메뉴 건너뛰기




Volumn 5, Issue 4, 1996, Pages 445-451

Characterization of appican, the chondroitin sulfate proteoglycan form of the Alzheimer amyloid precursor protein

Author keywords

Alzheimer's disease; APP; Inflammation; Proteoglycans

Indexed keywords

AMYLOID PRECURSOR PROTEIN; APPICAN; ISOPROTEIN; PROTEOCHONDROITIN SULFATE; UNCLASSIFIED DRUG;

EID: 0030483787     PISSN: 10558330     EISSN: None     Source Type: Journal    
DOI: 10.1006/neur.1996.0061     Document Type: Conference Paper
Times cited : (33)

References (58)
  • 1
    • 0030038809 scopus 로고    scopus 로고
    • Scavenging of Alzheimer's amyloid β-protein by microglia in culture
    • Ard MD, Cole GM, Wei J, Mehrle AP, Fratkin JD (1996) Scavenging of Alzheimer's amyloid β-protein by microglia in culture. J Neurosci Res 43:190-202
    • (1996) J Neurosci Res , vol.43 , pp. 190-202
    • Ard, M.D.1    Cole, G.M.2    Wei, J.3    Mehrle, A.P.4    Fratkin, J.D.5
  • 2
    • 0027526497 scopus 로고
    • Astrocytes: Targets and mediators of chemical induced CNS injury
    • Aschner M, Lopachin JRM (1993) Astrocytes: Targets and mediators of chemical induced CNS injury. J Toxic Envir Health 38:329-342.
    • (1993) J Toxic Envir Health , vol.38 , pp. 329-342
    • Aschner, M.1    Lopachin, J.R.M.2
  • 3
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D (1994) Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77:817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 4
    • 0011832293 scopus 로고
    • Identification and syntheses of a recognition signal for the attachment of GAGs to proteins
    • Bourdon M, Krusius T, Cambell S, Schwartz N, Ruoslahti E (1987) Identification and syntheses of a recognition signal for the attachment of GAGs to proteins. PNAS USA 84:3194-3198
    • (1987) PNAS USA , vol.84 , pp. 3194-3198
    • Bourdon, M.1    Krusius, T.2    Cambell, S.3    Schwartz, N.4    Ruoslahti, E.5
  • 5
    • 0025965521 scopus 로고
    • Amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion
    • Breen KC, Bruce M, Anderton BH (1991) β Amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J Neurosci Res 28:90-100
    • (1991) J Neurosci Res , vol.28 , pp. 90-100
    • Breen, K.C.1    Bruce, M.2    Anderton, B.H.3
  • 6
    • 0026511070 scopus 로고
    • Chondroitin sulfate as a regulator of neuronal patterning in the retina
    • Brittis PA, Canning DR, Silver J (1992) Chondroitin sulfate as a regulator of neuronal patterning in the retina. Nature 255:733-736
    • (1992) Nature , vol.255 , pp. 733-736
    • Brittis, P.A.1    Canning, D.R.2    Silver, J.3
  • 9
    • 0027209456 scopus 로고
    • Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease
    • DeWitt DA, Silver J, Canning DR, Perry G (1993) Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease. Exp Neurol 121:149-152
    • (1993) Exp Neurol , vol.121 , pp. 149-152
    • DeWitt, D.A.1    Silver, J.2    Canning, D.R.3    Perry, G.4
  • 10
    • 0029616545 scopus 로고
    • Receptor mediated adhesive and anti-adhesive functions of chondroitin sulfate proteoglycan preparations from embryonic chicken brain
    • Ernst H, Zanin MKB, Everman D, Hoffman S (1995) Receptor mediated adhesive and anti-adhesive functions of chondroitin sulfate proteoglycan preparations from embryonic chicken brain. J Cell Science 108:3807-3816
    • (1995) J Cell Science , vol.108 , pp. 3807-3816
    • Ernst, H.1    Zanin, M.K.B.2    Everman, D.3    Hoffman, S.4
  • 11
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser PE, Nguyen JT, Chin DT, Kirschner DA (1992) Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. J Neurochem 59:1531-1540
    • (1992) J Neurochem , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 12
    • 0029923520 scopus 로고    scopus 로고
    • Association of Aβ40-positive senile plaques with microglial cells in the brains of patients with Alzheimer's disease and in non-demented aged individuals
    • Fukumoto H, Asami-Odaka A, Suzuki N, Iwatsubo T (1996) Association of Aβ40-positive senile plaques with microglial cells in the brains of patients with Alzheimer's disease and in non-demented aged individuals. Neurodegeneration 5:13-17
