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Volumn 9, Issue 2, 2003, Pages 183-193

Prion diseases

Author keywords

Bovine spongiform encephalopathy; Creutzfeldt Jakob disease; Fatal familial insomnia; Gerstmann Straussler Scheinker syndrome; Kuru; Prion; Scrapie; Spongiform encephalopathy

Indexed keywords

BOVINE SPONGIFORM ENCEPHALOPATHY; CATTLE; CREUTZFELDT JAKOB DISEASE; DEGENERATIVE DISEASE; EPIDEMIC; FATAL FAMILIAL INSOMNIA; GERSTMANN STRAUSSLER SCHEINKER SYNDROME; HUMAN; INHERITANCE; KURU; MEDICAL RESEARCH; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; REVIEW; UNITED KINGDOM; VIRUS STRAIN;

EID: 0038813672     PISSN: 13550284     EISSN: None     Source Type: Journal    
DOI: 10.1080/13550280390194082     Document Type: Review
Times cited : (64)

References (74)
  • 1
    • 0027443762 scopus 로고
    • The scrapie enigma: Insights from radiation experiments
    • Alper T (1993). The scrapie enigma: insights from radiation experiments. Radiat Res 135: 283-292.
    • (1993) Radiat. Res. , vol.135 , pp. 283-292
    • Alper, T.1
  • 2
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T, Cramp WA, Haig DA, Clarke MC (1967). Does the agent of scrapie replicate without nucleic acid? Nature 214: 764-766.
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 6
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen RA, Marsh RF (1992). Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66: 2096-2101.
    • (1992) J. Virol. , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 7
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen RA, Marsh RF (1994). Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68: 7859-7868.
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 8
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley MP, Prusiner SB (1982). Identification of a protein that purifies with the scrapie prion. Science 218: 1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 11
    • 0028256033 scopus 로고
    • Iatrogenic Creutzfeldt-Jakob disease: An example of the interplay between ancient genes and modern medicine
    • Brown P, Cervenakova L, Goldfarb MD, McCombie WR, Rubenstein R, Will RG, et al (1994). Iatrogenic Creutzfeldt-Jakob disease: an example of the interplay between ancient genes and modern medicine. Neurology 44: 291-293.
    • (1994) Neurology , vol.44 , pp. 291-293
    • Brown, P.1    Cervenakova, L.2    Goldfarb, M.D.3    McCombie, W.R.4    Rubenstein, R.5    Will, R.G.6
  • 14
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler H, Fischer M, Lang Y, Bluethmann H, Lipp H-P, DeArmond SJ, et al (1992). Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature, 356: 577-582.
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3    Bluethmann, H.4    Lipp, H.-P.5    DeArmond, S.J.6
  • 15
    • 0029995499 scopus 로고    scopus 로고
    • Creutzfeldt-Jakob disease transmitted by dura mater graft
    • Clavel M, Clavel P (1996). Creutzfeldt-Jakob disease transmitted by dura mater graft. Eur Neurol 36: 239-240.
    • (1996) Eur. Neurol. , vol.36 , pp. 239-240
    • Clavel, M.1    Clavel, P.2
  • 16
    • 0033600407 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease
    • Collinge J (1999). Variant Creutzfeldt-Jakob disease. Lancet 354: 317-323.
    • (1999) Lancet , vol.354 , pp. 317-323
    • Collinge, J.1
  • 17
    • 0026650443 scopus 로고
    • Inherited prion disease with 144 base pair gene insertion: II: Clinical and pathological features
    • Collinge J, Brown J, Hardy J, Mullan M, Rossor MN, Baker H, et al (1992). Inherited prion disease with 144 base pair gene insertion: II: Clinical and pathological features. Brain 115: 687-710.
