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Volumn 9, Issue 6, 1996, Pages 492-500

Neurotoxicity of β-amyloid and prion peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; EXCITATORY AMINO ACID; PRION PROTEIN;

EID: 0030469956     PISSN: 13507540     EISSN: None     Source Type: Journal    
DOI: 10.1097/00019052-199612000-00017     Document Type: Review
Times cited : (43)

References (110)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D: The molecular pathology of Alzheimer's disease. Neuron 1991, 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.1
  • 4
    • 0028981717 scopus 로고
    • The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • Laferla FM, Tinkle BT, Bierberich CJ, Haudenschild CC, Jay G: The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nature Genet 1995, 9:21-30.
    • (1995) Nature Genet , vol.9 , pp. 21-30
    • Laferla, F.M.1    Tinkle, B.T.2    Bierberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 5
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley M, Prusiner SB: Identification of a protein that purifies with the scrapie prion. Science 1982, 218:1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.2    Prusiner, S.B.3
  • 6
    • 0027001034 scopus 로고
    • Chemistry and biology of prions
    • Prusiner SB. Chemistry and biology of prions. Biochemistry 1992, 31:12277-12288.
    • (1992) Biochemistry , vol.31 , pp. 12277-12288
    • Prusiner, S.B.1
  • 7
    • 0000383864 scopus 로고
    • Ageing and dementias
    • Edited by Hume-Adams J, Duchenne LV. London: Edward Arnold
    • Tomlinson BE. Ageing and dementias. In Greenfield's neuropathology. Edited by Hume-Adams J, Duchenne LV. London: Edward Arnold; 1992:1283-1410.
    • (1992) Greenfield's Neuropathology , pp. 1283-1410
    • Tomlinson, B.E.1
  • 8
    • 0027715580 scopus 로고
    • Neuropathology of human prion diseases (spongiform encephalopathies)
    • Kretzschmar HA: Neuropathology of human prion diseases (spongiform encephalopathies). Dev Biol Stand 1993, 80:71-90.
    • (1993) Dev Biol Stand , vol.80 , pp. 71-90
    • Kretzschmar, H.A.1
  • 9
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB: Novel proteinaceous infectious particles cause scrapie. Science 1982, 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 10
    • 0028922696 scopus 로고
    • Etiology and pathogenesis of prion diseases
    • De Armond SJ, Prusiner SB: Etiology and pathogenesis of prion diseases. Am J Pathol 1995, 146:785-811. An up-to-date review that analysed the neuropathological mechanisms associated with prion disease infection, based essentially on the vast experience of the authors using transgenic mice.
    • (1995) Am J Pathol , vol.146 , pp. 785-811
    • De Armond, S.J.1    Prusiner, S.B.2
  • 11
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy J, Higgins GA: Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.1    Higgins, G.A.2
  • 12
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli F, Castano E, Glenner GG, Frangione B: Differences between vascular and plaque core amyloid in Alzheimer's disease. J Neurochem 1988, 51:648-651.
    • (1988) J Neurochem , vol.51 , pp. 648-651
    • Prelli, F.1    Castano, E.2    Glenner, G.G.3    Frangione, B.4
  • 13
    • 0026794746 scopus 로고
    • Massspectrometry of purified amyloid β protein in Alzheimer's disease
    • Mori H, Takio K, Ogawara M, Selkoe D: Massspectrometry of purified amyloid β protein in Alzheimer's disease. J Biol Chem 1992, 267:17082-17086.
    • (1992) J Biol Chem , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3    Selkoe, D.4
  • 14
    • 0027332081 scopus 로고
    • Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher AE, Lowenson JD, Clarke S, Woods AS, Cotter RJ, Gowing E, Ball MJ: Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc Natl Acad Sci U S A 1993, 90:10836-10840.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 15
    • 0028981466 scopus 로고
    • Molecular pathogenesis of β-amyloidosis in Alzheimer's disease and other cerebral amyloidoses
    • Maury CPJ: Molecular pathogenesis of β-amyloidosis in Alzheimer's disease and other cerebral amyloidoses. Lab Invest 1995, 72:4-16.
    • (1995) Lab Invest , vol.72 , pp. 4-16
    • Maury, C.P.J.1
  • 16
    • 0025770134 scopus 로고
    • The distribution of tangles plaques and related immunohistochemical markers in healthy aging and Alzheimer's disease
    • Price JL, Davis PB, Morris JC, White DL: The distribution of tangles plaques and related immunohistochemical markers in healthy aging and Alzheimer's disease. Neurobiol Aging 1991, 12:295-312.