    • (1996) Neurodegeneration , vol.5 , pp. 13-17
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Iwatsubo, T.4
  • 14
    • 0029310601 scopus 로고
    • Chondroitin sulfate proteoglycan staining in astrocyte-Schwann cell co-cultures
    • Ghirinkar RS, Eng LF (1995) Chondroitin sulfate proteoglycan staining in astrocyte-Schwann cell co-cultures. Glia 14:145-152
    • (1995) Glia , vol.14 , pp. 145-152
    • Ghirinkar, R.S.1    Eng, L.F.2
  • 16
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G, Wong C (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.1    Wong, C.2
  • 17
    • 0011440558 scopus 로고
    • Potential role of proteoglycans in the accumulation and presistence of Aβ in Alzheimer's disease senile plaques
    • Gupta-Bansal R, Ziehler W, Wujek JR, Brunden KR (1993) Potential role of proteoglycans in the accumulation and presistence of Aβ in Alzheimer's disease senile plaques. Soc Neurosci Abstr 19:1471
    • (1993) Soc Neurosci Abstr , vol.19 , pp. 1471
    • Gupta-Bansal, R.1    Ziehler, W.2    Wujek, J.R.3    Brunden, K.R.4
  • 19
    • 0023791674 scopus 로고
    • Binding of human extracellular superoxide dismutase C to sulfated glycosaminoglycans
    • Karlsson KL, Lindahl U, Marklund SL (1988) Binding of human extracellular superoxide dismutase C to sulfated glycosaminoglycans. Biochem J 256:29-33
    • (1988) Biochem J , vol.256 , pp. 29-33
    • Karlsson, K.L.1    Lindahl, U.2    Marklund, S.L.3
  • 20
    • 0023872043 scopus 로고
    • Novel precursor of Alzheimer's disease amyloid precursor protein shows protease inhibitory activity
    • Kitaguchi N, Takahashi Y, Tokushima Y, Shiojiri S, Ito H (1988) Novel precursor of Alzheimer's disease amyloid precursor protein shows protease inhibitory activity. Nature 331:530-532
    • (1988) Nature , vol.331 , pp. 530-532
    • Kitaguchi, N.1    Takahashi, Y.2    Tokushima, Y.3    Shiojiri, S.4    Ito, H.5
  • 21
    • 0026670809 scopus 로고
    • Identification of a novel alternative splice isoform of the beta A4 amyloid precursor protein (APP) mRNA in leucocytes and microglial cells
    • Konig G, Monning U, Czech C, Prior R, Banati R, Schreiter-Gasser U, Bauer J, Masters CL, Beyreuther K (1992) Identification of a novel alternative splice isoform of the beta A4 amyloid precursor protein (APP) mRNA in leucocytes and microglial cells. J Biol Chem 267:10804-10809
    • (1992) J Biol Chem , vol.267 , pp. 10804-10809
    • Konig, G.1    Monning, U.2    Czech, C.3    Prior, R.4    Banati, R.5    Schreiter-Gasser, U.6    Bauer, J.7    Masters, C.L.8    Beyreuther, K.9
  • 22
    • 0028172886 scopus 로고
    • β Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A, Yankner BA (1994) β Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci USA 91:12243-12247
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 23
    • 0029869667 scopus 로고    scopus 로고
    • Predominant deposition of amyloid-β 42(43) in plaques in cases of Alzheimer's disease and hereditary cerebral hemorrhage associated with mutations in the amyoid precursor protein gene
    • Mann DMA, Iwatsubo T, Ihara Y, Cairns NJ, Lantos PL, Bogdanovic N, Lannfelt L, Winblad B, Maat-Schieman LC, Rossor MN (1996) Predominant deposition of amyloid-β 42(43) in plaques in cases of Alzheimer's disease and hereditary cerebral hemorrhage associated with mutations in the amyoid precursor protein gene. Am J Pathol 148:1257-1266
    • (1996) Am J Pathol , vol.148 , pp. 1257-1266
    • Mann, D.M.A.1    Iwatsubo, T.2    Ihara, Y.3    Cairns, N.J.4    Lantos, P.L.5    Bogdanovic, N.6    Lannfelt, L.7    Winblad, B.8    Maat-Schieman, L.C.9    Rossor, M.N.10
  • 26
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I, Rydel RE (1992) β-Amyloid peptides destabilize calcium homeostasis and render human neurons vulnerable to excitotoxicity. J Neurosci 12:376-389
    • (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
  • 27
    • 0025714819 scopus 로고
