, M.G.2    Hung, A.Y.3
  • 59
    • 0027535111 scopus 로고
    • β-amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • 59 Haass C, Hung AY, Schlossmacher MG, Teplow DB, Selkoe DJ. β-amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J Biol Chem 1993; 268: 3021-4
    • (1993) J Biol Chem , vol.268 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.J.5
  • 60
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor
    • 60 Haass C, Hung AY, Selkoe DJ, Teplow DJ. Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid β-protein precursor. J Biol Chem 1994; 269: 17741-8
    • (1994) J Biol Chem , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.J.4
  • 61
    • 0028922667 scopus 로고
    • 1 differentially affects proteolytic processing of mutant and wild-type β-amyloid precusor protein
    • 1 differentially affects proteolytic processing of mutant and wild-type β-amyloid precusor protein. J Biol Chem 1995; 270: 6186-92
    • (1995) J Biol Chem , vol.270 , pp. 6186-6192
    • Haass, C.1    Capell, A.2    Citron, M.3    Teplow, D.B.4    Selkoe, D.J.5
  • 62
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • 62 Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci 1997; 20: 154-9
    • (1997) Trends Neurosci , vol.20 , pp. 154-159
    • Hardy, J.1
  • 64
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease Aβ 40/42 amyloid peptides
    • 64 Hartmann T, Bieger SC, Brühl B et al. Distinct sites of intracellular production for Alzheimer's disease Aβ 40/42 amyloid peptides. Nature Med 1997; 3: 1016-20
    • (1997) Nature Med , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Brühl, B.3
  • 65
    • 0026879650 scopus 로고
    • Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β-amyloid precursor protein gene
    • 65 Hendriks L, van Duijn CM, Cras P et al. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β-amyloid precursor protein gene. Nature Genet 1992; 1: 218-21
    • (1992) Nature Genet , vol.1 , pp. 218-221
    • Hendriks, L.1    Van Duijn, C.M.2    Cras, P.3
  • 66
    • 0028177269 scopus 로고
    • The beta A4 amyloid precursor protein binding to copper
    • 66 Hesse L, Beher D, Masters CL, Multhaup G. The beta A4 amyloid precursor protein binding to copper. FEBS Lett 1994; 349: 109-16
    • (1994) FEBS Lett , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 67
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA. 4 peptides of Alzheimer's disease
    • 67 Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K. Aggregation and secondary structure of synthetic amyloid βA. 4 peptides of Alzheimer's disease. J Mol Biol 1991; 218: 149-63
    • (1991) J Mol Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 68
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • 68 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
  • 69
    • 0029034927 scopus 로고
    • Aggregation state and neurotoxic properties of Alzheimer β-amyloid peptide
    • 69 Howlett DR, Jennings KH, Lee DC et al. Aggregation state and neurotoxic properties of Alzheimer β-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
  • 70
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • 70 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
  • 71
    • 9344237637 scopus 로고    scopus 로고
    • Complete analysis of the presenilin 1 gene in early onset Alzheimer's disease
    • 71 Hutton M, Busfield F, Wragg M et al. Complete analysis of the presenilin 1 gene in early onset Alzheimer's disease. Neuroreport 1996; 7: 801-5
    • (1996) Neuroreport , vol.7 , pp. 801-805
    • Hutton, M.1    Busfield, F.2    Wragg, M.3
  • 72
    • 0028919919 scopus 로고
    • Amyloid beta protein (A β) deposition: A β precedes A β 40 in Down Syndrome
    • 72 Iwatsubo T, Mann DM, Odaka A, Suzuki N, Ihara Y. Amyloid beta protein (A β) deposition: a β precedes A β 40 in Down Syndrome. Ann Neurol 1995; 37: 294-9
    • (1995) Ann Neurol , vol.37 , pp. 294-299
    • Iwatsubo, T.1    Mann, D.M.2    Odaka, A.3    Suzuki, N.4    Ihara, Y.5
  • 73
    • 0028169925 scopus 로고
    • Visualization of Aβ42 (43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ
    • 73 Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Aβ42 (43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ. Neuron 1994; 13: 45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 74
    • 0028246846 scopus 로고
    • The release of Alzheimer's disease β-amyloid peptide is reduced by phorbol treatment
    • 74 Jacobsen JS. Spruyt MA, Brown AM et al. The release of Alzheimer's disease β-amyloid peptide is reduced by phorbol treatment. J Biol Chem 1994; 269: 8376-82
    • (1994) J Biol Chem , vol.269 , pp. 8376-8382
    • Jacobsen, J.S.1    Spruyt, M.A.2    Brown, A.M.3
  • 75
    • 0028342424 scopus 로고
    • Estrogen regulates metabolism of Alzheimer amyloid β precursor protein
    • 75 Jaffe AB, Toran-Allerand CD, Greengard P, Gandy SE. Estrogen regulates metabolism of Alzheimer amyloid β precursor protein. J Biol Chem 1994; 269: 13065-8
    • (1994) J Biol Chem , vol.269 , pp. 13065-13068
    • Jaffe, A.B.1    Toran-Allerand, C.D.2    Greengard, P.3    Gandy, S.E.4
  • 76
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallisation' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • 76 Jarrett JT, Lansbury PT, Jnr. Seeding 'one-dimensional crystallisation' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73: 1055-8
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jnr.2
  • 77
    • 0027258525 scopus 로고
    • The carboxy terminus of β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • 77 Jarrett JT, Berger EP, Lansbury PT, Jnr. The carboxy terminus of β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993; 32: 4693-7
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 78
    • 0024232950 scopus 로고
    • Protein chemical and immunocytochemical studies of meningovascular β-amyloid protein in Alzheimer's disease and normal aging
    • 78 Joachim CL, Duffy LK, Morris JH, Selkoe DJ. Protein chemical and immunocytochemical studies of meningovascular β-amyloid protein in Alzheimer's disease and normal aging. Brain Res 1988; 474: 100-11
