메뉴 건너뛰기




Volumn 158, Issue 10 I, 2002, Pages 998-1007

Prion diseases;Les maladies du prion

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; NUCLEIC ACID; PRION PROTEIN;

EID: 0036808246     PISSN: 00353787     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (2)

References (88)
  • 1
    • 0032934347 scopus 로고    scopus 로고
    • MS-8209, a water soluble amphotericin B derivative, affects both scrapie agent replication an PrPres accumulation in Syrian hamster scrapie
    • Adjou KT, Demaimay R, Deslys JP, et al., (1999). MS-8209, a water soluble amphotericin B derivative, affects both scrapie agent replication an PrPres accumulation in Syrian hamster scrapie. J Virol 80: 1079-85.
    • (1999) J Virol , vol.80 , pp. 1079-1085
    • Adjou, K.T.1    Demaimay, R.2    Deslys, J.P.3
  • 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: 764-66.
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 3
    • 0034044948 scopus 로고    scopus 로고
    • Opposite effects of dextran sulfate 500, the polyene antibiotic MS-8209, and Congo red on accumulation of the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent
    • Beringue V, Adjou K.T, Lamoury F, et al., (2000). Opposite effects of dextran sulfate 500, the polyene antibiotic MS-8209, and Congo red on accumulation of the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent. J Virol 74: 5432-40.
    • (2000) J Virol , vol.74 , pp. 5432-5440
    • Beringue, V.1    Adjou, K.T.2    Lamoury, F.3
  • 4
    • 0032950566 scopus 로고    scopus 로고
    • Maladie de Creutzfeldt-Jakob: Valeur diagnostique de la detection de la protéine 14-3-3 et du dosage de la NSE dans le liquide céphalo-rachidien
    • Brandel JP, Beaudry P, Delasnerie-Laupretre N, Laplanche JL. (1999). Maladie de Creutzfeldt-Jakob: Valeur diagnostique de la detection de la protéine 14-3-3 et du dosage de la NSE dans le liquide céphalo-rachidien. Rev Neurol 55: 148-51.
    • (1999) Rev Neurol , vol.55 , pp. 148-151
    • Brandel, J.P.1    Beaudry, P.2    Delasnerie-Laupretre, N.3    Laplanche, J.L.4
  • 5
    • 0022973492 scopus 로고
    • Clinical analysis of a consecutive series of 230 neuropathologically verified cases
    • Brown P, Cathala F, Castaigne P, Gajdusek C. (1986). Clinical analysis of a consecutive series of 230 neuropathologically verified cases. Ann Neurol 20: 597-602.
    • (1986) Ann Neurol , vol.20 , pp. 597-602
    • Brown, P.1    Cathala, F.2    Castaigne, P.3    Gajdusek, C.4
  • 6
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell surface PrP
    • Bueler H, Fischer M, Lang Y, et al., (1992). Normal development and behaviour of mice lacking the neuronal cell surface PrP. Nature 256: 577-582.
    • (1992) Nature , vol.256 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3
  • 7
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H, Aguzzi A, Sailer A, et al., (1993). Mice devoid of PrP are resistant to scrapie. Cell 7: 1339-47.
    • (1993) Cell , vol.7 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 8
    • 0035849483 scopus 로고    scopus 로고
    • CSF detection of the 14-3-3 in unselected patients with dementia
    • Burkhard PR, Sanchez JC, Landis T, Hochstrasser DF. (2001). CSF detection of the 14-3-3 in unselected patients with dementia. Neurology 56: 1528-33.
    • (2001) Neurology , vol.56 , pp. 1528-1533
    • Burkhard, P.R.1    Sanchez, J.C.2    Landis, T.3    Hochstrasser, D.F.4
  • 10
    • 0027535855 scopus 로고
    • Sulfated polyanion inhibition of scrapie-associated Prp accumulation in cultured cells
    • Caughey B, Raymond GJ. (1993). Sulfated polyanion inhibition of scrapie-associated Prp accumulation in cultured cells. J Virol 67: 643-50.