    • (1992) Brain , vol.115 , pp. 687-710
    • Collinge, J.1    Brown, J.2    Hardy, J.3    Mullan, M.4    Rossor, M.N.5    Baker, H.6
  • 19
    • 0025859996 scopus 로고
    • Genetic predisposition to Iatrogenic Creutzfeldt-Jakob disease
    • Collinge J, Palmer MS, Dryden AJ (1991). Genetic predisposition to Iatrogenic Creutzfeldt-Jakob disease. Lancet 337: 1441-1442.
    • (1991) Lancet , vol.337 , pp. 1441-1442
    • Collinge, J.1    Palmer, M.S.2    Dryden, A.J.3
  • 21
    • 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 (1996). Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 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
  • 22
    • 33746127253 scopus 로고
    • Uber eine eigenartige herdfoermige Erkrankung des Zentralnervensystems
    • Creutzfeldt HG (1920). Uber eine eigenartige herdfoermige Erkrankung des Zentralnervensystems. Z Gesamte Neurol Psychiatry 57: 1-18.
    • (1920) Z. Gesamte. Neurol. Psychiatry , vol.57 , pp. 1-18
    • Creutzfeldt, H.G.1
  • 23
    • 0032032312 scopus 로고    scopus 로고
    • Prion protein expression in human leukocyte differentiation
    • Dodelet VC, Cashman NR (1998). Prion protein expression in human leukocyte differentiation. Blood 91: 1556-1561.
    • (1998) Blood , vol.91 , pp. 1556-1561
    • Dodelet, V.C.1    Cashman, N.R.2
  • 24
    • 0021282464 scopus 로고
    • Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen
    • Ehlers B, Diringer H (1984). Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. J Gen Virol 65: 1325-1330.
    • (1984) J. Gen. Virol. , vol.65 , pp. 1325-1330
    • Ehlers, B.1    Diringer, H.2
  • 25
    • 0022609913 scopus 로고
    • Prolongation of scrapie incubation period by an injection of dextran sulphate 500 within the month before or after infection
    • Farquhar CF, Dickinson AG (1986). Prolongation of scrapie incubation period by an injection of dextran sulphate 500 within the month before or after infection. J Gen Virol 67: 463-473.
    • (1986) J. Gen. Virol. , vol.67 , pp. 463-473
    • Farquhar, C.F.1    Dickinson, A.G.2
  • 26
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino terminal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M, Rulicke T, Raber A, Sailer A, Oesch B, Brandner S, et al (1996). Prion protein (PrP) with amino terminal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 15: 1255-1264.
    • (1996) EMBO J. , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raber, A.3    Sailer, A.4    Oesch, B.5    Brandner, S.6
  • 27
    • 0014021742 scopus 로고
    • Experimental transmission of a kuru-like syndrome to chimpanzees
    • Gajdusek DC, Gibbs CJ Jr, Alpers MP (1966). Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 209: 794-796.
    • (1966) Nature , vol.209 , pp. 794-796
    • Gajdusek, D.C.1    Gibbs C.J., Jr.2    Alpers, M.P.3
  • 29
    • 0036215760 scopus 로고    scopus 로고
    • The epidemiology of variant Creutzfeldt-Jakob disease in Europe
    • Ghani AC (2002). The epidemiology of variant Creutzfeldt-Jakob disease in Europe. Microb Infect 4: 385-393.
    • (2002) Microb. Infect. , vol.4 , pp. 385-393
    • Ghani, A.C.1
  • 32
    • 0024333687 scopus 로고
    • Transplanted infections: Donor-to-host transmission with the allograft
    • Gottesdiener KM (1989). Transplanted infections: donor-to-host transmission with the allograft. Ann Intern Med 110: 1001-1016.
    • (1989) Ann. Intern. Med. , vol.110 , pp. 1001-1016
    • Gottesdiener, K.M.1
  • 33
    • 0014190760 scopus 로고
    • Self Replication and scrapie
    • Griffith JS (1967). Self Replication and scrapie. Nature 215: 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 34
    • 0033573778 scopus 로고    scopus 로고
    • Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples
    • Hill AF, Butterworth RJ, Joiner S, Jackson G, Rossor MN, Thomas DJ, et al (1999). Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples. Lancet 353: 183-189.