    • (1988) Brain Res , vol.474 , pp. 100-111
    • Joachim, C.L.1    Duffy, L.K.2    Morris, J.H.3    Selkoe, D.J.4
  • 79
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • 79 Kang J, Lemaire H-G, Unterbeck A et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987; 325: 733-6
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3
  • 80
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport and inducation of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • 80 Keller JN, Pang Z, Geddes JW et al. Impairment of glucose and glutamate transport and inducation of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: role of the lipid peroxidation product 4-hydroxynonenal. J Neurochem 1997; 69: 273-84
    • (1997) J Neurochem , vol.69 , pp. 273-284
    • Keller, J.N.1    Pang, Z.2    Geddes, J.W.3
  • 81
    • 0029905596 scopus 로고    scopus 로고
    • The carboxyl termini of beta-amyloid peptides 1 -40 and 1 -42 are generated by distinct gamma-secretase activities
    • 81 Klafki H, Abramowski D, Swoboda R, Paganetti PA, Staufenbiel M. The carboxyl termini of beta-amyloid peptides 1 -40 and 1 -42 are generated by distinct gamma-secretase activities. J Biol Chem 1996; 271: 28655-9
    • (1996) J Biol Chem , vol.271 , pp. 28655-28659
    • Klafki, H.1    Abramowski, D.2    Swoboda, R.3    Paganetti, P.A.4    Staufenbiel, M.5
  • 82
    • 0021022617 scopus 로고
    • Protease nexins: Cell-secreted proteins that mediate the binding, internalization and degradation of regulatory serine proteases
    • 82 Knauer DJ, Thompson JA, Cunningham DD. Protease nexins: cell-secreted proteins that mediate the binding, internalization and degradation of regulatory serine proteases. J Cell Physiol 1983; 117: 385-96
    • (1983) J Cell Physiol , vol.117 , pp. 385-396
    • Knauer, D.J.1    Thompson, J.A.2    Cunningham, D.D.3
  • 83
    • 0030592750 scopus 로고    scopus 로고
    • Cell surface APP. 751 forms complexes with protease nexin 2 ligands and is internalized via the low density lipoprotein receptor-related protein (LRP)
    • 83 Knauer MF, Orlando RA, Glabe CG. Cell surface APP. 751 forms complexes with protease nexin 2 ligands and is internalized via the low density lipoprotein receptor-related protein (LRP). Brain Res 1996; 740: 6-14
    • (1996) Brain Res , vol.740 , pp. 6-14
    • Knauer, M.F.1    Orlando, R.A.2    Glabe, C.G.3
  • 85
    • 0025110182 scopus 로고
    • β-amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage
    • 85 Koh J-Y, Yang LL, Cotman CW. β-amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage. Brain Res 1990; 533: 315-20
    • (1990) Brain Res , vol.533 , pp. 315-320
    • Koh, J.-Y.1    Yang, L.L.2    Cotman, C.W.3
  • 87
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • 87 Koo EH, Squazzo SL. Evidence that production and release of amyloid β-protein involves the endocytic pathway. J Biol Chem 1994; 269: 17386-9
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 88
    • 0030897134 scopus 로고    scopus 로고
    • 717 Alzheimer mutation increases the percentage of plasma amyloid-β protein ending at Aβ
    • 717 Alzheimer mutation increases the percentage of plasma amyloid-β protein ending at Aβ. Neurology 1997; 48: 741-5
    • (1997) Neurology , vol.48 , pp. 741-745
    • Kosaka, T.1    Imagawa, M.2    Seki, K.3
  • 89
    • 0029128232 scopus 로고
    • LDL receptor-relaled protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation
    • 89 Kounnas MZ, Moir RD, Rebeck GW et al. LDL receptor-relaled protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation. Cell 1995; 82: 331-40
    • (1995) Cell , vol.82 , pp. 331-340
    • Kounnas, M.Z.1    Moir, R.D.2    Rebeck, G.W.3
  • 90
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • 90 Kovacs DM, Fausett HJ, Page KJ et al. Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat Med 1996; 2: 224-9
    • (1996) Nat Med , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3
  • 91
    • 0025879957 scopus 로고
    • An in vivo model for the neurodegenerative effects of β amyloid and protection by substance P
    • 91 Kowall NW, Beal MF, Busciglio J, Duffy LK, Yankner BA. An in vivo model for the neurodegenerative effects of β amyloid and protection by substance P. Proc Natl Acad Sci USA 1991; 88: 7247-51
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7247-7251
    • Kowall, N.W.1    Beal, M.F.2    Busciglio, J.3    Duffy, L.K.4    Yankner, B.A.5
  • 92
    • 0027484116 scopus 로고
    • The Alzheimer β-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells
    • 92 Kuentzel SL, Ali KM, Altman RA, Greenberg BD, Raub TJ. The Alzheimer β-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells. Biochem J 1993; 295: 367-78
    • (1993) Biochem J , vol.295 , pp. 367-378
    • Kuentzel, S.L.1    Ali, K.M.2    Altman, R.A.3    Greenberg, B.D.4    Raub, T.J.5
  • 93
    • 0032523039 scopus 로고    scopus 로고
    • Protein Kinase C activation increases release of secreted amyloid precursor protein without decreasing Aβ production in human primary neuronal cultures
    • 93 Le Blanc AC, Koutroumanis M, Goodyer CG, Protein Kinase C activation increases release of secreted amyloid precursor protein without decreasing Aβ production in human primary neuronal cultures. J Neurosci 1998; 18: 2907-13
    • (1998) J Neurosci , vol.18 , pp. 2907-2913
    • Le Blanc, A.C.1    Koutroumanis, M.2    Goodyer, C.G.3
  • 94
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • 94 Lemere CA, Lopera F, Kosik KS et al. The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nature Med 1996; 2: 1146-50
    • (1996) Nature Med , vol.2 , pp. 1146-1150
    • Lemere, C.A.1    Lopera, F.2    Kosik, K.S.3
  • 95
    • 0031057837 scopus 로고    scopus 로고
    • Exploring the etiology of Alzheimer disease using molecular genetics
    • 95 Lendon CL, Ashall F, Goate AM. Exploring the etiology of Alzheimer disease using molecular genetics. JAMA 1997; 277: 825-31
    • (1997) JAMA , vol.277 , pp. 825-831
    • Lendon, C.L.1    Ashall, F.2    Goate, A.M.3
  • 96
    • 0025296269 scopus 로고
    • Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral haemorrhage, Dutch-type
    • 96 Levy E, Carman MD, Fernandez-Madrid IJ et al. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral haemorrhage, Dutch-type. Science 1990; 248: 1124-6
    • (1990) Science , vol.248 , pp. 1124-1126
    • Levy, E.1    Carman, M.D.2    Fernandez-Madrid, I.J.3
  • 97
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • 97 Levy-Lahad E, Wasco W, Poorkaj P et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 1995; 269: 973-7
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 98
    • 0029618686 scopus 로고
    • Identification and expression analysis of a potential familial Alzheimer disease gene on chromosome 1 related to AD 3
    • 98 Li J, Ma J, Potter H. Identification and expression analysis of a potential familial Alzheimer disease gene on chromosome 1 related to AD 3. Proc Natl Acad Sci USA 1995; 92: 12180-4
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12180-12184
    • Li, J.1    Ma, J.2    Potter, H.3
  • 99
    • 0028179851 scopus 로고
    • Membrane-associated forms of the ïïbA4 amyloid protein precursor of Alzheimer's disease in human platelet and brain: Surface expression on the activated human platelet
    • 99 Li QX, Berndt MC, Bush AI et al. Membrane-associated forms of the ïïbA4 amyloid protein precursor of Alzheimer's disease in human platelet and brain: surface expression on the activated human platelet. Blood 1994; 84: 113-42
    • (1994) Blood , vol.84 , pp. 113-142
    • Li, Q.X.1    Berndt, M.C.2    Bush, A.I.3
  • 100
    • 0029040554 scopus 로고
    • Proteolytic processing of Alzheimer's disease beta A. 4 amyloid precursor protein in human platelets
    • 100 Li QX, Evin G, Small DH, Multhaup G, Beyreuther K, Masters CL. Proteolytic processing of Alzheimer's disease beta A. 4 amyloid precursor protein in human platelets. J Biol Chem 1995; 270: 14140-7
    • (1995) J Biol Chem , vol.270 , pp. 14140-14147
    • Li, Q.X.1    Evin, G.2    Small, D.H.3    Multhaup, G.4    Beyreuther, K.5    Masters, C.L.6
  • 101
    • 0030293894 scopus 로고    scopus 로고
    • Membrane topology of the C. Elegans SEL-12 presenilin
    • 101 Li X, Greenwald I. Membrane topology of the C. elegans SEL-12 presenilin. Neuron 1996; 17: 1015-21
    • (1996) Neuron , vol.17 , pp. 1015-1021
    • Li, X.1    Greenwald, I.2
  • 102
    • 0017831892 scopus 로고
    • Glycosaminoglycans and their binding to biological macromolecules
    • 102 Lindahl U, Höök M. Glycosaminoglycans and their binding to biological macromolecules. Ann Rev Biochem 1978; 47: 385-417
    • (1978) Ann Rev Biochem , vol.47 , pp. 385-417
    • Lindahl, U.1    Höök, M.2
  • 103
    • 0028172886 scopus 로고
    • β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • 103 Lorenzo A, Yankner BA. β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci USA 1994; 91: 12243-7
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 104
    • 0028787671 scopus 로고
    • Protease nexin-2 amyloid β-protein precursor inhibits factor Xa in the prothrombinase complex
    • 104 Mahdi F, Van Nostrand WE, Schmaier AH. Protease nexin-2 amyloid β-protein precursor inhibits factor Xa in the prothrombinase complex. J Biol Chem 1995; 270: 25468-74
    • (1995) J Biol Chem , vol.270 , pp. 25468-25474
    • Mahdi, F.1    Van Nostrand, W.E.2    Schmaier, A.H.3
  • 105
    • 0030614569 scopus 로고    scopus 로고
    • Amyloid (A β) deposition in chromosome 1 linked Alzheimer disease: The Volga German families
    • 105 Mann DM, Iwatsubo T, Nochlin D, Sumi SM, Levy-Lahad E, Bird TD. Amyloid (A β) deposition in chromosome 1 linked Alzheimer disease: the Volga German families. Ann Neurol 1997; 41: 52-7
    • (1997) Ann Neurol , vol.41 , pp. 52-57
    • Mann, D.M.1    Iwatsubo, T.2    Nochlin, D.3    Sumi, S.M.4    Levy-Lahad, E.5    Bird, T.D.6
  • 106
    • 0027327488 scopus 로고
    • Aluminium, Iron, and Zinc ions promote aggregation of physiological concentrations of β-amyloid peptide
    • 106 Mantyh PW, Ghilardi JR. Rogers S et al. Aluminium, Iron, and Zinc ions promote aggregation of physiological concentrations of β-amyloid peptide. J Neurochem 1993; 61: 1171-4
    • (1993) J Neurochem , vol.61 , pp. 1171-1174
    • Mantyh, P.W.1    Ghilardi, J.R.2    Rogers, S.3
  • 107
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • 107 Mark RJ, Pang Z, Geddes JW, Uchida K, Mattson MP. Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J Neurosci 1997; 17: 1046-54
    • (1997) J Neurosci , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 109
    • 0026570528 scopus 로고
    • β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to exictotoxicity
    • 109 Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I, Rydel RE. β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to exictotoxicity. J Neurosci 1992; 12: 376-89
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 110
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein
    • 110 Mattson MP, Cheng B, Culwell AR, Esch FS, Lieberburg I, Rydel RE. Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein. Neuron 1993; 10: 243-54
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 111
    • 0028670780 scopus 로고
    • Increased numbers of bAPP-immunoreactive neurones in the entorhinal cortex after head injury
    • 111 McKenzie JE, Gentleman SM, Roberts GW, Graham DI, Royston MC. Increased numbers of bAPP-immunoreactive neurones in the entorhinal cortex after head injury. Neuroreport 1994; 6: 161-4
    • (1994) Neuroreport , vol.6 , pp. 161-164
    • McKenzie, J.E.1    Gentleman, S.M.2    Roberts, G.W.3    Graham, D.I.4    Royston, M.C.5
  • 112
    • 0028953529 scopus 로고
    • Activalion of microglial cells by β-amyloid protein and interferon-γ
    • 112 Meda L, Cassatella MA, Szendrei GI et al. Activalion of microglial cells by β-amyloid protein and interferon-γ. Nature 1995; 374: 647-50
    • (1995) Nature , vol.374 , pp. 647-650
    • Meda, L.1    Cassatella, Ma.2    Szendrei, G.I.3
  • 113
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • 113 Miller DL, Papayannopoulos IA, Styles J et al. Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch Biochem Biophys 1993; 301: 41-52