    • (1993) J Virol , vol.67 , pp. 643-650
    • Caughey, B.1    Raymond, G.J.2
  • 11
    • 0032514682 scopus 로고    scopus 로고
    • Inhibition of protease-resistant prion protein formation by porphyrins and phtalocyanines
    • Caughey WS, Raymond LD, Horiuchi M, Caughey B. (1998). Inhibition of protease-resistant prion protein formation by porphyrins and phtalocyanines. Proc Natl Acad Sci USA 95: 12117-22.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12117-12122
    • Caughey, W.S.1    Raymond, L.D.2    Horiuchi, M.3    Caughey, B.4
  • 12
    • 0027997387 scopus 로고
    • Prion protein is necessary for normal synaptic function
    • Collinge J, Whittington MA, Sidle KC, et al., (1994). Prion protein is necessary for normal synaptic function. Nature 370: 295-97.
    • (1994) Nature , vol.370 , pp. 295-297
    • Collinge, J.1    Whittington, M.A.2    Sidle, K.C.3
  • 13
    • 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 383 685-90.
    • (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
  • 14
  • 15
    • 0028015941 scopus 로고
    • Pharmacological studies of a new derivative of amphotericin B, MS-8209, in mouse and hamster scrapie
    • Demaimay R, Adjou K, Lasmezas C et al., (1994). Pharmacological studies of a new derivative of amphotericin B, MS-8209, in mouse and hamster scrapie. J Gen Virol 75:2499-2503.
    • (1994) J Gen Virol , vol.75 , pp. 2499-2503
    • Demaimay, R.1    Adjou, K.2    Lasmezas, C.3
  • 16
    • 0033787391 scopus 로고    scopus 로고
    • Ribozyme structures and mechanisms
    • Doherty EA, Doudna JA. (2000). Ribozyme structures and mechanisms. Annu Rev Biochem 69: 597-615.
    • (2000) Annu Rev Biochem , vol.69 , pp. 597-615
    • Doherty, E.A.1    Doudna, J.A.2
  • 17
    • 0024473899 scopus 로고
    • Pro-leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome
    • Doh-Ura K, Tateishi J, Sasaki H, Kitamoto T, Sakaki Y. (1989). Pro-leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome. Biochem Biophys Research Commun 163: 974-9.
    • (1989) Biochem Biophys Research Commun , vol.163 , pp. 974-979
    • Doh-Ura, K.1    Tateishi, J.2    Sasaki, H.3    Kitamoto, T.4    Sakaki, Y.5
  • 18
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • Doh-Ura K, Iwaki T, Caughey B. (2000). Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J Virol 74: 4894-7.
    • (2000) J Virol , vol.74 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 19
    • 0021282464 scopus 로고
    • Dextran sulphate 500delays and prevents mouse scrapie by impairment of agent replication in spleen
    • Ehlers B, Diringer H. (1984). Dextran sulphate 500delays and prevents mouse scrapie by impairment of agent replication in spleen. J Gen Virol 65: 1325-30.
    • (1984) J Gen Virol , vol.65 , pp. 1325-1330
    • Ehlers, B.1    Diringer, H.2
  • 20
    • 0035979274 scopus 로고    scopus 로고
    • Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody
    • Enari M, Flechsig E, Weissmann C. (2001). Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proced. Natl Acad Sci 98: 9295-9.
    • (2001) Proced Natl Acad Sci , vol.98 , pp. 9295-9299
    • Enari, M.1    Flechsig, E.2    Weissmann, C.3
  • 21
    • 0012950643 scopus 로고    scopus 로고
    • Antisense as a neuroscience tool and therapeutic agent
    • Estibeiro P, Godfray J. (2001). Antisense as a neuroscience tool and therapeutic agent. TINS 24: 56-62.
    • (2001) TINS , vol.24 , pp. 56-62
    • Estibeiro, P.1    Godfray, J.2
  • 22
    • 0033537348 scopus 로고    scopus 로고
    • Prophylactic potential of pentosan polysulphate in transmissible spongoform encephalopathies
    • Farquhar C, Dickinson A, Bruce M. (1999). Prophylactic potential of pentosan polysulphate in transmissible spongoform encephalopathies. Lancet 353: 117-8.