    • (1999) Lancet , vol.353 , pp. 183-189
    • Hill, A.F.1    Butterworth, R.J.2    Joiner, S.3    Jackson, G.4    Rossor, M.N.5    Thomas, D.J.6
  • 37
    • 0031015906 scopus 로고    scopus 로고
    • Diagnosis of new variant Creutzfeldt-Jakob disease by tonsil biopsy
    • Hill AF, Zeidler M, Ironside J, Collinge J (1997b). Diagnosis of new variant Creutzfeldt-Jakob disease by tonsil biopsy. Lancet 349: 99-100.
    • (1997) Lancet , vol.349 , pp. 99-100
    • Hill, A.F.1    Zeidler, M.2    Ironside, J.3    Collinge, J.4
  • 38
    • 0037151912 scopus 로고    scopus 로고
    • Accumulation of prion protein in tonsil and appendix: Review of tissue samples
    • Hilton DA, Ghani AC, Conyers L, Edwards P, McCardle L, Penney M, et al (2002). Accumulation of prion protein in tonsil and appendix: review of tissue samples. BMJ 325: 633-634.
    • (2002) BMJ , vol.325 , pp. 633-634
    • Hilton, D.A.1    Ghani, A.C.2    Conyers, L.3    Edwards, P.4    McCardle, L.5    Penney, M.6
  • 39
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw MP, McDermott Jr, Candy JM, Lakey JH (1995). Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem Biophys Res Commun 214: 993-999.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott A., Jr.2    Candy, J.M.3    Lakey, J.H.4
  • 40
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome
    • Hsiao K, Baker HF, Crow TJ, Poulter M, Owen F, Terwilliger JD, et al (1989). Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 338: 342-345.
    • (1989) Nature , vol.338 , pp. 342-345
    • Hsiao, K.1    Baker, H.F.2    Crow, T.J.3    Poulter, M.4    Owen, F.5    Terwilliger, J.D.6
  • 41
    • 0028970386 scopus 로고
    • Congo red prolongs the incubation period in scrapie-infected hamsters
    • Ingrosso L, Ladogana A, Pocchiari M (1995). Congo red prolongs the incubation period in scrapie-infected hamsters. J Virol 69: 506-508.
    • (1995) J. Virol. , vol.69 , pp. 506-508
    • Ingrosso, L.1    Ladogana, A.2    Pocchiari, M.3
  • 44
    • 51849177198 scopus 로고
    • Uber eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswertem anatomischem Befund
    • Jakob A (1921). Uber eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswertem anatomischem Befund. Z Gesamte Neurol Psychiatry 64: 147-228.
    • (1921) Z. Gesamte. Neurol. Psychiatry , vol.64 , pp. 147-228
    • Jakob, A.1
  • 45
    • 0028782011 scopus 로고
    • Nucleic acids in prion preparations: Unspecific background or essential component
    • Kellings K, Prusiner SB, Riesner D (1994). Nucleic acids in prion preparations: unspecific background or essential component. Philos Trans R Soc Lond [Biol] 343: 425-430.
    • (1994) Philos. Trans. R. Soc. Lond. [Biol] , vol.343 , pp. 425-430
    • Kellings, K.1    Prusiner, S.B.2    Riesner, D.3
  • 47
    • 0018329056 scopus 로고
    • Pathogenesis of scrapie: Agent multiplication in brain at the first and second passage of hamster scrapie in mice
    • Kimberlin RH, Walker CA (1979). Pathogenesis of scrapie: agent multiplication in brain at the first and second passage of hamster scrapie in mice. J Gen Virol 42: 107-117.
    • (1979) J. Gen. Virol. , vol.42 , pp. 107-117
    • Kimberlin, R.H.1    Walker, C.A.2
  • 48
    • 0022450560 scopus 로고
    • Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions
    • Kimberlin RH, Walker CA (1986). Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions. Antimicrob Agents Chemother 30: 409-413.