    • (1993) Arch Biochem Biophys , vol.301 , pp. 41-52
    • Miller, D.L.1    Papayannopoulos, I.A.2    Styles, J.3
  • 114
    • 0031453010 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway
    • 114 Mills J, Laurent Charest D, Lam F et al. Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway. J Neurosci 1997; 17: 9415-22
    • (1997) J Neurosci , vol.17 , pp. 9415-9422
    • Mills, J.1    Laurent Charest, D.2    Lam, F.3
  • 115
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • 115 Milward EA, Papadopoulos R, Fuller SJ et al. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron 1992; 9: 129-37
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3
  • 116
    • 0029765553 scopus 로고    scopus 로고
    • Apolipoprotein E allele-specific anti-oxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides
    • 116 Miyata M, Smith JD. Apolipoprotein E allele-specific anti-oxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides. Nat Genet 1996; 14: 55-61
    • (1996) Nat Genet , vol.14 , pp. 55-61
    • Miyata, M.1    Smith, J.D.2
  • 117
    • 0028982454 scopus 로고
    • Reduction of β-amyloid peptide 42 in the cerebrospinal fluid of patients with Alzhiemer's disease
    • 117 Motter R, Vigo-Pelfrey C, Kholodenko D et al. Reduction of β-amyloid peptide 42 in the cerebrospinal fluid of patients with Alzhiemer's disease. Ann Neurol 1995; 38: 643-8
    • (1995) Ann Neurol , vol.38 , pp. 643-648
    • Motter, R.1    Vigo-Pelfrey, C.2    Kholodenko, D.3
  • 118
    • 0027970897 scopus 로고
    • Synaptotrophic effects of human amyloid b protein precursors in the cortex of transgenic mice
    • 118 Mucke L, Masliah E, Johnson WB et al. Synaptotrophic effects of human amyloid b protein precursors in the cortex of transgenic mice. Brain Res 1994; 666: 151-67
    • (1994) Brain Res , vol.666 , pp. 151-167
    • Mucke, L.1    Masliah, E.2    Johnson, W.B.3
  • 119
    • 0028968005 scopus 로고
    • Protection against HIV-1 gp120-induced brain damage by neuronal expression of human amyloid precursor protein
    • 119 Mucke L, Abraham CR, Ruppe MD et al. Protection against HIV-1 gp120-induced brain damage by neuronal expression of human amyloid precursor protein. J Exp Med 1995; 181: 155 1-6
    • (1995) J Exp Med , vol.181 , pp. 1551-1556
    • Mucke, L.1    Abraham, C.R.2    Ruppe, M.D.3
  • 120
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of β-amyloid
    • 120 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 β-amyloid. Nature Genet 1992; 1: 345-7
    • (1992) Nature Genet , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 121
    • 0027981759 scopus 로고
    • Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans
    • 121 Multhaup G. Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans. Biochimie 1994; 76: 304-11
    • (1994) Biochimie , vol.76 , pp. 304-311
    • Multhaup, G.1
  • 122
    • 0027984643 scopus 로고
    • Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease beta A4 amyloid precursor protein (APP)
    • 122 Multhaup G, Bush AI, Pollwein P, Masters CL. Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease beta A4 amyloid precursor protein (APP). FEBS Lett 1994; 355: 151-4
    • (1994) FEBS Lett , vol.355 , pp. 151-154
    • Multhaup, G.1    Bush, A.I.2    Pollwein, P.3    Masters, C.L.4
  • 123
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I)
    • 123 Multhaup G, Schlicksupp A, Hesse L et al. The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I). Science 1996; 271: 1406-9
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3
  • 124
    • 0032546577 scopus 로고    scopus 로고
    • Copper-binding amyloid precursor protein undergoes a site-speciifc fragmentation in the reduction of hydrogen peroxide
    • 124 Multhaup G, Ruppert T, Schlicksupp A et al. Copper-binding amyloid precursor protein undergoes a site-speciifc fragmentation in the reduction of hydrogen peroxide. Biochemistry 1998; 37: 7224-30
    • (1998) Biochemistry , vol.37 , pp. 7224-7230
    • Multhaup, G.1    Ruppert, T.2    Schlicksupp, A.3
  • 125
    • 0026500019 scopus 로고
    • Amyloid β-protein precursor deposition in rat hippocampus lesioned by ibotenic acid injection
    • 125 Nakamura Y, Takeda M, Niigawa H, Hariguchi S, Nishimura T. Amyloid β-protein precursor deposition in rat hippocampus lesioned by ibotenic acid injection. Neurosci Letts 1992; 136: 95-8
    • (1992) Neurosci Letts , vol.136 , pp. 95-98
    • Nakamura, Y.1    Takeda, M.2    Niigawa, H.3    Hariguchi, S.4    Nishimura, T.5
  • 126
    • 0025668995 scopus 로고
    • Growth delay in Down syndrome and zinc sulphate supplementation
    • 126 Napolitano G, Palka G, Grimaldi S et al. Growth delay in Down syndrome and zinc sulphate supplementation. Am J Med Genet Suppl 1990; 7: 63-5
    • (1990) Am J Med Genet Suppl , vol.7 , pp. 63-65
    • Napolitano, G.1    Palka, G.2    Grimaldi, S.3
  • 127
    • 0026474527 scopus 로고
    • Characterization of high affinity binding between laminin and Alzheimer's disease amyloid precursor proteins
    • 127 Narindrasorasak S, Lowery DE, Altman RA, Gonzalez DeWhitt PA, Greenberg BD, Kisilevsky R. Characterization of high affinity binding between laminin and Alzheimer's disease amyloid precursor proteins. Lab Invest 1992; 67: 643-52
    • (1992) Lab Invest , vol.67 , pp. 643-652
    • Narindrasorasak, S.1    Lowery, D.E.2    Altman, R.A.3    DeWhitt, P.A.4    Greenberg, B.D.5    Kisilevsky, R.6
  • 128
    • 0028201847 scopus 로고
    • Role of neurotransmission in the regulation of amloid β-protein precursor processing
    • 128 Nitsch RM, Growdon JH. Role of neurotransmission in the regulation of amloid β-protein precursor processing. Biochem Pharmacol 1994; 47: 1275-84
    • (1994) Biochem Pharmacol , vol.47 , pp. 1275-1284
    • Nitsch, R.M.1    Growdon, J.H.2
  • 129
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • 129 Nitsch RM, Slack BE, Wurtman RJ, Growdon JH. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 1992; 258: 304-7
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 130
    • 0029240546 scopus 로고