    • (1999) Lancet , vol.353 , pp. 117-118
    • Farquhar, C.1    Dickinson, A.2    Bruce, M.3
  • 23
    • 0027483615 scopus 로고
    • Neurotoxicity of a prion protein fragment
    • Forloni G, Angeretti N, Chiesa R et al., (1993). Neurotoxicity of a prion protein fragment. Nature 362: 543-546.
    • (1993) Nature , vol.362 , pp. 543-546
    • Forloni, G.1    Angeretti, N.2    Chiesa, R.3
  • 24
    • 0023788957 scopus 로고
    • Creutzfeldt-Jakob disease: Correlation of MRI and neuropathologic findings
    • Gertz H.J, Henkes H, Cervos-Navarro J. (1988). Creutzfeldt-Jakob disease: Correlation of MRI and neuropathologic findings. Neurology 38: 1481-2.
    • (1988) Neurology , vol.38 , pp. 1481-1482
    • Gertz, H.J.1    Henkes, H.2    Cervos-Navarro, J.3
  • 25
    • 0026496257 scopus 로고
    • Fatal familial insomnia and familial Creutzfeld - Jakob disease: Disease phenotype determined by a DNA polymorphism
    • Goldfarb L.G, Petersen R.B, Taraton M, et al., (1992). Fatal familial insomnia and familial Creutzfeld - Jakob disease: Disease phenotype determined by a DNA polymorphism. Science 258: 806-8.
    • (1992) Science , vol.258 , pp. 806-808
    • Goldfarb, L.G.1    Petersen, R.B.2    Taraton, M.3
  • 26
    • 0014190760 scopus 로고
    • Self-repmication and scrapie
    • Griffith JS. (1967). Self-repmication and scrapie. Nature 215: 1043-4.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 27
    • 0034883360 scopus 로고    scopus 로고
    • Early behavioural changes in scrapie-affected mice and the influence of dapsone
    • Guenther K, Deacon RM, Perry VH, Rawlins JN. (2001). Early behavioural changes in scrapie-affected mice and the influence of dapsone. Eur J Neurosc. 14: 401-9.
    • (2001) Eur J Neurosc , vol.14 , pp. 401-409
    • Guenther, K.1    Deacon, R.M.2    Perry, V.H.3    Rawlins, J.N.4
  • 28
    • 0022606619 scopus 로고
    • Abnormal protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies
    • Harrington MG, Merril CR, Asher DM, Gajdusek DC, (1986). Abnormal protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N Eng J Med 315: 279-83.
    • (1986) N Eng J Med , vol.315 , pp. 279-283
    • Harrington, M.G.1    Merril, C.R.2    Asher, D.M.3    Gajdusek, D.C.4
  • 29
    • 0035812752 scopus 로고    scopus 로고
    • Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies
    • Heppner FL, Musahl C, Arrighy I et al., (2001). Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science, 294: 178-82.
    • (2001) Science , vol.294 , pp. 178-182
    • Heppner, F.L.1    Musahl, C.2    Arrighy, I.3
  • 31
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome
    • Hsiao KK, Baker HF, Crow TJ et al., (1989). Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 338: 342-5.
    • (1989) Nature , vol.338 , pp. 342-345
    • Hsiao, K.K.1    Baker, H.F.2    Crow, T.J.3
  • 33
    • 0029840653 scopus 로고    scopus 로고
    • The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies
    • Hsich G, Kenney K, Gibbs CJ, Lee KH, Harringtom MG. (1996). The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N Engl J Med 335: 924-30.
    • (1996) N Engl J Med , vol.335 , pp. 924-930
    • Hsich, G.1    Kenney, K.2    Gibbs, C.J.3    Lee, K.H.4    Harringtom, M.G.5
  • 34
    • 0035988619 scopus 로고    scopus 로고
    • Molecular diagnostics of transmissible spongiform encephalopathies
    • Ingrosso L, Vetrugno V, Cardone F, Pocchiari M. (2002). Molecular diagnostics of transmissible spongiform encephalopathies. Trends Mol Med 8: 273-80.