    • (1991) Neurobiol Aging , vol.12 , pp. 295-312
    • Price, J.L.1    Davis, P.B.2    Morris, J.C.3    White, D.L.4
  • 17
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong W: Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984, 120:885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, W.2
  • 18
  • 20
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phophatydilinosytol glycolipid
    • Stahl N, Boerchelt DR, Hsiao K, Prusiner SB: Scrapie prion protein contains a phophatydilinosytol glycolipid. Cell 1987, 51:229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Boerchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 21
    • 0025193792 scopus 로고
    • Normal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells
    • Caughey B, Neary K, Buller R, Ernst D, Derry LL, Chesebro B, Race RE: Normal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells. J Virol 1990, 64:1093-1101.
    • (1990) J Virol , vol.64 , pp. 1093-1101
    • Caughey, B.1    Neary, K.2    Buller, R.3    Ernst, D.4    Derry, L.L.5    Chesebro, B.6    Race, R.E.7
  • 22
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey B, Raymond J: The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J Biol Chem 1991, 266:18217-18223.
    • (1991) J Biol Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, J.2
  • 23
    • 0026683652 scopus 로고
    • A soluble form of prion protein in human cerebrospinal fluid: Implications for prion-related encephalopathies
    • Tagliavini F, Prelli F, Porro M, Salmona M, Bugiani O, Frangione B: A soluble form of prion protein in human cerebrospinal fluid: implications for prion-related encephalopathies. Biochem Biophys Res Commun 1992, 184:1398-1404.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1398-1404
    • Tagliavini, F.1    Prelli, F.2    Porro, M.3    Salmona, M.4    Bugiani, O.5    Frangione, B.6
  • 24
    • 0022878817 scopus 로고
    • In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein
    • Castano E, Ghiso J, Prelli FP, Gorevic PD, Migheli A, Frangione B: In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein. Biochem Biophys Res Commun 1986, 141:782-789.
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 782-789
    • Castano, E.1    Ghiso, J.2    Prelli, F.P.3    Gorevic, P.D.4    Migheli, A.5    Frangione, B.6
  • 25
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid β A4 peptides of Alzheimer's disease
    • Hilbich C, Kisters-Voike B, Reed J, Masters C, Beyreuther K: Aggregation and secondary structure of synthetic amyloid β A4 peptides of Alzheimer's disease. J Mol Biol 1991, 218:149-163.
    • (1991) J Mol Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Voike, B.2    Reed, J.3    Masters, C.4    Beyreuther, K.5
  • 27
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4
    • Wood SJ, Wetzel R, Martin JD, Hurle MR: Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry 1995. 34:724-730.
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 28
    • 0026045862 scopus 로고
    • Peptide homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation
    • Wisniewski T, Ghiso J, Frangione B: Peptide 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, 179:1247-1254.
    • (1991) Biochem Biophys Res Commun , vol.179 , pp. 1247-1254
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 29
    • 0028981466 scopus 로고
    • Molecular pathogenesis of β-amyloidosis in Alzheimer's disease and other cerebral amyloidoses
    • Maury CPJ: Molecular pathogenesis of β-amyloidosis in Alzheimer's disease and other cerebral amyloidoses. Lab Invest 1995, 72:4-16.
    • (1995) Lab Invest , vol.72 , pp. 4-16
    • Maury, C.P.J.1
  • 30
    • 0027258525 scopus 로고
    • The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation. Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger Ep, Lansbury PT: The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation. Implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, Ep.2    Lansbury, P.T.3
  • 31
    • 0027518937 scopus 로고
    • Alzheimer's disease-like dystrophic neurites characteristically associated with senile plaques are not found within other neurodegenerative diseases unless amyloid-β-protein is present
    • Benzing WC, Mufson EJ, Armstrong DM: Alzheimer's disease-like dystrophic neurites characteristically associated with senile plaques are not found within other neurodegenerative diseases unless amyloid-β-protein is present. Brain Res 1993, 606:10-18.
    • (1993) Brain Res , vol.606 , pp. 10-18
    • Benzing, W.C.1    Mufson, E.J.2    Armstrong, D.M.3
  • 32
    • 0027195933 scopus 로고
    • Seeding 'one dimensional crystallization' of amyloid: Pathogenic mechanism in Alzheimer disease and scrapie?
    • Jarrett JT, Lansbury PT: Seeding 'one dimensional crystallization' of amyloid: pathogenic mechanism in Alzheimer disease and scrapie? Cell 1993, 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 34
    • 0027432458 scopus 로고
    • Perlecan: The multidomain heparan sulphate proteoglycan of basement membrane and extracellular matrix
    • Murdoch AD, lozzo RV: Perlecan: the multidomain heparan sulphate proteoglycan of basement membrane and extracellular matrix [Editorial]. Virchows Arch A Pathol Anat Histopathol 1993, 423:237-242.