    • Inhibitory action of amyloid precursor protein against human Hageman factor (factor XII)
    • 130 Niwano H, Embury PB, Greenberg BD, Ratnoff OD. Inhibitory action of amyloid precursor protein against human Hageman factor (factor XII). J Lab Clin Med 1995; 125: 251-6
    • (1995) J Lab Clin Med , vol.125 , pp. 251-256
    • Niwano, H.1    Embury, P.B.2    Greenberg, B.D.3    Ratnoff, O.D.4
  • 131
    • 0024426526 scopus 로고
    • The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II
    • 131 Oltersdorf T, Fritz LC, Schenk DB et al. The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II. Nature 1989; 341: 144-7
    • (1989) Nature , vol.341 , pp. 144-147
    • Oltersdorf, T.1    Fritz, L.C.2    Schenk, D.B.3
  • 132
    • 0029910609 scopus 로고    scopus 로고
    • Amyloid precursor protein truncated at any of the gamma-secretase sites is not cleaved to β-amyloid
    • 132 Paganetti PA, Lis M, Klafki HW, Staufenbiel M. Amyloid precursor protein truncated at any of the gamma-secretase sites is not cleaved to β-amyloid. J Neurosci Res 1996; 46: 283-93
    • (1996) J Neurosci Res , vol.46 , pp. 283-293
    • Paganetti, P.A.1    Lis, M.2    Klafki, H.W.3    Staufenbiel, M.4
  • 133
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • 133 Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res 1991; 563: 311-4
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 134
    • 0028981219 scopus 로고
    • Structure-activity analysis of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • 134 Pike CJ, Walencewics-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG, Cotman CW. Structure-activity analysis of β-amyloid peptides: contributions of the β25-35 region to aggregation and neurotoxicity. J Neurochem 1995; 64: 253-65
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewics-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 135
    • 0026792932 scopus 로고
    • Bacterial expression, purification, and functional mapping of the amyloid beta/A4 protein precursor
    • 135 Roch JM, Shapiro IP, Sundsmo MP et al. Bacterial expression, purification, and functional mapping of the amyloid beta/A4 protein precursor. J Biol Chem 1992; 267: 2214-21
    • (1992) J Biol Chem , vol.267 , pp. 2214-2221
    • Roch, J.M.1    Shapiro, I.P.2    Sundsmo, M.P.3
  • 136
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • 136 Rogaev EI, Sherrington R, Rogaeva EA et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 1995; 376: 775-8
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3
  • 137
    • 0030250567 scopus 로고    scopus 로고
    • Inflammation and Alzheimer's disease pathogenesis
    • 137 Rogers J, Webster S, Lue LF et al. Inflammation and Alzheimer's disease pathogenesis. Neurobiol Aging 1996; 17: 681-6
    • (1996) Neurobiol Aging , vol.17 , pp. 681-686
    • Rogers, J.1    Webster, S.2    Lue, L.F.3
  • 138
    • 0027477463 scopus 로고
    • Structural altertions in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • 138 Roher AE, Lowenson JD, Clarke S et al. Structural altertions in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 1993; 268: 3072-83
    • (1993) J Biol Chem , vol.268 , pp. 3072-3083
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3
  • 139
    • 0012194808 scopus 로고
    • A Drosophila gene encoding a protein resembling the human beta-amyloid protein precursor
    • 139 Rosen DR, Martin-Morris L, Luo LQ, White K. A Drosophila gene encoding a protein resembling the human beta-amyloid protein precursor. Proc Natl Acad Sci USA 1989; 86: 2478-82
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2478-2482
    • Rosen, D.R.1    Martin-Morris, L.2    Luo, L.Q.3    White, K.4
  • 140
    • 0022220868 scopus 로고
    • Protease inhibitors of human plasma. Antithrombin-III. 'The heparin-antithrombin system'
    • 140 Rosenberg RD, Bauer KA, Marcum JA. Protease inhibitors of human plasma. Antithrombin-III. 'The heparin-antithrombin system'. J Med 1985; 16: 351-416
    • (1985) J Med , vol.16 , pp. 351-416
    • Rosenberg, R.D.1    Bauer, K.A.2    Marcum, J.A.3
  • 141
    • 0026442641 scopus 로고
    • Release of amino-terminal fragments from amyloid precursor protein reporter and mutated derivatives in cultured cells
    • 141 Sahasrabudhe SR, Spruyt MA, Muenkel HA, Blume AJ, Vitek MP, Jacobsen JS. Release of amino-terminal fragments from amyloid precursor protein reporter and mutated derivatives in cultured cells. J Biol Chem 1992; 267: 25602-8
    • (1992) J Biol Chem , vol.267 , pp. 25602-25608
    • Sahasrabudhe, S.R.1    Spruyt, M.A.2    Muenkel, H.A.3    Blume, A.J.4    Vitek, M.P.5    Jacobsen, J.S.6
  • 142
    • 0024395366 scopus 로고
    • Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts
    • 142 Saitoh T, Sundsmo M, Roch JM et al. Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts. Cell 1989; 58: 615-22
    • (1989) Cell , vol.58 , pp. 615-622
    • Saitoh, T.1    Sundsmo, M.2    Roch, J.M.3
  • 143
    • 0026665014 scopus 로고
    • Evidence for intracellular cleavage of the Alzheimer's amyloid precursor in PC12 cells
    • 143 Sambamurti K, Shioi J, Anderson JP, Pappolla MA, Robakis NK. Evidence for intracellular cleavage of the Alzheimer's amyloid precursor in PC12 cells. J Neurosci Res 1992; 33: 319-29
    • (1992) J Neurosci Res , vol.33 , pp. 319-329
    • Sambamurti, K.1    Shioi, J.2    Anderson, J.P.3    Pappolla, M.A.4    Robakis, N.K.5
  • 145
    • 0028799897 scopus 로고
    • Coagulation factor XIa cleaves the RDHS sequence and abolishes the cell adhesive properties of the amyloid ïïb-protein
    • 145 Saporito-Irwin SM, Van-Nostrand WE. Coagulation factor XIa cleaves the RDHS sequence and abolishes the cell adhesive properties of the amyloid ïïb-protein. J Biol Chem 1995; 270: 26265-9
    • (1995) J Biol Chem , vol.270 , pp. 26265-26269
    • Saporito-Irwin, S.M.1    Van-Nostrand, W.E.2
  • 146
    • 0029793482 scopus 로고    scopus 로고
    • Can the controversy of the role of aluminium in Alzheimer's disease be resolved? What are the suggested approaches to this controversy and methodological issues to he considered?