    • The response of the cerebral hemisphere of the rat to injury. 1. The mature rat
    • Maxwell WL, Follows R, Ashurst DE, Berry M (1990) The response of the cerebral hemisphere of the rat to injury. 1. The mature rat. Philos Trans R Soc Lond 328:479-513
    • (1990) Philos Trans R Soc Lond , vol.328 , pp. 479-513
    • Maxwell, W.L.1    Follows, R.2    Ashurst, D.E.3    Berry, M.4
  • 28
    • 0028245678 scopus 로고
    • Chondroitin sulfate proteoglycans protect cultured rat's cortical and hippocampal neurons from delayed cell death induced by excitatory amino acids
    • Okamato M, Mori S, Ichimura M, Endo H (1994) Chondroitin sulfate proteoglycans protect cultured rat's cortical and hippocampal neurons from delayed cell death induced by excitatory amino acids. Neurosci Lett 172:51-54
    • (1994) Neurosci Lett , vol.172 , pp. 51-54
    • Okamato, M.1    Mori, S.2    Ichimura, M.3    Endo, H.4
  • 29
    • 0028903888 scopus 로고
    • The chondroitin sulfate attachment site of appican is formed by splicing out exon 15 of the amyloid precursor gene
    • Pangalos MN, Efthimiopoulos S, Shioi J, Robakis J (1995a) The chondroitin sulfate attachment site of appican is formed by splicing out exon 15 of the amyloid precursor gene. J Biol Chem 270:10388-10391
    • (1995) J Biol Chem , vol.270 , pp. 10388-10391
    • Pangalos, M.N.1    Efthimiopoulos, S.2    Shioi, J.3    Robakis, J.4
  • 30
    • 0029081283 scopus 로고
    • Expression of the chondroitin sulfate proteoglycans of amyloid precursor (appican) and amyloid precursor-like protein 2
    • Pangalos MN, Shioi J, Robakis NK (1995b) Expression of the chondroitin sulfate proteoglycans of amyloid precursor (appican) and amyloid precursor-like protein 2. J Neurochem 65:762-769
    • (1995) J Neurochem , vol.65 , pp. 762-769
    • Pangalos, M.N.1    Shioi, J.2    Robakis, N.K.3
  • 31
    • 0029016635 scopus 로고
    • Early association of reactive astrocytes with senile plaques in Alzheimer's disease
    • Pike CJ, Cummings BJ, Cotman CW (1995) Early association of reactive astrocytes with senile plaques in Alzheimer's disease. Exp Neurol 132:172-179
    • (1995) Exp Neurol , vol.132 , pp. 172-179
    • Pike, C.J.1    Cummings, B.J.2    Cotman, C.W.3
  • 32
    • 0028870182 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β amyloid in rat PC12 cells
    • Pollack SJ, Sadler IIJ, Hawtin SR, Tailor VJ, Shearman MS (1995) Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β amyloid in rat PC12 cells. Neurosci Lett 184:113-116
    • (1995) Neurosci Lett , vol.184 , pp. 113-116
    • Pollack, S.J.1    Sadler, I.I.J.2    Hawtin, S.R.3    Tailor, V.J.4    Shearman, M.S.5
  • 33
    • 0015340401 scopus 로고
    • Mode of cell migration to the superficial layers of fetal monkey neocortex
    • Rakic P (1972) Mode of cell migration to the superficial layers of fetal monkey neocortex. J Comp Neurol 145:61-84
    • (1972) J Comp Neurol , vol.145 , pp. 61-84
    • Rakic, P.1
  • 34
    • 0026781306 scopus 로고
    • The role of amyloid β-protein in Alzheimer's disease
    • Regland B, Gottfries C (1992) The role of amyloid β-protein in Alzheimer's disease. Lancet 340:467-469
    • (1992) Lancet , vol.340 , pp. 467-469
    • Regland, B.1    Gottfries, C.2
  • 35
    • 2142777413 scopus 로고
    • Molecular cloning and characterisation of a cDNA encoding the cerebral vascular and the neuritic plaque core amyloid peptides
    • Robakis NK, Ramakrishna N, Wolfe G, Wisniewski HM (1987) Molecular cloning and characterisation of a cDNA encoding the cerebral vascular and the neuritic plaque core amyloid peptides. PNAS USA 84:4190-4194
    • (1987) PNAS USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 36
    • 0028148332 scopus 로고
    • Involvement of amyloid as a central step in the development of Alzheimer's disease
    • Robakis NK, Pangalos MN (1994) Involvement of amyloid as a central step in the development of Alzheimer's disease. Neurobiol Aging 15:S127-S129
    • (1994) Neurobiol Aging , vol.15
    • Robakis, N.K.1    Pangalos, M.N.2