    • (2002) Trends Mol Med , vol.8 , pp. 273-280
    • Ingrosso, L.1    Vetrugno, V.2    Cardone, F.3    Pocchiari, M.4
  • 35
    • 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: 506-8.
    • (1995) J Virol , vol.69 , pp. 506-508
    • Ingrosso, L.1    Ladogana, A.2    Pocchiari, M.3
  • 36
    • 0035662673 scopus 로고    scopus 로고
    • The molecular pathology of CJD: Old and new variants
    • Jackson G.S, Collinge J. (2001). The molecular pathology of CJD: Old and new variants. J Clin Pathol: Mol Pathol 54: 393-9.
    • (2001) J Clin Pathol: Mol Pathol , vol.54 , pp. 393-399
    • Jackson, G.S.1    Collinge, J.2
  • 37
    • 0033849497 scopus 로고    scopus 로고
    • An enzyme-linked immunosorbent assay to quantify 14-3-3 proteins in the cerebrospinal fluid of suspected Creutzfeldt-Jakob disease patients
    • Kenney K, Brechtel C, Takahashi H, Kurohara K, Anderson P, Gibbs CJ. (2000). An enzyme-linked immunosorbent assay to quantify 14-3-3 proteins in the cerebrospinal fluid of suspected Creutzfeldt-Jakob disease patients. Ann Neurol 48: 395-8.
    • (2000) Ann Neurol , vol.48 , pp. 395-398
    • Kenney, K.1    Brechtel, C.2    Takahashi, H.3    Kurohara, K.4    Anderson, P.5    Gibbs, C.J.6
  • 38
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • Korth C, May BCH, Cohen FE, Prusiner SB. (2001). Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc Natl Acad Sci, 98: 9836-41.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.C.H.2    Cohen, F.E.3    Prusiner, S.B.4
  • 39
    • 0033964470 scopus 로고    scopus 로고
    • Effect of amphotericin B on wild-type and mutated prion proteins in cultured cells: Putative mechanism of action in transmissible spongiform encephalopathies
    • Mange A, Milhavet O, McMahon HEM, Casanova D, Lehmann S. (1999). Effect of amphotericin B on wild-type and mutated prion proteins in cultured cells: Putative mechanism of action in transmissible spongiform encephalopathies. J Neurochem 74: 754-62.
    • (1999) J Neurochem , vol.74 , pp. 754-762
    • Mange, A.1    Milhavet, O.2    McMahon, H.E.M.3    Casanova, D.4    Lehmann, S.5
  • 40
    • 0032497163 scopus 로고    scopus 로고
    • Dapsone to delay symptoms in Creutzfeldt-Jakob disease
    • Manuelidis L, Fritch W, Zaitsev I. (1998). Dapsone to delay symptoms in Creutzfeldt-Jakob disease. Lancet, 352: 456.
    • (1998) Lancet , vol.352 , pp. 456
    • Manuelidis, L.1    Fritch, W.2    Zaitsev, I.3
  • 41
    • 0026719975 scopus 로고
    • Failure to ameliorate Creutzfeldt-Jakob disease with amphotericin B therapy
    • Massulo C, Macchi G, Xi YG, Pochiari M. (1992). Failure to ameliorate Creutzfeldt-Jakob disease with amphotericin B therapy. J Infect Dis 165: 784-5.
    • (1992) J Infect Dis , vol.165 , pp. 784-785
    • Massulo, C.1    Macchi, G.2    Xi, Y.G.3    Pochiari, M.4
  • 42
    • 0028914019 scopus 로고
    • Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: Inhibition of amyloidogenesis
    • Merlini G, Ascari E, Amboldi N, et al., (1995). Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: Inhibition of amyloidogenesis. Proc Natl Acad Sci 92: 2959-63.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 2959-2963
    • Merlini, G.1    Ascari, E.2    Amboldi, N.3
  • 43
    • 0033961817 scopus 로고    scopus 로고
    • Effect of Congo red on wild-type and mutated prion proteins in cultured cells
    • Milhavet O, Mange A, Casanova D, Lehmann S. (2000). Effect of Congo red on wild-type and mutated prion proteins in cultured cells. J Neurochem 74: 1-9.
