메뉴 건너뛰기




Volumn 584, Issue 11, 2010, Pages 2409-2414

Cellular factors implicated in prion replication

Author keywords

Conversion factor; Infectious protein; Prion; Protein misfolding cyclic amplification; Transmissible spongiform encephalopathy

Indexed keywords

PRION PROTEIN;

EID: 77952956256     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.04.040     Document Type: Article
Times cited : (50)

References (27)
  • 1
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J., Saá P., Hetz C., Soto C. In vitro generation of infectious scrapie prions. Cell 2005, 121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saá, P.2    Hetz, C.3    Soto, C.4
  • 4
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F., Wang X., Yuan C.-G., Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010, 327:1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.-G.3    Ma, J.4
  • 9
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio G.P., Permanne B., Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001, 411:810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 10
    • 33750442933 scopus 로고    scopus 로고
    • The intriguing prion disorders
    • Abid K., Soto C. The intriguing prion disorders. Cell Mol. Life Sci. 2006, 63:2342-2351.
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 2342-2351
    • Abid, K.1    Soto, C.2
  • 11
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F.E., DeArmond S.J., Prusiner S.B. 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
  • 14
    • 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. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 1999, 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
  • 15
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault N.R., Lucassen R.W., Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003, 425:717-720.
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 16
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • Deleault N.R., Geoghegan J.C., Nishina K., Kascsak R., Williamson R.A., Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J. Biol. Chem. 2005, 280:26873-26879.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 18
    • 33749632465 scopus 로고    scopus 로고
    • Protein misfolding cyclic amplification for diagnosis and prion propagation studies
    • Castilla J., Saa P., Morales R., Abid K., Maundrell K., Soto C. Protein misfolding cyclic amplification for diagnosis and prion propagation studies. Methods Enzymol. 2006, 412:3-21.
    • (2006) Methods Enzymol. , vol.412 , pp. 3-21
    • Castilla, J.1    Saa, P.2    Morales, R.3    Abid, K.4    Maundrell, K.5    Soto, C.6
  • 19
    • 22844434827 scopus 로고    scopus 로고
    • Cyclic amplification of protein misfolding and aggregation
    • Saa P., Castilla J., Soto C. Cyclic amplification of protein misfolding and aggregation. Methods Mol. Biol. 2005, 299:53-65.
    • (2005) Methods Mol. Biol. , vol.299 , pp. 53-65
    • Saa, P.1    Castilla, J.2    Soto, C.3
  • 20
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • Saa P., Castilla J., Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 2006, 281:35245-35252.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35245-35252
    • Saa, P.1    Castilla, J.2    Soto, C.3
  • 21
    • 0025165213 scopus 로고
    • Three hamster species with different scrapie incubation times and neuropathological features encode distinct prion proteins
    • Lowenstein D.H., Butler D.A., Westaway D., McKinley M.P., DeArmond S.J., Prusiner S.B. Three hamster species with different scrapie incubation times and neuropathological features encode distinct prion proteins. Mol. Cell Biol. 1990, 10:1153-1163.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1153-1163
    • Lowenstein, D.H.1    Butler, D.A.2    Westaway, D.3    McKinley, M.P.4    DeArmond, S.J.5    Prusiner, S.B.6
  • 22
    • 0037301367 scopus 로고    scopus 로고
    • Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
    • Vorberg I., Groschup M.H., Pfaff E., Priola S.A. Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J. Virol. 2003, 77:2003-2009.
    • (2003) J. Virol. , vol.77 , pp. 2003-2009
    • Vorberg, I.1    Groschup, M.H.2    Pfaff, E.3    Priola, S.A.4
  • 24
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N., Stein R., Yanai A., Friedlander G., Taraboulos A. Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 1997, 272:6324-6331.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 25
    • 0033301552 scopus 로고    scopus 로고
    • Cell biological studies of the prion protein
    • Harris D.A. Cell biological studies of the prion protein. Curr. Issues Mol. Biol. 1999, 1:65-75.
    • (1999) Curr. Issues Mol. Biol. , vol.1 , pp. 65-75
    • Harris, D.A.1
  • 26
    • 0035253848 scopus 로고    scopus 로고
    • Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein
    • Wong C., Xiong L.W., Horiuchi M., Raymond L., Wehrly K., Chesebro B., Caughey B. Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. EMBO J. 2001, 20:377-386.
    • (2001) EMBO J. , vol.20 , pp. 377-386
    • Wong, C.1    Xiong, L.W.2    Horiuchi, M.3    Raymond, L.4    Wehrly, K.5    Chesebro, B.6    Caughey, B.7
  • 27


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.