    • 146 Savory J, Exley C, Forbes WF et al. Can the controversy of the role of aluminium in Alzheimer's disease be resolved? What are the suggested approaches to this controversy and methodological issues to he considered? J Toxicol Environ Health 1996; 48: 615-35
    • (1996) J Toxicol Environ Health , vol.48 , pp. 615-635
    • Savory, J.1    Exley, C.2    Forbes, W.F.3
  • 147
    • 0031020877 scopus 로고    scopus 로고
    • Progress curve analysis of the kinetics with which blood coaggulation factor XIa is inhibited by protease nexin-2
    • 147 Scandura JM, Zhang Y, Van Nostrand WE, Walsh PN. Progress curve analysis of the kinetics with which blood coaggulation factor XIa is inhibited by protease nexin-2. Biochemistry 1997; 36: 412-20
    • (1997) Biochemistry , vol.36 , pp. 412-420
    • Scandura, J.M.1    Zhang, Y.2    Van Nostrand, W.E.3    Walsh, P.N.4
  • 148
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • 148 Scheuner D, Eckman C, Jensen M et al. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med 1996; 2: 864-70
    • (1996) Nature Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 149
    • 0027517128 scopus 로고
    • Protease nexin-2/amyloid beta protein precursor. A tight-binding inhibitor of coagulation factor IXa
    • 149 Schmaler AH, Dahl LD, Rozemuller AJ et al. Protease nexin-2/amyloid beta protein precursor. A tight-binding inhibitor of coagulation factor IXa. J Clin Invest 1993; 92: 2540-5
    • (1993) J Clin Invest , vol.92 , pp. 2540-2545
    • Schmaler, A.H.1    Dahl, L.D.2    Rozemuller, A.J.3
  • 150
    • 0029972129 scopus 로고    scopus 로고
    • Effect of alkalizing agents on the processing of the β-amyloid precursor protein
    • 150 Schrader-Fischer G, Paganetti PA. Effect of alkalizing agents on the processing of the β-amyloid precursor protein. Brain Res 1996; 716: 91-100
    • (1996) Brain Res , vol.716 , pp. 91-100
    • Schrader-Fischer, G.1    Paganetti, P.A.2
  • 151
    • 0024560146 scopus 로고
    • Characterization of an amyloid beta precursor protein that binds heparin and contains tyrosine sulfate
    • 151 Schubert D, LaCorbiere M, Saitoh T, Cole G. Characterization of an amyloid beta precursor protein that binds heparin and contains tyrosine sulfate. Proc Natl Acad Sci USA 1989; 86: 2066-9
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2066-2069
    • Schubert, D.1    LaCorbiere, M.2    Saitoh, T.3    Cole, G.4
  • 152
    • 0027421474 scopus 로고
    • The expression of amyloid beta protein precursor protects nerve cells from beta-amyloid and glutamate toxicity and alters their interaction with the extracellular matrix
    • 152 Schubert D, Behl C. The expression of amyloid beta protein precursor protects nerve cells from beta-amyloid and glutamate toxicity and alters their interaction with the extracellular matrix. Brain Res 1993; 629: 275-82
    • (1993) Brain Res , vol.629 , pp. 275-282
    • Schubert, D.1    Behl, C.2
  • 153
    • 0028957882 scopus 로고
    • Amyloid peptides are toxic via a common oxidative mechanism
    • 153 Schubert D, Behl C, Lesley R et al. Amyloid peptides are toxic via a common oxidative mechanism. Proc Natl Acad Sci USA 1995; 92: 1989-93
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1989-1993
    • Schubert, D.1    Behl, C.2    Lesley, R.3
  • 154
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • 154 Selkoe DJ. Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu Rev Cell Biol 1994; 10: 373-403
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 155
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
    • 155 Seubert P, Vigo-Pelfrey C, Esch F et al. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 1992; 359: 325-7
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3
  • 156
    • 0027459686 scopus 로고
    • Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide
    • 156 Seubert P, Oltersdorf T, Lee MG et al. Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide. Nature 1993; 361: 260-3
    • (1993) Nature , vol.361 , pp. 260-263
    • Seubert, P.1    Oltersdorf, T.2    Lee, M.G.3
  • 157
    • 8944241774 scopus 로고    scopus 로고
    • Alzheimer's disease associated with mutations in presenilin 2 is rare and variably penetrant
    • 157 Sherrington R, Froelich S, Sorbi S et al. Alzheimer's disease associated with mutations in presenilin 2 is rare and variably penetrant. Hum Mol Genet 1996; 5: 985-8
    • (1996) Hum Mol Genet , vol.5 , pp. 985-988
    • Sherrington, R.1    Froelich, S.2    Sorbi, S.3
  • 158
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • 158 Sherrington R, Rogaev EI, Liang Y et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 1995; 375: 754-60
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 159
    • 0024005801 scopus 로고
    • Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • 159 Shivers BD, Hilbich C, Multhaup G, Salbaum M, Beyreuther K, Seeburg PH. Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact. EMBO J 1988; 7: 1365-70
    • (1988) EMBO J , vol.7 , pp. 1365-1370
    • Shivers, B.D.1    Hilbich, C.2    Multhaup, G.3    Salbaum, M.4    Beyreuther, K.5    Seeburg, P.H.6
  • 160
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid β protein by normal proteolytic processing
    • 160 Shoji M, Golde TE, Ghiso J et al. Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 1992; 258: 126-9
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1    Golde, T.E.2    Ghiso, J.3
  • 161
    • 0025373508 scopus 로고
    • Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing
    • 161 Sisodia SS, Koo EH, Beyreuther K, Unterbeck A, Price DL. Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Seience 1990; 248: 492-5
    • (1990) Seience , vol.248 , pp. 492-495
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.L.5
  • 162
    • 0027056827 scopus 로고
    • Secretion of the beta-amyloid precursor protein
    • 162 Sisodia SS. Secretion of the beta-amyloid precursor protein. Ann NY Acad Sci 1992; 674: 53-7
    • (1992) Ann NY Acad Sci , vol.674 , pp. 53-57
    • Sisodia, S.S.1
  • 163
    • 0028891759 scopus 로고
    • Nucleotide sequence of the chromosome 14-encoded S182 cDNA and revised secondary structure prediction
    • 163 Slunt HH, Thinakaran G, Lee MK, Sisodia SS. Nucleotide sequence of the chromosome 14-encoded S182 cDNA and revised secondary structure prediction. Amyloid: Int. J Exp Clin Invest 1995; 2: 188-90
    • (1995) Amyloid: Int. J Exp Clin Invest , vol.2 , pp. 188-190
    • Slunt, H.H.1    Thinakaran, G.2    Lee, M.K.3    Sisodia, S.S.4
  • 164
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • 164 Small DH, Nurcombe V, Reed G et al. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J Neurosci 1994; 14: 2117-27
    • (1994) J Neurosci , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3
  • 165
    • 0025365401 scopus 로고
    • Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein
    • 165 Smith RP, Higuchi DA, Broze GJ. Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein. Science 1990; 248: 1126-8
    • (1990) Science , vol.248 , pp. 1126-1128
    • Smith, R.P.1    Higuchi, D.A.2    Broze, G.J.3
  • 167