    • (1993) Virchows Arch A Pathol Anat Histopathol , vol.423 , pp. 237-242
    • Murdoch, A.D.1    Lozzo, R.V.2
  • 35
    • 0029905421 scopus 로고    scopus 로고
    • Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide Aβ
    • Chan W, Fornwald J, Brawner M, Wetzel R: Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide Aβ. Biochemistry 1996, 35:7123-7130. The interaction between apolipoprotein E and Aβ peptides was explored under native conditions. The data suggested two classes of apolipoprotein E-Aβ complex but no major differences were observed in the behavior of the three apolipoprotein E isotypes.
    • (1996) Biochemistry , vol.35 , pp. 7123-7130
    • Chan, W.1    Fornwald, J.2    Brawner, M.3    Wetzel, R.4
  • 36
    • 0028135459 scopus 로고
    • Enhanced aggregation and β structure of amyloid β peptide after coincubation with C1Q
    • Webster S, O'Barr S, Rogers J: Enhanced aggregation and β structure of amyloid β peptide after coincubation with C1Q. J Neurosci Res 1994, 39:448-456.
    • (1994) J Neurosci Res , vol.39 , pp. 448-456
    • Webster, S.1    O'Barr, S.2    Rogers, J.3
  • 37
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • Wisniewski T, Castano EM, Golabek A, Vogel T, Frangione B: Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am J Pathol 1994, 145:1030-1035.
    • (1994) Am J Pathol , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castano, E.M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 38
    • 0028173205 scopus 로고
    • Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • Ma J, Yee A, Brewer HB Jr, Das S, Potter H: Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature 1994, 372:92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer Jr., H.B.3    Das, S.4    Potter, H.5
  • 41
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of β-amyloid protein: Reversal by tachykinin neuropeptides
    • Yankner BS, Duffy LK, Kirshner DA: Neurotrophic and neurotoxic effects of β-amyloid protein: reversal by tachykinin neuropeptides. Science 1990, 250:279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.S.1    Duffy, L.K.2    Kirshner, D.A.3
  • 42
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio J, Lorenzo A, Yankner BA: Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol Aging 1992, 13:609-612.
    • (1992) Neurobiol Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 43
    • 0027191973 scopus 로고
    • Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35
    • Forloni G, Chiesa R, Smiroldo S, Salmona M, Tagliavini F, Angeretti N: Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35. NeuroReport 1993, 4:523-526.
    • (1993) NeuroReport , vol.4 , pp. 523-526
    • Forloni, G.1    Chiesa, R.2    Smiroldo, S.3    Salmona, M.4    Tagliavini, F.5    Angeretti, N.6
  • 44
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW: Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures. Eur J Pharmacol 1991, 207:367-368.
    • (1991) Eur J Pharmacol , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 45
    • 0028033386 scopus 로고
    • Human cortical neuronal (HCN) cell lines: A model for amyloid neurotoxicity
    • Zhang Z, Drzewiecki GJ, Horn JT, May PC, Hyslop PA: Human cortical neuronal (HCN) cell lines: a model for amyloid neurotoxicity. Neurosci Lett 1994, 177:162-164.
    • (1994) Neurosci Lett , vol.177 , pp. 162-164
    • Zhang, Z.1    Drzewiecki, G.J.2    Horn, J.T.3    May, P.C.4    Hyslop, P.A.5
  • 47
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG, Cotman CW: Structure-activity analyses of β-amyloid peptides: contributions of the β25-35 region to aggregation and neurotoxicity. J Neurochem 1995, 64:253-265. The relationship between the fibrillogenic and neurotoxicity activities of amyloid-β peptides was carefully investigated. The idrophobic sequence β33-35 is essential for both the self-aggregation and neurotoxic mechanisms and numerous substitutions of amino acids did not dissociate the neurotoxic from the amyloidogenic activity.
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 48
    • 0028181758 scopus 로고
    • Reversible random coil-beta-sheet transition of the Alzheimer beta-amyloid fragment (25-35)
    • Terzi E, Holzemann G, Seelig J: Reversible random coil-beta-sheet transition of the Alzheimer beta-amyloid fragment (25-35). Biochemistry 1994, 33:1345-1350.
    • (1994) Biochemistry , vol.33 , pp. 1345-1350
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 49
    • 0028179865 scopus 로고
    • Alzheimer β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • Terzi E, Hblzemann G, Seelig J: Alzheimer β-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes. Biochemistry 1994, 33:7434-7441.
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Hblzemann, G.2    Seelig, J.3
  • 51
    • 0028983336 scopus 로고
    • Amyloid β-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells
    • David-Salinas J, Saponto-Irwin SM, Cotman CW, Van Nostrand WE: Amyloid β-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells. J Neurochem 1995, 65:931-934.
