메뉴 건너뛰기




Volumn 148, Issue 4, 1998, Pages 67-73

Transmissible spongiform encephalopathies (Prion diseases) - Molecular biology and in vitro models;Ubertragbare spongiforme enzephalopathien (Prion-krankheiten) - Molekulare grundlagen und in-vitro-modelle

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PRION PROTEIN;

EID: 0031595526     PISSN: 00435341     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (1)

References (93)
  • 3
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borehelt DR, Scott D, Taraboulos A, Stahl N, Prusiner SB: Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J Cell Biol 1990;110:743-752.
    • (1990) J Cell Biol , vol.110 , pp. 743-752
    • Borehelt, D.R.1    Scott, D.2    Taraboulos, A.3    Stahl, N.4    Prusiner, S.B.5
  • 4
    • 0028356488 scopus 로고
    • Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous system
    • Borchelt DR, Koliatsos VE, Guarnieri M, Pardo CA, Sisodia SS, Price DL: Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous system. J Biol Chem 1994;269:14711-14714.
    • (1994) J Biol Chem , vol.269 , pp. 14711-14714
    • Borchelt, D.R.1    Koliatsos, V.E.2    Guarnieri, M.3    Pardo, C.A.4    Sisodia, S.S.5    Price, D.L.6
  • 6
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of prion protein fragment
    • Brown DR, Schmidt B, Kretzschmar HA: Role of microglia and host prion protein in neurotoxicity of prion protein fragment. Nature 1996;380:345-347.
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 8
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown DR, Schulz-Schaeffer WJ, Schmidt B, Kretzschmar HA: Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp Neurol 1997;146:104-112.
    • (1997) Exp Neurol , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 10
    • 0027724039 scopus 로고
    • Apoptosis and necrosis. Basic types and mechanisms of cell death
    • Buja LM, Eigenbrodt ML, Eigenbrodt EH: Apoptosis and necrosis. Basic types and mechanisms of cell death. Arch Pathol Lab Med 1993;117:1208-1214.
    • (1993) Arch Pathol Lab Med , vol.117 , pp. 1208-1214
    • Buja, L.M.1    Eigenbrodt, M.L.2    Eigenbrodt, E.H.3
  • 13
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-sensitive and phospholipase-sensitive
    • Caughey B, Raymond GJ: The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-sensitive and phospholipase-sensitive. J Biol Chem 1991;266:18217-18223.
    • (1991) J Biol Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 14
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS: Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991;30:7672-7679.
    • (1991) Biochemistry , vol.30 , pp. 7672-7679
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 16
    • 0025859996 scopus 로고
    • Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease
    • Collinge J, Palmer MS, Dryden AJ: Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease. Lancet 1991;337:1441-1442.
    • (1991) Lancet , vol.337 , pp. 1441-1442
    • Collinge, J.1    Palmer, M.S.2    Dryden, A.J.3
  • 19
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of "new variant" CJD
    • Collinge J, Sidle KCL, Meads J, Ironside J, Hill AF: Molecular analysis of prion strain variation and the aetiology of "new variant" CJD. Nature 1996;383:685-690.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 20
    • 33746127253 scopus 로고
    • Über eine eigenartige herdförmige Erkrankung des Zentralnervensystems
    • Creutzfeldt HG: Über eine eigenartige herdförmige Erkrankung des Zentralnervensystems. Z Ges Neurol Psychiatr 1920;57:1-18.
    • (1920) Z Ges Neurol Psychiatr , vol.57 , pp. 1-18
    • Creutzfeldt, H.G.1
  • 21
    • 0001289828 scopus 로고
    • La maladie dite tremblante du mouton cst-elle inoculable?
    • Cuillé J, Chelle P-L: La maladie dite tremblante du mouton cst-elle inoculable? C R Acad Sci 1936;(III)203:1552-1554.
    • (1936) C R Acad Sci , vol.203 , Issue.3 , pp. 1552-1554
    • Cuillé, J.1    Chelle, P.-L.2
  • 23
    • 0027972696 scopus 로고
    • Similar genetic susceptibility in iatrogenic and sporadic Creutzfeldt-Jakob disease
    • Deslys J-P, Marcé D, Dormont D: Similar genetic susceptibility in iatrogenic and sporadic Creutzfeldt-Jakob disease. J Gen Virol 1994;75:23-27.