  • 37
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoslahti E, Yamaguchi Y (1991) Proteoglycans as modulators of growth factor activities. Cell 64:867-869
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoslahti, E.1    Yamaguchi, Y.2
  • 38
    • 0024810385 scopus 로고
    • The regulation of amyloid β protein precursor and its modulatory role in cell adhesion
    • Schubert D, LaCorbiere M, Saitoh T, Cole G (1989) The regulation of amyloid β protein precursor and its modulatory role in cell adhesion. Neuron 3:689-694
    • (1989) Neuron , vol.3 , pp. 689-694
    • Schubert, D.1    LaCorbiere, M.2    Saitoh, T.3    Cole, G.4
  • 39
    • 0024313844 scopus 로고
    • Molecular pathology of amyloidogenic proteins and the role of vascular amyloidosis in Alzheimer's disease
    • Selkoe DJ (1989) Molecular pathology of amyloidogenic proteins and the role of vascular amyloidosis in Alzheimer's disease. Neurobiol Aging 10:387-395
    • (1989) Neurobiol Aging , vol.10 , pp. 387-395
    • Selkoe, D.J.1
  • 40
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
    • Seubert P, Vigo-Pelfrey C, Esch F, Lee M, Dovey H (1992) Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359:325-327
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3    Lee, M.4    Dovey, H.5
  • 42
    • 0026691805 scopus 로고
    • Chondroitin sulfate proteoglycan form of the Alzheimer's beta-amyloid precursor
    • Shioi J, Anderson JP, Ripellino JA, Robakis NK (1992) Chondroitin sulfate proteoglycan form of the Alzheimer's beta-amyloid precursor. J Biol Chem 267:13819-13822
    • (1992) J Biol Chem , vol.267 , pp. 13819-13822
    • Shioi, J.1    Anderson, J.P.2    Ripellino, J.A.3    Robakis, N.K.4
  • 43
    • 0027319004 scopus 로고
    • Chondroitin sulfate proteoglycan form of cellular and cell-surface Alzheimer amyloid precursor
    • Shioi J, Refolo LM, Efthimiopoulos S, Robakis NK (1993) Chondroitin sulfate proteoglycan form of cellular and cell-surface Alzheimer amyloid precursor. Neurosci Lett 154:121-124
    • (1993) Neurosci Lett , vol.154 , pp. 121-124
    • Shioi, J.1    Refolo, L.M.2    Efthimiopoulos, S.3    Robakis, N.K.4
  • 44
    • 0029058742 scopus 로고
    • The Alzheimer amyloid precursor proteoglycan (Appican) is present in brain and is produced by astrocytes but not neurons in primary cultures
    • Shioi J, Pangalos MN, Ripellino JA, Vassilacopoulou D, Mytilineou C, Margolis RU, Robakis NK (1995) The Alzheimer amyloid precursor proteoglycan (Appican) is present in brain and is produced by astrocytes but not neurons in primary cultures. J Biol Chem 270:11839-11844
    • (1995) J Biol Chem , vol.270 , pp. 11839-11844
    • Shioi, J.1    Pangalos, M.N.2    Ripellino, J.A.3    Vassilacopoulou, D.4    Mytilineou, C.5    Margolis, R.U.6    Robakis, N.K.7
  • 45
    • 0022004144 scopus 로고
    • Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study
    • Snow AD, Kisilevsky R (1985) Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study. Lab Invest 53:37-44
    • (1985) Lab Invest , vol.53 , pp. 37-44
    • Snow, A.D.1    Kisilevsky, R.2
  • 46
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain
    • Snow AD, Sekiguchi R, Nochlin D, Fraser P, Kimata K, Mizutani A, Arai M, Schreier WA, Morgan DG (1994a) An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain. Neuron 12:219-234
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 47
    • 0028362886 scopus 로고
    • Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not of cerebellum in Alzheimer's disease brain
    • Snow AD, Sekiguchi RT, Nochlin D, Kalaria RN, Kimata K (1994b) Heparan sulfate proteoglycan in diffuse plaques of hippocampus but not of cerebellum in Alzheimer's disease brain. Am J Pathol 144:337-347
    • (1994) Am J Pathol , vol.144 , pp. 337-347
    • Snow, A.D.1    Sekiguchi, R.T.2    Nochlin, D.3    Kalaria, R.N.4    Kimata, K.5
  • 48
    • 0029881267 scopus 로고    scopus 로고
    • Identification and immunolocalization of a new class of proteoglycan (keratan sulfate) to the neuritic plaques of Alzheimer's disease