    • (2000) J Neurochem , vol.74 , pp. 1-9
    • Milhavet, O.1    Mange, A.2    Casanova, D.3    Lehmann, S.4
  • 44
    • 0036142960 scopus 로고    scopus 로고
    • Correlation of diffusion-weighted magnetic resonance imaging with neuropathology in Creutzfeldt-Jakob disease
    • Mittal S, Farmer P, Kalina P, Kingsley P, Halperin J. (2002). Correlation of diffusion-weighted magnetic resonance imaging with neuropathology in Creutzfeldt-Jakob disease. Arch Neurol 59: 128-4.
    • (2002) Arch Neurol , vol.59 , pp. 128-134
    • Mittal, S.1    Farmer, P.2    Kalina, P.3    Kingsley, P.4    Halperin, J.5
  • 45
    • 7144253795 scopus 로고    scopus 로고
    • Clinical features of fatal familial insomnia: Phenotypic variability in relation to a polymorphism at codon 129 of the prion protein gene
    • Montagna P, Cortelli P, Avoni P et al., (1998). Clinical features of fatal familial insomnia: Phenotypic variability in relation to a polymorphism at codon 129 of the prion protein gene. Brain Pathol 8: 515-20.
    • (1998) Brain Pathol , vol.8 , pp. 515-520
    • Montagna, P.1    Cortelli, P.2    Avoni, P.3
  • 46
    • 0033215478 scopus 로고    scopus 로고
    • Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel
    • Moore R, Lee IY, Silvermann GL et al., (1999). Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol 292: 797-817.
    • (1999) J Mol Biol , vol.292 , pp. 797-817
    • Moore, R.1    Lee, I.Y.2    Silvermann, G.L.3
  • 47
    • 0035909931 scopus 로고    scopus 로고
    • Doppel-induced cerebellar degeneration in transgenic mice
    • Moore RC, Mastrangelo P, Bouzamondo E et al., (2001). Doppel-induced cerebellar degeneration in transgenic mice. Proc Natl Acad Sci 98: 15288-93.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 15288-15293
    • Moore, R.C.1    Mastrangelo, P.2    Bouzamondo, E.3
  • 48
    • 0035899460 scopus 로고    scopus 로고
    • A route for prion neuroinvasion
    • Nicotera P. (2001). A route for prion neuroinvasion. Neuron 31: 345-8.
    • (2001) Neuron , vol.31 , pp. 345-348
    • Nicotera, P.1
  • 49
    • 6844255891 scopus 로고    scopus 로고
    • Diagnosis of Creutzfeldt-Jakob disease by measurement of S100 protein in serum: Prospective case-control strudy
    • Otto M, Wiltfang J, Schutz E et al., (1998). Diagnosis of Creutzfeldt-Jakob disease by measurement of S100 protein in serum: Prospective case-control strudy. BMJ 316: 577-82.
    • (1998) BMJ , vol.316 , pp. 577-582
    • Otto, M.1    Wiltfang, J.2    Schutz, E.3
  • 50
    • 0037154135 scopus 로고    scopus 로고
    • Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeldt-Jakob disease
    • Otto M, Wiltfang J, Cepek L et al., (2002). Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeldt-Jakob disease. Neurology 58: 192-7.
    • (2002) Neurology , vol.58 , pp. 192-197
    • Otto, M.1    Wiltfang, J.2    Cepek, L.3
  • 51
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer MS, Dryden AJ, Hughes JT, Collinge J. (1991). Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352: 340-42.
    • (1991) Nature , vol.352 , pp. 340-342
    • Palmer, M.S.1    Dryden, A.J.2    Hughes, J.T.3    Collinge, J.4
  • 52
    • 0027332116 scopus 로고
    • Conversion of αhelices into β-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J et al., (1993). Conversion of αhelices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90: 10962-6.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3
  • 53
    • 8944259890 scopus 로고    scopus 로고
    • Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease
    • Parchi P, Castellani R, Capellari S et al., (1996). Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann Neurol 39: 767-78.