    • (1995) J Neurochem , vol.65 , pp. 931-934
    • David-Salinas, J.1    Saponto-Irwin, S.M.2    Cotman, C.W.3    Van Nostrand, W.E.4
  • 52
    • 0028982272 scopus 로고
    • Amyloid β protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells
    • David-Salinas J, Van Nostrand WE: Amyloid β protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells. J Biol Chem 1995, 270:20887-20890. Soluble Aβ1-42 peptide induced degeneration of cultured cerebrovascular smooth muscle cells. In this study, the authors showed that preaggregation of Aβ1-42 abolishes the ability of the peptide to induce these cellular pathologic responses. These findings suggested that soluble unaggregated Aβ1-42 may interact with a receptor to initiate the pathologic response.
    • (1995) J Biol Chem , vol.270 , pp. 20887-20890
    • David-Salinas, J.1    Van Nostrand, W.E.2
  • 54
    • 0029969354 scopus 로고    scopus 로고
    • Glutamine synthetase-induced enhancement of β-amyloid peptide Aβ (1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation
    • Aksenov MY, Aksenova MV, Butterfield DA, Hensley K, Vigo-Pelfrey C, Carney JM: Glutamine synthetase-induced enhancement of β-amyloid peptide Aβ (1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation. J Neurochem 1996, 66:2050-2056. In contrast with the initial hypothesis proposed, glutamine synthetase enhanced the toxicity of β1-40 and this effect was accompanied by abrogation of fibril formation and partial fragmentation of β1-40. Although the molecular basis for the increase in β1-40 toxicity by glutamine synthetase remains unknown, the data indicate a neurotoxic effect of P1-40 independent of the aggregate state of the peptide.
    • (1996) J Neurochem , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 55
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease
    • Kisilevsky R, Lemieux LJ, Fraser PE, Kong X, Hultin PG, Szarek WA: Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nature Med 1995, 1:143-148.
    • (1995) Nature Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1    Lemieux, L.J.2    Fraser, P.E.3    Kong, X.4    Hultin, P.G.5    Szarek, W.A.6
  • 57
    • 0028176698 scopus 로고
    • β-Cyclodextrin interacts with Alzheimer amyloid β-A4 peptide
    • Camilleri P, Haskins NJ, Hewlett DR: β-Cyclodextrin interacts with Alzheimer amyloid β-A4 peptide. FEBS Lett 1994, 341:256-258.
    • (1994) FEBS Lett , vol.341 , pp. 256-258
    • Camilleri, P.1    Haskins, N.J.2    Hewlett, D.R.3
  • 58
    • 0028870182 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β amyloid in rat PC 12 cells
    • Pollack SJ, Sadler IIJ, Hawtin SR, Tailor VJ, Shearman MS: Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β amyloid in rat PC 12 cells. Neurosci Lett 1995, 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
  • 59
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin
    • Tomiyama T, Shoji A, Kataoka K, Suwa Y, Asano S, Kaneko H, Endo N: Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin. J Biol Chem 1996. 271:6839-6844. The neuroprotective mechanism of rifampicin was investigated, and its possible function as a hydroxyl radical scavenger appeared relevant to the protection of neuronal cells from AβP injury rather than its anti-amyloidogenic activity.
    • (1996) J Biol Chem , vol.271 , pp. 6839-6844
    • Tomiyama, T.1    Shoji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7
  • 60
    • 0029549796 scopus 로고    scopus 로고
    • Sulphated compounds attenuate β-amyloid toxicity by inhibiting its association with cells
    • Sadler II, Smith DW, Shearman MS, Ragan CI, Tailor VJ, Pollack SJ; Sulphated compounds attenuate β-amyloid toxicity by inhibiting its association with cells. NeuroReport 1996, 7:49-53. This group reported that the protective effect of sulphated compounds is caused by interference of β-amyloid cell association rather than effects on β-amyloid structure.
    • (1996) NeuroReport , vol.7 , pp. 49-53
    • Sadler, I.I.1    Smith, D.W.2    Shearman, M.S.3    Ragan, C.I.4    Tailor, V.J.5    Pollack, S.J.6
  • 61
    • 0028172886 scopus 로고
    • β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A, Yankner BA: β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci U S A 1994, 91:12243-12247.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 62
    • 0028914019 scopus 로고
    • Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: Inhibition of amyloidogenesis
    • Merlini G, Ascan E, Amboldi N, Bellotti V, Arbustini E, Perfetti V, Ferrari M, Zorzoli I, Mannone G, Diegoli M, et al.: Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis. Proc Natl Acad Sci U S A 1995, 92:2959-2963. 4′-iodo-4′-deoxydoxorubicin, an anti-tumoral drug, inhibited insulin amyloid fibrillogenesis in vitro and specifically bound to different amyloid fibrils, including Aβ extracted from patients with Alzheimer's disease. 4′-iodo-4′-deoxydoxorubicin also reduced the amyloid deposited in the spleen after in-vivo induction of inflammation-associated amyloid.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2959-2963
    • Merlini, G.1    Ascan, E.2    Amboldi, N.3    Bellotti, V.4    Arbustini, E.5    Perfetti, V.6    Ferrari, M.7    Zorzoli, I.8    Mannone, G.9    Diegoli, M.10
  • 63
    • 0029094670 scopus 로고
    • New drug therapy of amyloidoses: Resorption of AL-type deposits with 4′-iodo-4′-deoxydoxorubicin
    • Gianni L, Bellotti V, Gianni AM, Merlini G: New drug therapy of amyloidoses: resorption of AL-type deposits with 4′-iodo-4′-deoxydoxorubicin. Blood 1995, 86:855-861. Clinical evidence was presented of amyloid resorption in patients with immunoglobulin light-chain amyloidosis. The serendipitous observation of 4′-iodo-4′-deoxydoxorubicin effects in a patient prompted this study. 4′-iodo-4′-deoxydoxorubicin produced clinical benefits in five out of eight patients.