    • (1994) J Gen Virol , vol.75 , pp. 23-27
    • Deslys, J.-P.1    Marcé, D.2    Dormont, D.3
  • 27
    • 0029026433 scopus 로고
    • Early loss of neurons and axon terminals in scrapie-affected mice revealed by morphometry and immunocytochemistry
    • Fraser J, Jeffrey M, Halliday W, Fowler N, Goodsir C, Brown D: Early loss of neurons and axon terminals in scrapie-affected mice revealed by morphometry and immunocytochemistry. Mol Chem Neuropathol 1995;24:245-249.
    • (1995) Mol Chem Neuropathol , vol.24 , pp. 245-249
    • Fraser, J.1    Jeffrey, M.2    Halliday, W.3    Fowler, N.4    Goodsir, C.5    Brown, D.6
  • 29
    • 0014021742 scopus 로고
    • Experimental transmission of a kuru-like syndrome to chimpanzees
    • Gajdusek DC, Gibbs CJ, Alpers M: Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 1966;209:794-796.
    • (1966) Nature , vol.209 , pp. 794-796
    • Gajdusek, D.C.1    Gibbs, C.J.2    Alpers, M.3
  • 30
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y, Sherman Y, Ben-Sasson SA: Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 1992;119:493-501.
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 31
    • 0027163053 scopus 로고
    • Detection of DNA fragmentation in apoptosis: Application of in situ nick translation to cell culture systems and tissue sections
    • Gold R, Schmied M, Rothe G, Zischler H, Breitschopf H, Wekerle H, Lassmann H: Detection of DNA fragmentation in apoptosis: application of in situ nick translation to cell culture systems and tissue sections. J Histochem Cytochem 1993;41:1023-1030.
    • (1993) J Histochem Cytochem , vol.41 , pp. 1023-1030
    • Gold, R.1    Schmied, M.2    Rothe, G.3    Zischler, H.4    Breitschopf, H.5    Wekerle, H.6    Lassmann, H.7
  • 34
    • 0026017096 scopus 로고
    • Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon
    • Goldmann W, Hunter N, Martin T, Dawson M, Hope J: Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon. J Gen Virol 1991;72:201-204.
    • (1991) J Gen Virol , vol.72 , pp. 201-204
    • Goldmann, W.1    Hunter, N.2    Martin, T.3    Dawson, M.4    Hope, J.5
  • 35
    • 49749220574 scopus 로고
    • Scrapie and kuru
    • Hadlow WJ: Scrapie and kuru. Lancet 1959;II:289-290.
    • (1959) Lancet , vol.2 , pp. 289-290
    • Hadlow, W.J.1
  • 36
    • 0028793453 scopus 로고
    • Patch-clamp analysis of synaptic transmission to cerebellar Purkinje cells of prion protein knockout mice
    • Herms JW, Kretzschmar HA, Titz S, Keller BU: Patch-clamp analysis of synaptic transmission to cerebellar Purkinje cells of prion protein knockout mice. Eur J Neurosci 1995;7:2508-2512.
    • (1995) Eur J Neurosci , vol.7 , pp. 2508-2512
    • Herms, J.W.1    Kretzschmar, H.A.2    Titz, S.3    Keller, B.U.4
  • 40
    • 0000781428 scopus 로고
    • Über eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswertem anatomischem Befunde (spastische Pseudosklerosc-Encephalomyelopathie mit disseminierten Degenerationsherden)
    • Jakob A: Über eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswertem anatomischem Befunde (spastische Pseudosklerosc-Encephalomyelopathie mit disseminierten Degenerationsherden). Dtsch Z Nervenheilk 1921;70:132-146.
    • (1921) Dtsch Z Nervenheilk , vol.70 , pp. 132-146
    • Jakob, A.1
  • 41
    • 0002691909 scopus 로고    scopus 로고
    • Spastische Pseudosklerose
    • Jakob A (ed): Berlin: Springer
    • Jakob A: Spastische Pseudosklerose. In Jakob A (ed): Die extrapyramidalen Erkrankungen. Berlin: Springer, pp. 215-245.
