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Volumn 84, Issue 4, 2003, Pages 1013-1020

In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BACTERIAL PROTEIN; CHLORPROMAZINE; CONGO RED; GUANIDINE; ISOPROTEIN; MEPACRINE; PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN;

EID: 0037385673     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.18903-0     Document Type: Review
Times cited : (63)

References (38)
  • 2
    • 0028997297 scopus 로고
    • Non-genetic propagation of strain-specific properties of scrapie prion protein
    • Bessen, R. A., Kocisko, D. A., Raymond, G. J., Marsh, R. F., Lansbury, P. T. & Caughey, B. (1995). Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375, 698-700.
    • (1995) Nature , vol.375 , pp. 698-700
    • Bessen, R.A.1    Kocisko, D.A.2    Raymond, G.J.3    Marsh, R.F.4    Lansbury, P.T.5    Caughey, B.6
  • 3
    • 0012856184 scopus 로고
    • The essential role of the intestinal flora in the toxification of orally-administered benzidine-based dyes: Internal exposure of rats to benzidine after intestinal azo reduction
    • (Abstract)
    • Boss, R. P., Koopman, J. P., Theuws, J. I. & Henderson, P. T. (1987). The essential role of the intestinal flora in the toxification of orally-administered benzidine-based dyes: internal exposure of rats to benzidine after intestinal azo reduction. Mut Res 181, 327 (Abstract).
    • (1987) Mut. Res. , vol.181 , pp. 327
    • Boss, R.P.1    Koopman, J.P.2    Theuws, J.I.3    Henderson, P.T.4
  • 4
    • 0031000201 scopus 로고    scopus 로고
    • Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms
    • Bossers, A., Belt, P. B. G. M., Raymond, G. J., Caughey, B., de Vries, R. & Smits, M. A. (1997). Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms. Proc Natl Acad Sci U S A 94, 4931-4936.
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 4931-4936
    • Bossers, A.1    Belt, P.B.G.M.2    Raymond, G.J.3    Caughey, B.4    de Vries, R.5    Smits, M.A.6
  • 5
    • 0033982338 scopus 로고    scopus 로고
    • Susceptibility of sheep for scrapie as assessed by in vitro conversion of nine naturally occurring variants of PrP
    • Bossers, A., de Vries, R. & Smits, M. A. (2000). Susceptibility of sheep for scrapie as assessed by in vitro conversion of nine naturally occurring variants of PrP. J Virol 74, 1407-1414.
    • (2000) J. Virol. , vol.74 , pp. 1407-1414
    • Bossers, A.1    de Vries, R.2    Smits, M.A.3
  • 6
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by Congo Red
    • Caughey, B. & Race, R. E. (1992). Potent inhibition of scrapie-associated PrP accumulation by Congo Red. J Neurochem 59, 768-771.
    • (1992) J. Neurochem. , vol.59 , pp. 768-771
    • Caughey, B.1    Race, R.E.2
  • 7
    • 0031080867 scopus 로고    scopus 로고
    • Prion protein and the transmissible spongiform encephalopathies
    • Caughey, B. & Chesebro, B. (1997). Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol 7, 56-62.
    • (1997) Trends Cell Biol. , vol.7 , pp. 56-62
    • Caughey, B.1    Chesebro, B.2
  • 8
    • 0027280172 scopus 로고
    • Congo red inhibition of scrapie agent replication
    • Caughey, B., Ernst, D. & Race, R. E. (1993). Congo red inhibition of scrapie agent replication. J Virol 67, 6270-6272.
    • (1993) J. Virol. , vol.67 , pp. 6270-6272
    • Caughey, B.1    Ernst, D.2    Race, R.E.3
  • 9
  • 10
  • 11
    • 0031797266 scopus 로고    scopus 로고
    • Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation
    • Demaimay, R., Harper, J., Gordon, H., Weaver, D., Chesebro, B. & Caughey, B. (1998). Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation. J Neurochem 71, 2534-2541.
    • (1998) J. Neurochem. , vol.71 , pp. 2534-2541
    • Demaimay, R.1    Harper, J.2    Gordon, H.3    Weaver, D.4    Chesebro, B.5    Caughey, B.6
  • 12
    • 28444498432 scopus 로고    scopus 로고
    • Inhibition of formation of protease-resistant prion protein by Trypan Blue, Sirius Red and other Congo Red analogs
    • Demaimay, R., Chesebro, B. & Caughey, B. (2000). Inhibition of formation of protease-resistant prion protein by Trypan Blue, Sirius Red and other Congo Red analogs. Arch Virol 16, 277-283.
    • (2000) Arch. Virol. , vol.16 , pp. 277-283
    • Demaimay, R.1    Chesebro, B.2    Caughey, B.3
  • 13
    • 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, 4894-4897.
    • (2000) J. Virol. , vol.74 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 14
    • 0032816362 scopus 로고    scopus 로고
    • Inhibitors of protease-resistant prion formation