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 409-413
    • Kimberlin, R.H.1    Walker, C.A.2
  • 49
    • 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
    • Kretzschmar HA, Neumann M, Stavrou D (1995). 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) 89: 96-98.
    • (1995) Acta Neuropathol. (Berl) , vol.89 , pp. 96-98
    • Kretzschmar, H.A.1    Neumann, M.2    Stavrou, D.3
  • 50
    • 0028131841 scopus 로고
    • Molecular genetics of prion diseases in France
    • French Research Group on Epidemiology of Human Spongiform Encephalopathies
    • Laplanche J-L, Delasnerie-Lauprêtre N, Brandel JP, Chatelain J, Beaudry P, Alpérovitch A, et al (1994). Molecular genetics of prion diseases in France. French Research Group on Epidemiology of Human Spongiform Encephalopathies. Neurology 44: 2347-2351.
    • (1994) Neurology , vol.44 , pp. 2347-2351
    • Laplanche, J.-L.1    Delasnerie-Lauprêtre, N.2    Brandel, J.P.3    Chatelain, J.4    Beaudry, P.5    Alpérovitch, A.6
  • 52
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci GR, Ratté S, Asante EA, Linehan J, Gowland I, Jefferys JGR, et al (2002). Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J 21: 202-210.
    • (2002) EMBO J. , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratté, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5    Jefferys, J.G.R.6
  • 53
    • 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 (1994). 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 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
    • 0029905230 scopus 로고    scopus 로고
    • Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease
    • Mastrianni JA, Iannicola C, Myers RM, DeArmond S, Prusiner SB (1996). Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease. Neurology 47: 1305-1312.
    • (1996) Neurology , vol.47 , pp. 1305-1312
    • Mastrianni, J.A.1    Iannicola, C.2    Myers, R.M.3    DeArmond, S.4    Prusiner, S.B.5
  • 56
  • 57
    • 0026552043 scopus 로고
    • Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene
    • [see comments]
    • Medori R, Tritschler HJ, LeBlanc A, Villare F, Manetto V, Chen HY, et al (1992a). Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene [see comments]. N Engl J Med 326: 444-449.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 444-449
    • Medori, R.1    Tritschler, H.J.2    LeBlanc, A.3    Villare, F.4    Manetto, V.5    Chen, H.Y.6
  • 58
    • 0026690906 scopus 로고
    • Fatal familial insomnia: A second kindred with mutation of prion protein gene at codon 178
    • Medori R, Montagna P, Tritschler HJ, LeBlanc A, Cortelli P, Tinupar P, et al (1992b). Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178. Neurology 42: 669-670.
    • (1992) Neurology , vol.42 , pp. 669-670
    • Medori, R.1    Montagna, P.2    Tritschler, H.J.3    LeBlanc, A.4    Cortelli, P.5    Tinupar, P.6
  • 59
    • 0025820942 scopus 로고
    • Hemozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer MS, Dryden AJ, Hughes JT, Collinge J (1991). Hemozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 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
  • 60
    • 0001074386 scopus 로고
    • Experiments with scrapie with special reference to the nature of the agent and the pathology of the disease
    • Gajdusek CJ, Gibbs CJ, Alpers MP (eds). Washington DC: US Government Printing
    • Pattison IH (1965). Experiments with scrapie with special reference to the nature of the agent and the pathology of the disease. In: Slow latent and temperate virus infections, NINDB Monograph 2. Gajdusek CJ, Gibbs CJ, Alpers MP (eds). Washington DC: US Government Printing, p. 249-257.