    • Die Extrapyramidalen Erkrankungen , pp. 215-245
    • Jakob, A.1
  • 42
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid - A pathogenic mechanism in Alzheimer's disease and scrapie
    • Jarrett JT, Lansbury PT: Seeding one-dimensional crystallization of amyloid - a pathogenic mechanism in Alzheimer's disease and scrapie. Cell 1993;73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 43
    • 0028949460 scopus 로고
    • Early unsuspected neuron and axon terminal loss in scrapie-in-fected mice revealed by morphometry and immunocytochemistry
    • Jeffrey M, Fraser JR, Halliday WG, Fowler N, Goodsir CM, Brown DA: Early unsuspected neuron and axon terminal loss in scrapie-in-fected mice revealed by morphometry and immunocytochemistry. Neuropathol Appl Neurobiol 1995;21:41-49.
    • (1995) Neuropathol Appl Neurobiol , vol.21 , pp. 41-49
    • Jeffrey, M.1    Fraser, J.R.2    Halliday, W.G.3    Fowler, N.4    Goodsir, C.M.5    Brown, D.A.6
  • 44
    • 0026604959 scopus 로고
    • Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis
    • Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D: Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis. J Gen Virol 1992;73:1025-1029.
    • (1992) J Gen Virol , vol.73 , pp. 1025-1029
    • Kellings, K.1    Meyer, N.2    Mirenda, C.3    Prusiner, S.B.4    Riesner, D.5
  • 45
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JFR, Wyllie AH, Currie AR: Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972;26:239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 47
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
    • Kocisko DA, Priola SA, Raymond GJ, Chesebro, B, Lansbury PT, Caughey B: Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier. Proc Natl Acad Sci USA 1995;92:3923-3927.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    Lansbury, P.T.5    Caughey, B.6
  • 50
    • 0028894604 scopus 로고
    • Codon 178 mutation of the human prion protein gene in a German family (Backer family): Sequencing data from 72 year-old celloidin-embedded brain tissue
    • Berl
    • Kretzschmar HA, Neumann M, Stavrou D: Codon 178 mutation of the human prion protein gene in a German family (Backer family): sequencing data from 72 year-old celloidin-embedded brain tissue. Acta Neuropathol (Berl) 1995;89:96-98.
    • (1995) Acta Neuropathol , vol.89 , pp. 96-98
    • Kretzschmar, H.A.1    Neumann, M.2    Stavrou, D.3
  • 52
    • 0029916617 scopus 로고    scopus 로고
    • Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus
    • Lledo PM, Tremblay P, DeArmond SJ, Prusiner SB, Nicoll RA: Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc Natl Acad Sci USA 1996;93:2403-2407.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2403-2407
    • Lledo, P.M.1    Tremblay, P.2    DeArmond, S.J.3    Prusiner, S.B.4    Nicoll, R.A.5
  • 54
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • Manson JC, Clarke AR, Hooper ML, Aitchison L, McConnell I, Hope J: 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 1994;8:121-127.
    • (1994) Mol Neurobiol , vol.8 , pp. 121-127
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3    Aitchison, L.4    McConnell, I.5    Hope, J.6
  • 55
    • 0028703452 scopus 로고
    • PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology
    • Manson JC, Clarke AR, McBride PA, McConnell I, Hope J: PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 1994;3:331-340.
    • (1994) Neurodegeneration , vol.3 , pp. 331-340
    • Manson, J.C.1    Clarke, A.R.2    McBride, P.A.3    McConnell, I.4    Hope, J.5
  • 57
    • 0019778656 scopus 로고
    • Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Sträussler syndrome. with an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies
    • Masters CL, Gajdusek DC, Gibbs CJ jr: Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Sträussler syndrome. With an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies. Brain 1981;104:559-588.
    • (1981) Brain , vol.104 , pp. 559-588
    • Masters, C.L.1    Gajdusek, D.C.2    Gibbs Jr., C.J.3
  • 58
    • 0000940311 scopus 로고
    • Klinische und genealogische Beobachtungen bei einem Fall von spastischer Pseudosklerose
    • Meggendorfer F: Klinische und genealogische Beobachtungen bei einem Fall von spastischer Pseudosklerose. Z Ges Neurol Psychiatr 1930;128:337-341.
    • (1930) Z Ges Neurol Psychiatr , vol.128 , pp. 337-341
    • Meggendorfer, F.1
  • 59
    • 0026675218 scopus 로고
    • Creutzfeldt-Jakob disease with codon-129 polymorphism (valine). A comparative study of patients with codon-102 point mutation or without mutations
    • Berl
    • Miyazono M, Kitamoto T, Dohura K, Iwaki T, Tateishi J: Creutzfeldt-Jakob disease with codon-129 polymorphism (valine). A comparative study of patients with codon-102 point mutation or without mutations. Acta Neuropathol (Berl) 1992;84:349-354.