    • Gilbert, I. H. & Rudyk, H. (1999). Inhibitors of protease-resistant prion formation. Int Antiviral News 7, 78-82.
    • (1999) Int. Antiviral News , vol.7 , pp. 78-82
    • Gilbert, I.H.1    Rudyk, H.2
  • 15
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith, J. S. (1967). Self-replication and scrapie. Nature 215, 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 16
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill, A. F., Antoniou, M. & Collinge, J. (1999). Protease-resistant prion protein produced in vitro lacks detectable infectivity. J Gen Virol 80, 11-14.
    • (1999) J. Gen. Virol. , vol.80 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge, J.3
  • 17
    • 0022802258 scopus 로고
    • The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP)
    • Hope, J., Morton, L. J. D., Farquhar, C. F., Multhaup, G., Beyreuther, K. & Kimberlin, R. H. (1986). The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO J 5, 2591-2597.
    • (1986) EMBO J. , vol.5 , pp. 2591-2597
    • Hope, J.1    Morton, L.J.D.2    Farquhar, C.F.3    Multhaup, G.4    Beyreuther, K.5    Kimberlin, R.H.6
  • 18
    • 0033564204 scopus 로고    scopus 로고
    • Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state
    • Horiuchi, M. & Caughey, B. (1999). Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state. EMBO J 18, 3193-3203.
    • (1999) EMBO J. , vol.18 , pp. 3193-3203
    • Horiuchi, M.1    Caughey, B.2
  • 19
    • 0034705020 scopus 로고    scopus 로고
    • Interactions between heterologous forms of prion protein: Binding, inhibition of conversion, and species barriers
    • Horiuchi, M., Priola, S. A., Chabry, J. & Caughey, B. (2000). Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers. Proc Natl Acad Sci U S A 97, 5836-5841.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 5836-5841
    • Horiuchi, M.1    Priola, S.A.2    Chabry, J.3    Caughey, B.4
  • 20
    • 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
  • 23
    • 0027195933 scopus 로고
    • Seeding 'one- dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T. & Lansbury, P. T., Jr (1993). Seeding 'one- dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 25
    • 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, D. A., Priola, S. A., Raymond, G. J., Chesebro, B., Lansbury, P. T., Jr & Caughey, B. (1995). 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 U S A 92, 3923-3927.
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    Lansbury P.T., Jr.5    Caughey, B.6
  • 26
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • Korth, C., May, B. C. H., Cohen, F. E. & Prusiner, S. B. (2001). Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc Natl Acad Sci U S A 98, 9836-9841.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.C.H.2    Cohen, F.E.3    Prusiner, S.B.4
  • 27
    • 0023001210 scopus 로고
    • Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent
    • Locht, C., Chesebro, B., Race, R. & Keith, J. M. (1986). Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Proc Natl Acad Sci U S A 83, 6372-6376.
    • (1986) Proc. Natl. Acad. Sci. U S A , vol.83 , pp. 6372-6376
    • Locht, C.1    Chesebro, B.2    Race, R.3    Keith, J.M.4
  • 31
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. (1991). Molecular biology of prion diseases. Science 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 33
    • 0030802361 scopus 로고    scopus 로고
    • Molecular assessment of the potential transmissibilities of BSE and scrapie to humans
    • & 12 other authors
    • Raymond, G. J., Hope, J., Kocisko, D. A. & 12 other authors (1997). Molecular assessment of the potential transmissibilities of BSE and scrapie to humans. Nature 388, 285-288.
    • (1997) Nature , vol.388 , pp. 285-288
    • Raymond, G.J.1    Hope, J.2    Kocisko, D.A.3
  • 35
    • 0033542142 scopus 로고    scopus 로고
    • Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone
    • Saborio, G. P., Soto, C., Kascsak, R. J., Levy, E., Kascsak, R., Harris, D. A. & Frangione, B. (1999). Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem Biophys Res Commun 258, 470-475.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 470-475
    • Saborio, G.P.1    Soto, C.2    Kascsak, R.J.3    Levy, E.4    Kascsak, R.5    Harris, D.A.6    Frangione, B.7
  • 37
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • & 7 other authors
    • Will, R. G., Ironside, J. W., Zeidler, M. & 7 other authors (1996). A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921-925.
    • (1996) Lancet , vol.347 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3


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