    • (1995) Blood , vol.86 , pp. 855-861
    • Gianni, L.1    Bellotti, V.2    Gianni, A.M.3    Merlini, G.4
  • 64
    • 0029001091 scopus 로고
    • Neuronal membrane conductance activated by amyloid β peptide: Importance of peptide conformation
    • Ying Li W, Czilli DL, Simmons LK: Neuronal membrane conductance activated by amyloid β peptide: importance of peptide conformation. Brain Res 1995, 682:207-211.
    • (1995) Brain Res , vol.682 , pp. 207-211
    • Ying Li, W.1    Czilli, D.L.2    Simmons, L.K.3
  • 65
    • 0029057814 scopus 로고
    • Intracellular Aβ 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang AJ, Knauer M, Burdick DA, Glabe C: Intracellular Aβ 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. J Biol Chem 1995, 270:14786-14792.
    • (1995) J Biol Chem , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 66
    • 0028828044 scopus 로고
    • Clusterin (Apo J) alters the aggregation of amyloid β-peptide (Aβ 1-42) and forms slowly sedimenting Aβ complexes that cause oxidative stress
    • Oda T, Wals P, Osterburg HH, Pasinetti GM, Morgan TE, Rozovsky I, Blainestine W, Snyder SW, Holzman F, Krafft GA, Finch CB: Clusterin (Apo J) alters the aggregation of amyloid β-peptide (Aβ 1-42) and forms slowly sedimenting Aβ complexes that cause oxidative stress. Exp Neurol 1995, 136:2-31. Aβ1-42 incubated with apolipoprotein J partially blocked the aggregation of the peptide and led to the formation of slowly sedimenting complexes that caused oxidative stress in PC12 cells. Despite the decreased amount of fibrils, Aβ1-42 coincubated with apolipoprotein J demonstrated a two-fold increase in cytotoxicity.
    • (1995) Exp Neurol , vol.136 , pp. 2-31
    • Oda, T.1    Wals, P.2    Osterburg, H.H.3    Pasinetti, G.M.4    Morgan, T.E.5    Rozovsky, I.6    Blainestine, W.7    Snyder, S.W.8    Holzman, F.9    Krafft, G.A.10    Finch, C.B.11
  • 67
    • 0027320359 scopus 로고
    • Beta-amyloid neurotoxicity
    • Forloni G: Beta-amyloid neurotoxicity. Funct Neurol 1993, 8:211-225.
    • (1993) Funct Neurol , vol.8 , pp. 211-225
    • Forloni, G.1
  • 68
    • 0026656042 scopus 로고
    • β-amyloid precursor protein and Alzheimer's disease: The peptide plot thickens
    • Mattson MP, Rydel RE: β-amyloid precursor protein and Alzheimer's disease: the peptide plot thickens. Neurobiol Aging 1992, 13:617-621.
    • (1992) Neurobiol Aging , vol.13 , pp. 617-621
    • Mattson, M.P.1    Rydel, R.E.2
  • 69
    • 0029120647 scopus 로고
    • Evidence for apoptotic cell death in Alzheimer's disease
    • Smale G, Nichols NR, Brady DR, Finch CE, Horton WE Jr: Evidence for apoptotic cell death in Alzheimer's disease. Exp Neurol 1995, 133:225-230. The in situ labelling technique TUNEL (terminal transferase-mediated dUTP-biotin nick end labelling) was used to investigate apoptosis in Alzheimer's disease brains. The incidence of apoptosis was elevated in brains in comparison with age-matched control individuals. Immunostaining indicated that both neurons and astrocytes were undergoing apoptosis.
    • (1995) Exp Neurol , vol.133 , pp. 225-230
    • Smale, G.1    Nichols, N.R.2    Brady, D.R.3    Finch, C.E.4    Horton Jr., W.E.5
  • 70
    • 0029040355 scopus 로고
    • In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes
    • Dragunow M, Faull RLM, Lawlor P, Beilharz EJ, Singleton K, Walker EB, Mee E: In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. NeuroReport 1995, 6:1053-1057. Using the TUNEL technique, DNA fragmentation was observed in cells in the temporal cortex and hippocampus of Alzheimer's disease patients and in the striatum of Huntington's disease patients, whereas in neurologically normal human brains very few apoptotic cells were identified.