    • (1992) Acta Neuropathol , vol.84 , pp. 349-354
    • Miyazono, M.1    Kitamoto, T.2    Dohura, K.3    Iwaki, T.4    Tateishi, J.5
  • 60
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • Moser M, Colello RJ, Pott U, Oesch B: Developmental expression of the prion protein gene in glial cells. Neuron 1995;14:509-517.
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 63
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer MS, Dryden AJ, Hughes JT, Collinge J: Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 1991;352:340-342.
    • (1991) Nature , vol.352 , pp. 340-342
    • Palmer, M.S.1    Dryden, A.J.2    Hughes, J.T.3    Collinge, J.4
  • 64
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan KM, Stahl N, Prusiner SB: Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci 1992;1:1343-1352.
    • (1992) Protein Sci , vol.1 , pp. 1343-1352
    • Pan, K.M.1    Stahl, N.2    Prusiner, S.B.3
  • 69
    • 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
  • 72
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB: Molecular biology of prion diseases. Science 1991;252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 74
    • 0028876414 scopus 로고
    • Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent
    • Race RE, Priola SA, Bessen RA, Ernst D, Dockter J, Rall GF, Mucke L, Chesebro B, Oldstone MBA: Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron 1995;15:1183-1191.
    • (1995) Neuron , vol.15 , pp. 1183-1191
    • Race, R.E.1    Priola, S.A.2    Bessen, R.A.3    Ernst, D.4    Dockter, J.5    Rall, G.F.6    Mucke, L.7    Chesebro, B.8    Oldstone, M.B.A.9
  • 76
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-lenth recombinant murine prion protein. mPrP(23-231)
    • Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K: NMR characterization of the full-lenth recombinant murine prion protein. mPrP(23-231). FEBS Lett 1997;413:282-288.
    • (1997) FEBS Lett , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüthrich, K.5
  • 81
    • 0020405571 scopus 로고
    • Necrosis and apoptosis: Distinct modes of cell death with fundamentally different significance
    • Searle J, Kerr JFR, Bishop CJ: Necrosis and apoptosis: distinct modes of cell death with fundamentally different significance. Path Ann 1982;17:229-259.
    • (1982) Path Ann , vol.17 , pp. 229-259
    • Searle, J.1    Kerr, J.F.R.2    Bishop, C.J.3
  • 82
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng SL, Huber MT, Harris DA: A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J Biol Chem 1993;268:15922-15928.
    • (1993) J Biol Chem , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 83
    • 0027408285 scopus 로고
    • Electron microscopic analysis of adrenalectomy-induced hippocampal granule cell degeneration in the rat: Apoptosis in the adult central nervous system
    • Sloviter RS, Dean E, Neubort S: Electron microscopic analysis of adrenalectomy-induced hippocampal granule cell degeneration in the rat: apoptosis in the adult central nervous system. J Comp Neurol 1993;330:337-351.
    • (1993) J Comp Neurol , vol.330 , pp. 337-351
    • Sloviter, R.S.1    Dean, E.2    Neubort, S.3
  • 84
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phospatidylinositol glycolipid
    • Stahl N, Borchelt DR, Hsiao K, Prusiner SB: Scrapie prion protein contains a phospatidylinositol glycolipid. Cell 1987;51:229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 85
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, DeArmond SJ, Prusiner SB: Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995;83:79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 89
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • Westaway D, DeArmond SJ, Cayetano-Canlas J, Groth D, Foster D, Yang SL, Torchia M, Carlson GA, Prusiner SB: Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 1994;76:117-129.
    • (1994) Cell , vol.76 , pp. 117-129
    • Westaway, D.1    DeArmond, S.J.2    Cayetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9
  • 92
    • 0029077964 scopus 로고
    • A candidate marsupial PrP gene reveals two domains conserved in mammalian PrP proteins
    • Windl O, Dempster M, Estibeiro P, Lathe R: A candidate marsupial PrP gene reveals two domains conserved in mammalian PrP proteins. Gene 1995;159:181-186.
    • (1995) Gene , vol.159 , pp. 181-186
    • Windl, O.1    Dempster, M.2    Estibeiro, P.3    Lathe, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.