    • (1965) Slow Latent and Temperate Virus Infections, NINDB Monograph 2 , pp. 249-257
    • Pattison, I.H.1
  • 62
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, SB (1982). Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 63
    • 0038741564 scopus 로고
    • D 216. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. D 217. Production of human hemoglobin S antilles in transgenic mice. D 218. Analysis of murine Nmyc function by in situ hydridization and homologous recombination
    • UCLA Symposium Suppl
    • Prusiner SB et al; Rubin E et al; Stanton BR et al (1990). D 216. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. D 217. Production of human hemoglobin S antilles in transgenic mice. D 218. Analysis of murine Nmyc function by in situ hydridization and homologous recombination. J Cellular Biochem UCLA Symposium Suppl 14A: 363.
    • (1990) J. Cellular Biochem. , vol.14 A , pp. 363
    • Prusiner, S.B.1    Rubin, E.2    Stanton, B.R.3
  • 64
    • 0023187877 scopus 로고
    • Pituitary growth hormone from human cadavers: Neurologic disease in ten recipients
    • Rappaport EB, Graham DJ (1987). Pituitary growth hormone from human cadavers: neurologic disease in ten recipients. Neurology 37: 1211-1213.
    • (1987) Neurology , vol.37 , pp. 1211-1213
    • Rappaport, E.B.1    Graham, D.J.2
  • 66
    • 0024820814 scopus 로고
    • Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques
    • Scott M, Foster D, Mirenda C, Serban D, Coufal F, Wälchli M, et al (1989). Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59: 847-857.
    • (1989) Cell , vol.59 , pp. 847-857
    • Scott, M.1    Foster, D.2    Mirenda, C.3    Serban, D.4    Coufal, F.5    Wälchli, M.6
  • 67
    • 0028305135 scopus 로고
    • A glycolipid-anchored prion protein is endocytosed via clathrincoated pits
    • Shyng S-L, Heuser JE, Harris DA (1994). A glycolipid-anchored prion protein is endocytosed via clathrincoated pits. J Cell Biol 125: 1239-1250.
    • (1994) J. Cell Biol. , vol.125 , pp. 1239-1250
    • Shyng, S.-L.1    Heuser, J.E.2    Harris, D.A.3
  • 68
    • 0034650634 scopus 로고    scopus 로고
    • Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides
    • Soto C, Kascsack RJ, Saborío GP, Aucouturier P, Wisniewski T, Prelli F, et al (2000). Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet 355: 192-197.
    • (2000) Lancet , vol.355 , pp. 192-197
    • Soto, C.1    Kascsack, R.J.2    Saborío, G.P.3    Aucouturier, P.4    Wisniewski, T.5    Prelli, F.6
  • 70
    • 17344382240 scopus 로고    scopus 로고
    • Effectiveness of anthracycline against experimental prion disease in syrian hamsters
    • Tagliavini F, McArthur RA, Canciani B, Giaccone G, Porro M, Bugiani M, et al (1997). Effectiveness of anthracycline against experimental prion disease in syrian hamsters. Science 276: 1119-1122.
    • (1997) Science , vol.276 , pp. 1119-1122
    • Tagliavini, F.1    McArthur, R.A.2    Canciani, B.3    Giaccone, G.4    Porro, M.5    Bugiani, M.6
  • 73
    • 0035928432 scopus 로고    scopus 로고
    • Tissue distribution of protease resistant prion protein in variant CJD using a highly sensitive immuno-blotting assay
    • Wadsworth JDF, Joiner S, Hill AF, Campbell TA, Desbruslais M, Luthert PJ, et al (2001). Tissue distribution of protease resistant prion protein in variant CJD using a highly sensitive immuno-blotting assay. Lancet 358: 171-180.
    • (2001) Lancet , vol.358 , pp. 171-180
    • Wadsworth, J.D.F.1    Joiner, S.2    Hill, A.F.3    Campbell, T.A.4    Desbruslais, M.5    Luthert, P.J.6
  • 74
    • 0025800143 scopus 로고
    • A 'unified theory' of prion propagation
    • Weissmann C (1991). A 'unified theory' of prion propagation. Nature 352: 679-683.
    • (1991) Nature , vol.352 , pp. 679-683
    • Weissmann, C.1


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