    • (1996) Ann Neurol , vol.39 , pp. 767-778
    • Parchi, P.1    Castellani, R.2    Capellari, S.3
  • 54
    • 12944253111 scopus 로고    scopus 로고
    • Genetic influence on the structural variations of the abnormal prion protein
    • Parchi P, Zou W, Wang W et al., (2000). Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci 97: 10168-72.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 10168-10172
    • Parchi, P.1    Zou, W.2    Wang, W.3
  • 55
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Pepys M.B, Herbert J, Hutchinson WL, et al., (2002). Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature, 417: 254-9.
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1    Herbert, J.2    Hutchinson, W.L.3
  • 56
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D, Williamson AR, Kaneko, et al., (2001). Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412: 739-43.
    • (2001) Nature , vol.412 , pp. 739-743
    • Peretz, D.1    Williamson, A.R.2    Kaneko3
  • 57
    • 0034705043 scopus 로고    scopus 로고
    • Mimicking dominant negative inhibition of prion replication through structure-based drug design
    • Perrier V, Wallace A.C, Kaneko K, Safar J, Prusiner SB, Cohen FE. (2000). Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc Natl Acad Sci 97: 6073-8.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 6073-6078
    • Perrier, V.1    Wallace, A.C.2    Kaneko, K.3    Safar, J.4    Prusiner, S.B.5    Cohen, F.E.6
  • 58
    • 0023243085 scopus 로고
    • AmphotericinB delays the incubation period of scrapie in intracerebrally inoculated hamsters
    • Pocchiari M, Schmittinger S, Masullo C. (1987). AmphotericinB delays the incubation period of scrapie in intracerebrally inoculated hamsters. J Gen Virol 8: 219-23.
    • (1987) J Gen Virol , vol.8 , pp. 219-223
    • Pocchiari, M.1    Schmittinger, S.2    Masullo, C.3
  • 59
    • 0037154263 scopus 로고    scopus 로고
    • Lymph nodal prion replication and neuroinvasion in mice devoid of follicular dendritic cells
    • Prinz M, Montrasio F, Klein MA, et al., (2002). Lymph nodal prion replication and neuroinvasion in mice devoid of follicular dendritic cells. Proc Natl Acad Sci 99: 919-24.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 919-924
    • Prinz, M.1    Montrasio, F.2    Klein, M.A.3
  • 60
    • 0032829347 scopus 로고    scopus 로고
    • Novel therapeutic uses for porphyrins and phthalocyanines in the transmissible spongiform encephalopathies
    • Priola SA, Caughey B, Caughey WS. (1999). Novel therapeutic uses for porphyrins and phthalocyanines in the transmissible spongiform encephalopathies. Current Opinion in Microbiology 2: 563-6.
    • (1999) Current Opinion in Microbiology , vol.2 , pp. 563-566
    • Priola, S.A.1    Caughey, B.2    Caughey, W.S.3
  • 62
    • 0020321767 scopus 로고
    • Novel proteinaceous infectous particles cause scrapie
    • Prusiner SB. (1982). Novel proteinaceous infectous particles cause scrapie. Science 216: 136-44.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 65
    • 0035943651 scopus 로고    scopus 로고
    • A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases
    • Shaked GM, Shaked Y, Kariv-Inbal Z, Halimi M, Avraham I, Gabizon R. (2001). A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J Biol Chem. 276: 31479-82.
    • (2001) J Biol Chem , vol.276 , pp. 31479-31482
    • Shaked, G.M.1    Shaked, Y.2    Kariv-Inbal, Z.3    Halimi, M.4    Avraham, I.5    Gabizon, R.6
  • 66
    • 0036317750 scopus 로고    scopus 로고
    • Immunization delays the onset of prion disease in mice
    • Sigurdsson EM, Brown DR, Daniels M, et al., (2002). Immunization delays the onset of prion disease in mice. Am J Pathol 161: 13-7.