    • 0029047722 scopus 로고
    • Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease
    • 167 Snow AD, Kinsella MG, Parks E et al. Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease. Arch Biochem Biophys 1995; 320: 84-95
    • (1995) Arch Biochem Biophys , vol.320 , pp. 84-95
    • Snow, A.D.1    Kinsella, M.G.2    Parks, E.3
  • 168
    • 0031873102 scopus 로고    scopus 로고
    • β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • 168 Soto C, Sigurdsson EM, Morelli L, Kumar RA, Castaño EM, Frangione B. β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nature Med 1998; 4: 822-6
    • (1998) Nature Med , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castaño, E.M.5    Frangione, B.6
  • 169
    • 0027198831 scopus 로고
    • Molecular cloning of the cDNA for a human amyloid precursor protein homolog: Evidence for a multigene family
    • 169 Sprecher CA, Grant FJ, Grimm G et al. Molecular cloning of the cDNA for a human amyloid precursor protein homolog: evidence for a multigene family. Biochemistry 1993; 32: 4481-6
    • (1993) Biochemistry , vol.32 , pp. 4481-4486
    • Sprecher, C.A.1    Grant, F.J.2    Grimm, G.3
  • 170
    • 0027407565 scopus 로고
    • Apolipoprotein E. High-avidity binding to β-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • 170 Strittmatter WJ, Saunders AM, Schmechel D et al. Apolipoprotein E. high-avidity binding to β-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci USA 1993; 90: 1977-81
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1977-1981
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3
  • 171
    • 0030851944 scopus 로고    scopus 로고
    • Superoxide free radical and intracellular calcium mediate Aβ (1-42) induced endothelial toxicity
    • 171 Suo Z, Fang C, Crawford F, Mullan M. Superoxide free radical and intracellular calcium mediate Aβ (1-42) induced endothelial toxicity. Brain Res 1997; 762: 144-52
    • (1997) Brain Res , vol.762 , pp. 144-152
    • Suo, Z.1    Fang, C.2    Crawford, F.3    Mullan, M.4
  • 172
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP 717) mutants
    • 172 Suzuki N, Cheung TT, Cai X-D et al. An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP 717) mutants. Science 1994; 264: 133-6
    • (1994) Science , vol.264 , pp. 133-136
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.-D.3
  • 173
    • 0029795197 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer disease: An alternative to the amyloid hypothesis
    • 173 Terry RD. The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis. J Neuropathol Exp Neurol 1996; 55: 1023-5
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1023-1025
    • Terry, R.D.1
  • 174
    • 10144263284 scopus 로고    scopus 로고
    • The ïïb-amyloid domain is essential for axonal sorting of amyloid precursor protein
    • 174 Tienari PJ, De Strooper B, Ikonen E et al. The ïïb-amyloid domain is essential for axonal sorting of amyloid precursor protein. EMBO J 1996; 15: 5218-29
    • (1996) EMBO J , vol.15 , pp. 5218-5229
    • Tienari, P.J.1    De Strooper, B.2    Ikonen, E.3
  • 175
    • 0030966774 scopus 로고    scopus 로고
    • Intracellular and secreted Alzheimer beta-amyloid species are generated by distinct mechanisms in cultured hippocampal neurons
    • 175 Tienari PJ, Ida N, Ikonen E et al. Intracellular and secreted Alzheimer beta-amyloid species are generated by distinct mechanisms in cultured hippocampal neurons. Proc Natl Acad Sci USA 1997; 94: 4125-30
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4125-4130
    • Tienari, P.J.1    Ida, N.2    Ikonen, E.3
  • 176
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin 2 mutation (N14H) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid β protein ending at the 42nd (or 43rd) residue
    • 176 Tomita T, Maruyama K, Saido TC et al. The presenilin 2 mutation (N14H) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid β protein ending at the 42nd (or 43rd) residue. Proc Natl Acad Sci USA 1997; 94: 2025-30
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2025-2030
    • Tomita, T.1    Maruyama, K.2    Saido, T.C.3
  • 177
    • 0029664624 scopus 로고    scopus 로고
    • Amyloids β40 and β42 are generated intracellularly in cultured human neurons and their secretion increases with maturation
    • 177 Turner RS, Suzuki N, Chyung ASC, Younkin SG, Lee VM-Y. Amyloids β40 and β42 are generated intracellularly in cultured human neurons and their secretion increases with maturation. J Biol Chem 1996; 271: 8966-70
    • (1996) J Biol Chem , vol.271 , pp. 8966-8970
    • Turner, R.S.1    Suzuki, N.2    Chyung, A.S.C.3    Younkin, S.G.4    Lee, V.M-Y.5
  • 178
    • 0024463491 scopus 로고
    • Protease nexin-II, a potent antichymotrypsin, shows identity to amyloid ïïb-protein precursor
    • 178 Van Nostrand WE, Wagner SL, Suzuki M et al. Protease nexin-II, a potent antichymotrypsin, shows identity to amyloid ïïb-protein precursor. Nature 1989; 341: 546-9
    • (1989) Nature , vol.341 , pp. 546-549
    • Van Nostrand, W.E.1    Wagner, S.L.2    Suzuki, M.3
  • 179
    • 0025371509 scopus 로고
    • Protease nexin-II (amyloid beta-protein precursor): A platelet alpha-granule protein
    • 179 Van Nostrand WE, Schmaier AH, Farrow JS, Cunningham DD. Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein. Science 1990; 248: 745-8
    • (1990) Science , vol.248 , pp. 745-748
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Farrow, J.S.3    Cunningham, D.D.4
  • 180
    • 0028568061 scopus 로고
    • Expression, purification, and characterization of the Kunitz-type proteinase inhibitor domain of the amyloid ïïb-protein precursor-like protein-2
    • 180 Van Nostrand WE, Schmaier AH, Neiditch BR et al. Expression, purification, and characterization of the Kunitz-type proteinase inhibitor domain of the amyloid ïïb-protein precursor-like protein-2. Biochim Biophys Acta 1994; 1209: 165-70
    • (1994) Biochim Biophys Acta , vol.1209 , pp. 165-170
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Neiditch, B.R.3
  • 181
    • 0028940070 scopus 로고
    • Zinc (II) selectively enhances the inhibition of coagulation factor XIa by protease nexin-2/amyloid beta-protein precursor
    • 181 Van Nostrand WE. Zinc (II) selectively enhances the inhibition of coagulation factor XIa by protease nexin-2/amyloid beta-protein precursor. Thromb Res 1995; 78: 43-53
    • (1995) Thromb Res , vol.78 , pp. 43-53
    • Van Nostrand, W.E.1
  • 182
    • 0027055973 scopus 로고
    • A murine sequence-specific DNA binding protein shows extensive local similarities to the amyloid precursor protein
    • 182 Vidal F, Blangy A, Rassoulzadegan M, Cuzin F. A murine sequence-specific DNA binding protein shows extensive local similarities to the amyloid precursor protein. Biochem Biophys Res Commun 1992; 189: 1336-41
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1336-1341
    • Vidal, F.1    Blangy, A.2    Rassoulzadegan, M.3    Cuzin, F.4
  • 183
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • 183 Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I, Schenk DB. Characterization of β-amyloid peptide from human cerebrospinal fluid. J Neurochem 1993; 61: 1965-8