    • (1995) NeuroReport , vol.6 , pp. 1053-1057
    • Dragunow, M.1    Faull, R.L.M.2    Lawlor, P.3    Beilharz, E.J.4    Singleton, K.5    Walker, E.B.6    Mee, E.7
  • 72
    • 0029055175 scopus 로고
    • Oxidative process and antioxidative defense mechanisms in the aging brain
    • Reiter RJ: Oxidative process and antioxidative defense mechanisms in the aging brain. FASEB J 1995, 9:526-533.
    • (1995) FASEB J , vol.9 , pp. 526-533
    • Reiter, R.J.1
  • 73
    • 0028059308 scopus 로고
    • Oxidative damage in neurodegenerative disease
    • Jenner P: Oxidative damage in neurodegenerative disease. Lancet 1994, 344:796-798.
    • (1994) Lancet , vol.344 , pp. 796-798
    • Jenner, P.1
  • 74
    • 0027496238 scopus 로고
    • A radical hypothesis for neurodegeneration
    • Olanow CW: A radical hypothesis for neurodegeneration. Trends Neurosci 1993, 16:439-444.
    • (1993) Trends Neurosci , vol.16 , pp. 439-444
    • Olanow, C.W.1
  • 75
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Buttke TM, Sandstrom PA: Oxidative stress as a mediator of apoptosis. Immunol Today 1994, 15:7-10.
    • (1994) Immunol Today , vol.15 , pp. 7-10
    • Buttke, T.M.1    Sandstrom, P.A.2
  • 77
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D: Hydrogen peroxide mediates amyloid β protein toxicity. Cell 1994, 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 79
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • Mattson MP, Goodman Y: Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res 1995, 676:219-224.
    • (1995) Brain Res , vol.676 , pp. 219-224
    • Mattson, M.P.1    Goodman, Y.2
  • 82
    • 0028208495 scopus 로고
    • Glutamate uptake by oxygen free radicals in rat cortical astrocytes
    • Volterra A, Trotti D, Tromba C, Floridi S, Racagni G: Glutamate uptake by oxygen free radicals in rat cortical astrocytes. J Neurosci 1994, 14:2924-2932.
    • (1994) J Neurosci , vol.14 , pp. 2924-2932
    • Volterra, A.1    Trotti, D.2    Tromba, C.3    Floridi, S.4    Racagni, G.5
  • 83
    • 0028980414 scopus 로고
    • β-amyloid peptide-derived, oxygen-dependent free radicals inhibit glutamate uptake in cultured astrocytes: Implications for Alzheimer's disease
    • Harris ME, Carney JM, Cole PS, Hensley K, Howard BJ, Martin L, Bummer P, Wang Y, Pedigo NWJR, Butterfield DA: β-amyloid peptide-derived, oxygen-dependent free radicals inhibit glutamate uptake in cultured astrocytes: implications for Alzheimer's disease. NeuroReport 1995, 6:1875-1879. The production of radicals by Aβ peptides can directly activate a neurodegenerative mechanism and can produce an excess of glutamate (through an inhibition of glutamate uptake in astrocytes) that might contribute to the Aβ neurotoxicity.
    • (1995) NeuroReport , vol.6 , pp. 1875-1879
    • Harris, M.E.1    Carney, J.M.2    Cole, P.S.3    Hensley, K.4    Howard, B.J.5    Martin, L.6    Bummer, P.7    Wang, Y.8    Pedigo, N.W.J.R.9    Butterfield, D.A.10
  • 84
    • 0025110182 scopus 로고
    • β-amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxin damage
    • Koh J, Yang LL, Cotman CW: β-amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxin damage. Brain Res 1990, 533:315-320.
    • (1990) Brain Res , vol.533 , pp. 315-320
    • Koh, J.1    Yang, L.L.2    Cotman, C.W.3
  • 85
    • 0026333250 scopus 로고
    • β-amyloid increases neuronal susceptibility to injury by glucose deprivation
    • Copani A, Koh JY, Cotman CW: β-amyloid increases neuronal susceptibility to injury by glucose deprivation. NeuroReport 1991, 2:763-765.
    • (1991) NeuroReport , vol.2 , pp. 763-765
    • Copani, A.1    Koh, J.Y.2    Cotman, C.W.3
  • 86
    • 0011849134 scopus 로고
    • 25-35 potentiates neurodegeneration mediated by glutamate
    • 25-35 potentiates neurodegeneration mediated by glutamate. Alzheimer's Res 1995, 1:41-44. Pretreatment of cortical neurons for 2 days with a sublethal concentration of β25-35 had no effect by itself but it rendered the neurons more vulnerable to degeneration mediated by glutamate. However, exposure to the same amount of β25-35 together with glutamate for 15 min did not alter the toxic effect of glutamate.