    • (2002) Am J Pathol , vol.161 , pp. 13-17
    • Sigurdsson, E.M.1    Brown, D.R.2    Daniels, M.3
  • 67
    • 0034837694 scopus 로고    scopus 로고
    • Value of fluid-attenuated inversion recovery MR imaging in an unusual case of sporadic Creutzfeldt-Jakob disease
    • Smart JM, Wood A. (2001). Value of fluid-attenuated inversion recovery MR imaging in an unusual case of sporadic Creutzfeldt-Jakob disease. Am J Roentgenol 177: 948-9.
    • (2001) Am J Roentgenol , vol.177 , pp. 948-949
    • Smart, J.M.1    Wood, A.2
  • 68
    • 0035090680 scopus 로고    scopus 로고
    • Prions: Disease propagation and disease therapy by conformational transmission
    • Soto C, Saborio GP. (2001). Prions: Disease propagation and disease therapy by conformational transmission. Trends Mol Med 7: 10914.
    • (2001) Trends Mol Med , vol.7 , pp. 10914
    • Soto, C.1    Saborio, G.P.2
  • 69
    • 0034650634 scopus 로고    scopus 로고
    • Reversion of prion protein conformational changes by synthetic β-shett breaker peptides
    • Soto C, Kasczak R.J, Saborio GP, et al., (2000). Reversion of prion protein conformational changes by synthetic β-shett breaker peptides. Lancet 355: 192-7.
    • (2000) Lancet , vol.355 , pp. 192-197
    • Soto, C.1    Kasczak, R.J.2    Saborio, G.P.3
  • 70
    • 0030056269 scopus 로고    scopus 로고
    • Accuracy and reliability of periodic sharp wave complexes in Creutzfeldt-Jakob disease
    • Steinhoff BJ, Racker S, Herrendorf G, et al., (1996). Accuracy and reliability of periodic sharp wave complexes in Creutzfeldt-Jakob disease. Arch Neurol 53: 162-6.
    • (1996) Arch Neurol , vol.53 , pp. 162-166
    • Steinhoff, B.J.1    Racker, S.2    Herrendorf, G.3
  • 72
    • 0037091006 scopus 로고    scopus 로고
    • Pharmacological approaches to prion research
    • Supattapone S, Nishina K, Rees JR. (2002). Pharmacological approaches to prion research. Bioch Pharmacol 63: 1383-88.
    • (2002) Bioch Pharmacol , vol.63 , pp. 1383-1388
    • Supattapone, S.1    Nishina, K.2    Rees, J.R.3
  • 73
    • 17344382240 scopus 로고    scopus 로고
    • Effectiveness of antrhracycline against experimental prion disease in syrian hamster
    • Tagliavini F, McArthur RA, Canciani B, et al., (1997). Effectiveness of antrhracycline against experimental prion disease in syrian hamster. Science 276: 1119-22.
    • (1997) Science , vol.276 , pp. 1119-1122
    • Tagliavini, F.1    McArthur, R.A.2    Canciani, B.3
  • 74
    • 0031991757 scopus 로고    scopus 로고
    • Gerstmann-Straüssler-Scheinker syndrome
    • Tranchant C, Warter JM. (1998). Gerstmann-Straüssler-Scheinker syndrome. Rev Neurol 2: 152-7.
    • (1998) Rev Neurol , vol.2 , pp. 152-157
    • Tranchant, C.1    Warter, J.M.2
  • 76
    • 0036298656 scopus 로고    scopus 로고
    • Phosphorylated tau in cerebrospinal fluid as a marker for Creutzfeldt-Jakob disease
    • Van Everbroeck B, Green AJE, Vanmechelen E, et al., (2002). Phosphorylated tau in cerebrospinal fluid as a marker for Creutzfeldt-Jakob disease. J Neurol Neurosurg 73: 79-82.
    • (2002) J Neurol Neurosurg , vol.73 , pp. 79-82
    • Van Everbroeck, B.1    Green, A.J.E.2    Vanmechelen, E.3
  • 78
    • 0041406097 scopus 로고    scopus 로고
    • Les maladies humaines familiales à prion
    • Warter JM. (2001). Les maladies humaines familiales à prion. Bull Acad Natle Méd 185: 405-15.