    • (1993) J Neurochem , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 184
    • 0026442891 scopus 로고
    • Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid beta protein precursor
    • 184 Wasco W, Bupp K, Magendantz M, Gusella JF, Tanzi RE, Solomon F. Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid beta protein precursor. Proc Natl Acad Sci USA 1992; 89: 10758-62
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10758-10762
    • Wasco, W.1    Bupp, K.2    Magendantz, M.3    Gusella, J.F.4    Tanzi, R.E.5    Solomon, F.6
  • 185
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • 185 Weidemann A, König G, Bunke D et al. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 1989; 57: 115-26
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    König, G.2    Bunke, D.3
  • 186
    • 0031054505 scopus 로고    scopus 로고
    • Formation of stable complexes between two Alzheimer's disease gene products: Presenilin-2 and β-amyloid precursor protein
    • 186 Weidemann A, Paliga K, Durrwang U et al. Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and β-amyloid precursor protein. Nat Med 1997; 3: 328-32
    • (1997) Nat Med , vol.3 , pp. 328-332
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3
  • 187
    • 0027361386 scopus 로고
    • Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid precursor protein and produce intracellular β-amyloid or A4 peptides
    • 187 Wertkin AM, Turner RS, Pleasure SJ et al. Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid precursor protein and produce intracellular β-amyloid or A4 peptides. Proc Natl Acad Sci USA 1993; 90: 9513-7
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9513-9517
    • Wertkin, A.M.1    Turner, R.S.2    Pleasure, S.J.3
  • 188
    • 0003033067 scopus 로고    scopus 로고
    • The metabolism of the amyloid precursor protein of Alzheimer's disease and dietary zinc
    • Eds. K Iqbal, B Winblad, T Nishimura, M Takeda, HM Wisniewski, Chichester: John Wiley and Sons Ltd
    • 188 Whyte S, Jones L, Coulson EJ et al. The metabolism of the amyloid precursor protein of Alzheimer's disease and dietary zinc. In: Alzheimer'z Disease. Biology, Diagnosis and Therapeutics, Eds. K Iqbal, B Winblad, T Nishimura, M Takeda, HM Wisniewski, Chichester: John Wiley and Sons Ltd, 1997: 417-22
    • (1997) Alzheimer'z Disease. Biology, Diagnosis and Therapeutics , pp. 417-422
    • Whyte, S.1    Jones, L.2    Coulson, E.J.3
  • 189
    • 0032529710 scopus 로고    scopus 로고
    • Survival of cultured neurons from APP. Knockout mice against Alzheimer's amyloid Aβ toxicity and oxidative stress
    • in press
    • 189 White AR, Zheng H, Galatis D et al. Survival of cultured neurons from APP. knockout mice against Alzheimer's amyloid Aβ toxicity and oxidative stress. J Neurosci 1998; 18: in press
    • (1998) J Neurosci , pp. 18
    • White, A.R.1    Zheng, H.2    Galatis, D.3
  • 190
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42
    • 190 Wild-Bode C, Yamazaki T, Capell A et al. Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42. J Biol Chem 1997; 272: 16085-8
    • (1997) J Biol Chem , vol.272 , pp. 16085-16088
    • Wild-Bode, C.1    Yamazaki, T.2    Capell, A.3
  • 191
    • 10544230644 scopus 로고    scopus 로고
    • Secreted glypican binds to the amyloid precursor protein of Alzheimer's disease (APP) and inhibits APP-induced neurite out-growth
    • 191 Williamson TG, Mok SS, Henry A et al Secreted glypican binds to the amyloid precursor protein of Alzheimer's disease (APP) and inhibits APP-induced neurite out-growth. J Biol Chem 1996; 271: 31215-21
    • (1996) J Biol Chem , vol.271 , pp. 31215-31221
    • Williamson, T.G.1    Mok, S.S.2    Henry, A.3
  • 192
    • 0026045862 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation
    • 192 Wisniewski T, Ghiso J. Frangione B. Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation. Biochem Biophys Res Commun 1991; 179: 1247-54
    • (1991) Biochem Biophys Res Commun , vol.179 , pp. 1247-1254
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 193
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease
    • 193 Xia W, Zhang J. Perez R, Koo EH, Selkoe DJ. Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease. Proc Natl Natl Sci USA 1997; 94: 8208-13
    • (1997) Proc Natl Natl Sci USA , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Perez, R.3    Koo, E.H.4    Selkoe, D.J.5
  • 194
    • 0031946864 scopus 로고    scopus 로고
    • Estrogen reduces neuronal generation of Alzheimer β-amyloid peptides
    • 194 Xu H, Gouras GK, Greenfield JP et al. Estrogen reduces neuronal generation of Alzheimer β-amyloid peptides. Nature Med 1998; 4: 447-51
    • (1998) Nature Med , vol.4 , pp. 447-451
    • Xu, H.1    Gouras, G.K.2    Greenfield, J.P.3
  • 195
    • 0030963605 scopus 로고    scopus 로고
    • Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
    • 195 Xu H, Sweeney D, Wang R et al. Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation. Proc Natl Acad Sci USA 1997; 94: 3748-52
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3748-3752
    • Xu, H.1    Sweeney, D.2    Wang, R.3
  • 197
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • 197 Yan SD, Chen X, Fu J et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 1996; 382: 685-91
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 198
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of anyloid β protein: Reversal by tachykinin neuropeptides
    • 198 Yankner BA, Duffy LK, Kirschner DA. Neurotrophic and neurotoxic effects of anyloid β protein: reversal by tachykinin neuropeptides. Science 1990; 250: 279-82
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 199
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • 199 Yankner BA. Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 1996; 16: 921-32
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 200
    • 0025363827 scopus 로고
    • Molecular architecture of basement membranes
    • 200 Yurchenco PD, Schittny JC. Molecular architecture of basement membranes. FASEB J 1990; 4: 1577-90
    • (1990) FASEB J , vol.4 , pp. 1577-1590
    • Yurchenco, P.D.1    Schittny, J.C.2
  • 201
    • 10544248594 scopus 로고    scopus 로고
    • β-secretase processing of the β-amyloid precursor protein in transgenic mice is efficient in neurons but inefficient in astrocytes
    • 201 Zhao J, Paganini L, Mucke L et al. β-secretase processing of the β-amyloid precursor protein in transgenic mice is efficient in neurons but inefficient in astrocytes. J Biol Chem 1996; 271: 31407-11
    • (1996) J Biol Chem , vol.271 , pp. 31407-31411
    • Zhao, J.1    Paganini, L.2    Mucke, L.3
  • 202
    • 0028177688 scopus 로고
    • Secretion of β-amyloid precursor protein involves multiple cleavage sites
    • 202 Zhong Z, Higaki J, Murakami K et al. Secretion of β-amyloid precursor protein involves multiple cleavage sites. J Biol Chem 1994; 269: 627-32
    • (1994) J Biol Chem , vol.269 , pp. 627-632
    • Zhong, Z.1    Higaki, J.2    Murakami, K.3


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