    • Snow AD, Nochlin D, Skiguchi R, Carlson SS (1996) Identification and immunolocalization of a new class of proteoglycan (keratan sulfate) to the neuritic plaques of Alzheimer's disease. Exp Neurol 138:305-317
    • (1996) Exp Neurol , vol.138 , pp. 305-317
    • Snow, A.D.1    Nochlin, D.2    Skiguchi, R.3    Carlson, S.S.4
  • 49
    • 0025323095 scopus 로고
    • Sulfated proteoglycans in astroglial barriers inhibit neurite outgrowth in vitro
    • Snow DM, Lemmon V, Carrino D, Caplan A, Silver J (1990) Sulfated proteoglycans in astroglial barriers inhibit neurite outgrowth in vitro. Exp Neurol 109:111-130
    • (1990) Exp Neurol , vol.109 , pp. 111-130
    • Snow, D.M.1    Lemmon, V.2    Carrino, D.3    Caplan, A.4    Silver, J.5
  • 51
    • 0026468915 scopus 로고
    • Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease
    • Su JH, Cummings BJ, Cotman CW (1992) Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease. Neuroscience 51:801-813
    • (1992) Neuroscience , vol.51 , pp. 801-813
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 52
    • 0027931658 scopus 로고
    • Amyloid precursor-like protein 2 (APLP2) is modified by the addition of chondroitin sulfate glycosaminoglycan at a single site
    • Thinakaran G, Sisodia SS (1994) Amyloid precursor-like protein 2 (APLP2) is modified by the addition of chondroitin sulfate glycosaminoglycan at a single site. J Biol Chem 269:22099-22104
    • (1994) J Biol Chem , vol.269 , pp. 22099-22104
    • Thinakaran, G.1    Sisodia, S.S.2
  • 53
    • 0002521732 scopus 로고
    • Molecular genetics of amyloid and apolipoprotein E in Alzheimer's disease
    • Dawbarn D, Allen SJ (eds), Oxford
    • Wasco W, Tanzi RE (1995) Molecular genetics of amyloid and apolipoprotein E in Alzheimer's disease. In Dawbarn D, Allen SJ (eds), Neurobiology of Alzheimer's Disease, Bios Scientific, Oxford, pp. 51-76
    • (1995) Neurobiology of Alzheimer's Disease, Bios Scientific , pp. 51-76
    • Wasco, W.1    Tanzi, R.E.2
  • 54
    • 0028792576 scopus 로고
    • Heparan sulfate and chondroitin sulfate glycosaminoglycans attenuate β amyloid (25-35) induced neurodegeneration in cultured hippocampal neurons
    • Woods AG, Cribbs DH, Whittemore ER, Cotman CW (1995) Heparan sulfate and chondroitin sulfate glycosaminoglycans attenuate β amyloid (25-35) induced neurodegeneration in cultured hippocampal neurons. Brain Res 697:53-62
    • (1995) Brain Res , vol.697 , pp. 53-62
    • Woods, A.G.1    Cribbs, D.H.2    Whittemore, E.R.3    Cotman, C.W.4
  • 55
    • 0029670992 scopus 로고    scopus 로고
    • Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro
    • Wujek JR, Dority MD, Frederickson RCA, Brunden KR (1996) Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro. Neurobiol Aging 17:107-113
    • (1996) Neurobiol Aging , vol.17 , pp. 107-113
    • Wujek, J.R.1    Dority, M.D.2    Frederickson, R.C.A.3    Brunden, K.R.4
  • 56
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA (1990) Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides. Science 250:279-281
    • (1990) Science , vol.250 , pp. 279-281
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 57
    • 0011442440 scopus 로고
    • Proteoglycan synthesis in Alzheimer's disease fibroblasts
    • Zebrower M, Beeber C, Kieras FJ (1993) Proteoglycan synthesis in Alzheimer's disease fibroblasts. Soc Neurosci Abstr 19:164
    • (1993) Soc Neurosci Abstr , vol.19 , pp. 164
    • Zebrower, M.1    Beeber, C.2    Kieras, F.J.3
  • 58
    • 0028787769 scopus 로고
    • Distribution of beta amyloid associated proteins in plaques in Alzheimer's disease and in the non-demented elderly
    • Zhan S, Veerhuis R, Kamphorst W, Eikelenboom P (1995) Distribution of beta amyloid associated proteins in plaques in Alzheimer's disease and in the non-demented elderly. Neurodegeneration 4:291-297
    • (1995) Neurodegeneration , vol.4 , pp. 291-297
    • Zhan, S.1    Veerhuis, R.2    Kamphorst, W.3    Eikelenboom, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.