    • (2001) Bull Acad Natle Méd , vol.185 , pp. 405-415
    • Warter, J.M.1
  • 79
    • 0033615415 scopus 로고    scopus 로고
    • PrP's double causes trouble
    • Weissmann C, Aguzzi A. (1999). PrP's double causes trouble. Science 286: 914-5.
    • (1999) Science , vol.286 , pp. 914-915
    • Weissmann, C.1    Aguzzi, A.2
  • 80
    • 0023669586 scopus 로고
    • A novel progressive spongiform encephalopathy in cattle
    • Wells GAH, Scott AC, Johnson CT, et al., (1987). A novel progressive spongiform encephalopathy in cattle. Vet Rec 121: 419-20.
    • (1987) Vet Rec , vol.121 , pp. 419-420
    • Wells, G.A.H.1    Scott, A.C.2    Johnson, C.T.3
  • 81
    • 0042422345 scopus 로고    scopus 로고
    • Diagnosis of new variant Creutzfeldt-Jakob disease
    • Will RG, Zeidler M, Stewart GE. (2000). Diagnosis of new variant Creutzfeldt-Jakob disease. Ann. Neuro 147: 575-82.
    • (2000) Ann Neuro , vol.147 , pp. 575-582
    • Will, R.G.1    Zeidler, M.2    Stewart, G.E.3
  • 82
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • Will RG, Ironside JW, Zeidler M, et al., (1996). A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347: 921-5.
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 83
    • 0035253848 scopus 로고    scopus 로고
    • Sulfated glycans and elevated temperature stimulate PrPsc-dependent cell-free formation of protease-resistant prion protein
    • Wong C, Xiong LW, Horiuchi M, et al., (2001). Sulfated glycans and elevated temperature stimulate PrPsc-dependent cell-free formation of protease-resistant prion protein. The EMBO Journal 20: 377-86.
    • (2001) The EMBO Journal , vol.20 , pp. 377-386
    • Wong, C.1    Xiong, L.W.2    Horiuchi, M.3
  • 84
    • 0026600866 scopus 로고
    • Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation
    • Xi YG, Ingrosso L, Ladogana A, Masullo C, Pocchiari M. 1992). Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation. Nature 356: 598-601.
    • (1992) Nature , vol.356 , pp. 598-601
    • Xi, Y.G.1    Ingrosso, L.2    Ladogana, A.3    Masullo, C.4    Pocchiari, M.5
  • 85
    • 0034718472 scopus 로고    scopus 로고
    • Analysis of EEG and CSF 14-3-3 proteins as aids to the diagnostic of Creutzfeldt-Jakob disease
    • Zerr I, Pocchiari M, Collins S, et al., (2000). Analysis of EEG and CSF 14-3-3 proteins as aids to the diagnostic of Creutzfeldt-Jakob disease. Neurology 55: 811-5.
    • (2000) Neurology , vol.55 , pp. 811-815
    • Zerr, I.1    Pocchiari, M.2    Collins, S.3
  • 86
    • 0029078348 scopus 로고
    • Cerebrospinal fluid concentration of neuron specific endolase in diagnostic of Creutzfeldt-Jakob disease
    • Zerr I, Bodemer M, Räcker S, et al., (1995). Cerebrospinal fluid concentration of neuron specific endolase in diagnostic of Creutzfeldt-Jakob disease. Lancet 345: 1609-10.
    • (1995) Lancet , vol.345 , pp. 1609-1610
    • Zerr, I.1    Bodemer, M.2    Räcker, S.3
  • 87
    • 0033999341 scopus 로고    scopus 로고
    • Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein
    • Zuljanello L, Kaneko K, Scott M, et al., (2000). Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J Virol 74: 4351-60 replicate without nucleic acid? Nature 214: 764-6.
    • (2000) J Virol , vol.74 , pp. 4351-4360
    • Zuljanello, L.1    Kaneko, K.2    Scott, M.3
  • 88
    • 0011341005 scopus 로고    scopus 로고
    • Replicate without nucleic acid?
    • Zuljanello L, Kaneko K, Scott M, et al., (2000). Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J Virol 74: 4351-60 replicate without nucleic acid? Nature 214: 764-6.
    • Nature , vol.214 , pp. 764-766


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.