    • (1995) Alzheimer's Res , vol.1 , pp. 41-44
    • Patel, A.J.1
  • 88
    • 0028180304 scopus 로고
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurons in culture
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurons in culture. J Neurochem 1994, 62:372-375.
    • (1994) J Neurochem , vol.62 , pp. 372-375
    • Weiss, J.H.1    Pike, C.J.2    Cotman, C.3
  • 89
    • 0027429732 scopus 로고
    • Beta-amyloid neurotoxicity in human cortical culture is not mediated by excitotoxins
    • Busciglio J, Yeh J, Yankner BA: Beta-amyloid neurotoxicity in human cortical culture is not mediated by excitotoxins. J Neurochem 1993, 61:1565-1568.
    • (1993) J Neurochem , vol.61 , pp. 1565-1568
    • Busciglio, J.1    Yeh, J.2    Yankner, B.A.3
  • 90
    • 0029056516 scopus 로고
    • Cell death induced β-amyloid 1-40 in MES 23.5 hybrid clone: The role of nitric oxide and NMDA-gated channel activation leading apoptosis
    • Le W-D, Colom L, Xie W-J, Smith G, Alexianu M, Appel SH: Cell death induced β-amyloid 1-40 in MES 23.5 hybrid clone: the role of nitric oxide and NMDA-gated channel activation leading apoptosis. Brain Res 1995, 686:40-60.
    • (1995) Brain Res , vol.686 , pp. 40-60
    • Le, W.-D.1    Colom, L.2    Xie, W.-J.3    Smith, G.4    Alexianu, M.5    Appel, S.H.6
  • 92
    • 0026033998 scopus 로고
    • Amyloid protein of Gerstmann-Sträussler- Scheinker disease (Indiana Kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58
    • Tagliavini F, Prelli F, Ghiso J, Bugiani O, Serban D, Prusiner SB, Farlow MR, Ghetti B, Frangione B: Amyloid protein of Gerstmann-Sträussler- Scheinker disease (Indiana Kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J 1991, 10:513-519.
    • (1991) EMBO J , vol.10 , pp. 513-519
    • Tagliavini, F.1    Prelli, F.2    Ghiso, J.3    Bugiani, O.4    Serban, D.5    Prusiner, S.B.6    Farlow, M.R.7    Ghetti, B.8    Frangione, B.9
  • 95
    • 0028172208 scopus 로고
    • The Alzheimer Aβ peptide develops protease resistance in association with its polymerization into fibrils
    • Nordstedt C, Naslund J, Tjernberg LO, Karlstrom AR, Thyberg J, Terenius L: The Alzheimer Aβ peptide develops protease resistance in association with its polymerization into fibrils. J Biol Chem 1994, 269:30773-30776.
    • (1994) J Biol Chem , vol.269 , pp. 30773-30776
    • Nordstedt, C.1    Naslund, J.2    Tjernberg, L.O.3    Karlstrom, A.R.4    Thyberg, J.5    Terenius, L.6
  • 96
    • 0027388993 scopus 로고
    • Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
    • Gasset M, Baldwin MA, Flettenck RJ, Prusiner SB: Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc Natl Acad Sci U S A 1993, 90:1-5.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 1-5
    • Gasset, M.1    Baldwin, M.A.2    Flettenck, R.J.3    Prusiner, S.B.4
  • 97
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by Congo red
    • Caughy B, Race RE: Potent inhibition of scrapie-associated PrP accumulation by Congo red. J Neurochem 1992, 59:768-771.
    • (1992) J Neurochem , vol.59 , pp. 768-771
    • Caughy, B.1    Race, R.E.2
  • 99
    • 0028301577 scopus 로고
    • Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
    • De Gioia L, Selvaggini C, Ghibaudi E, Diomede L, Bugiani O, Forloni G, Tagliavini F, Salmona M: Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J Biol Chem 1994, 269:7859-7862.
    • (1994) J Biol Chem , vol.269 , pp. 7859-7862
    • De Gioia, L.1    Selvaggini, C.2    Ghibaudi, E.3    Diomede, L.4    Bugiani, O.5    Forloni, G.6    Tagliavini, F.7    Salmona, M.8
  • 100
    • 0028925377 scopus 로고
    • Prion protein peptides induce α-helix to β-sheet conformational transition
    • Nguyen J, Baldwin MA, Cohen FE, Prusiner SB: Prion protein peptides induce α-helix to β-sheet conformational transition. Biochemistry 1995, 34:4186-4192. The PrP peptides were used to investigate the conformational character of transition between PrPc and PrPsc The addition of high β-sheet conformed peptide PrP 109-122 to an acetonitrile solution containing PrP 104-122, that itself had a low level of β-sheet, progressively converted PrP 104-122 to the β-sheet conformation.
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1    Baldwin, M.A.2    Cohen, F.E.3    Prusiner, S.B.4
  • 102
    • 0028008896 scopus 로고
    • Detection of apoptosis induced DNA cleavage in scrapie-infected sheep brain
    • Fairbain DW, Camahan KG, Thwaits RN, Grigsby RV, Reed Holyoak G, O'Neill KL: Detection of apoptosis induced DNA cleavage in scrapie-infected sheep brain. FEMS Microbiol Lett 1995, 115:341-346. The authors reported the detection of DNA damage consistent with apoptosis in the brain cells of sheep infected with scrapie using laser scanning microscope analysis of the single cell assay.
    • (1995) FEMS Microbiol Lett , vol.115 , pp. 341-346
    • Fairbain, D.W.1    Camahan, K.G.2    Thwaits, R.N.3    Grigsby, R.V.4    Reed Holyoak, G.5    O'Neill, K.L.6
  • 104
    • 13344282734 scopus 로고    scopus 로고
    • Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene
    • Sakaguchi S, Katamine S, Nishida N, Moriuci R, Shigematsu K, Sugimoto T, Nakatani A, Kataoka Y, Houtani T, Shirabe S et al.: Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 1996, 380:528-531. The PrP-null mice grew normally after birth, but at about 70 weeks of age they all began to show the progressive symptoms of ataxia. Pathological examination revealed extensive loss of Purkinje cells in the majority of cerebellar folia, suggesting that PrP plays a role in the long-term survival of Purkinje cells.
    • (1996) Nature , vol.380 , pp. 528-531
    • Sakaguchi, S.1    Katamine, S.2    Nishida, N.3    Moriuci, R.4    Shigematsu, K.5    Sugimoto, T.6    Nakatani, A.7    Kataoka, Y.8    Houtani, T.9    Shirabe, S.10
  • 105
    • 15844421385 scopus 로고    scopus 로고
    • Altered circadian activity rhythms and sleep in mice devoid of prion protein
    • Tobler I, Gaus SE, Deboer T, Achermann P, Fischer M, Rüliche T, Moser M, Oesch B, McBride PA, Manson JC: Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 1996, 380:639-642. In two lines of PrP-null mice there was an alteration in both circadian activity rhythms and sleep patterns. Because of the intriguing similarities to rhythm and sleep alterations in fatal familial insomnia, the authors suggested that loss of function of PrP leads to neurological dysfunction in at least one of the prion diseases.
    • (1996) Nature , vol.380 , pp. 639-642
    • Tobler, I.1    Gaus, S.E.2    Deboer, T.3    Achermann, P.4    Fischer, M.5    Rüliche, T.6    Moser, M.7    Oesch, B.8    McBride, P.A.9    Manson, J.C.10
  • 106
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown DR, Herms J, Kretzschmar HA: Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. NeuroReport 1994, 5:2057-2060.
    • (1994) NeuroReport , vol.5 , pp. 2057-2060
    • Brown, D.R.1    Herms, J.2    Kretzschmar, H.A.3
  • 107
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
    • Brown DR, Schmidt B, Kretzschmar HA: Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 1996, 380:345-347. The toxic effect of amyloidogenic peptide homologous to the 106-126 fragment of prion protein requires the presence of microglia which respond to PrP 106-126 by increasing their oxygen radical production. The combined direct and microglia-mediated effects of PrP 106-126 are toxic to normal neurons but are not active on neurons from PrP-deficient mice.
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 108
    • 0028004290 scopus 로고
    • Amyloid fibrils in Gerstmann-Sträussler-Scheinker disease (Indiana and Swedish kindreds) express only PrP peptides encoded by the mutant allele
    • Tagliavini F, Prelli F, Porro M, Rossi G, Giaccone G, Farlow MR, Diouthy SR, Ghetti B, Bugiani O, Frangione B: Amyloid fibrils in Gerstmann-Sträussler-Scheinker disease (Indiana and Swedish kindreds) express only PrP peptides encoded by the mutant allele. Cell 1994, 79:695-703.
    • (1994) Cell , vol.79 , pp. 695-703
    • Tagliavini, F.1    Prelli, F.2    Porro, M.3    Rossi, G.4    Giaccone, G.5    Farlow, M.R.6    Diouthy, S.R.7    Ghetti, B.8    Bugiani, O.9    Frangione, B.10
  • 109
    • 0000383864 scopus 로고
    • Ageing and dementias
    • Edited by Hume-Adams J, Duchenne L. London: Edward Arnold
    • Tomlinson BE: Ageing and dementias. In Greenfield's neuropathology, Edited by Hume-Adams J, Duchenne L. London: Edward Arnold; 1993:1284-1410.
    • (1993) Greenfield's Neuropathology , pp. 1284-1410
    • Tomlinson, B.E.1


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