메뉴 건너뛰기




Volumn 580, Issue 17, 2006, Pages 4231-4235

In vitro self-propagation of recombinant PrPSc-like conformation generated in the yeast cytoplasm

Author keywords

Cytoplasm; Prion; Protein misfolding; Transmissible spongiform encephalopathies

Indexed keywords

AMYLOID; PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN;

EID: 33745857629     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.06.074     Document Type: Article
Times cited : (10)

References (17)
  • 2
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 4
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J., Saa P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 6
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 7
    • 0037446508 scopus 로고    scopus 로고
    • In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups
    • Lucassen R., Nishina K., and Supattapone S. In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups. Biochemistry 42 (2003) 4127-4135
    • (2003) Biochemistry , vol.42 , pp. 4127-4135
    • Lucassen, R.1    Nishina, K.2    Supattapone, S.3
  • 8
    • 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., and Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J. Biol. Chem. 280 (2005) 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
  • 9
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault N.R., Lucassen R.W., and Supattapone S. RNA molecules stimulate prion protein conversion. Nature 425 (2003) 717-720
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 10
    • 0033203242 scopus 로고    scopus 로고
    • Sc-like conformation in living cells
    • Sc-like conformation in living cells. Nat. Cell. Biol. 1 (1999) 358-361
    • (1999) Nat. Cell. Biol. , vol.1 , pp. 358-361
    • Ma, J.1    Lindquist, S.2
  • 12
    • 0026751734 scopus 로고
    • Genes required for vacuolar acidity in Saccharomyces cerevisiae
    • Preston R.A., Reinagel P.S., and Jones E.W. Genes required for vacuolar acidity in Saccharomyces cerevisiae. Genetics 131 (1992) 551-558
    • (1992) Genetics , vol.131 , pp. 551-558
    • Preston, R.A.1    Reinagel, P.S.2    Jones, E.W.3
  • 13
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • Ross E.D., Baxa U., and Wickner R.B. Scrambled prion domains form prions and amyloid. Mol. Cell. Biol. 24 (2004) 7206-7213
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 14
    • 33144469836 scopus 로고    scopus 로고
    • Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res
    • Baron G.S., Magalhaes A.C., Prado M.A., and Caughey B. Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res. J. Virol. 80 (2006) 2106-2117
    • (2006) J. Virol. , vol.80 , pp. 2106-2117
    • Baron, G.S.1    Magalhaes, A.C.2    Prado, M.A.3    Caughey, B.4
  • 15
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma J., and Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. USA 98 (2001) 14955-14960
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 16
    • 0037195617 scopus 로고    scopus 로고
    • Sc-like conformation in the cytosol
    • Sc-like conformation in the cytosol. Science 298 (2002) 1785-1788
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 17
    • 12844249401 scopus 로고    scopus 로고
    • Calpain and other cytosolic proteases can contribute to the degradation of retro-translocated prion protein in the cytosol
    • Wang X., Wang F., Sy M.S., and Ma J. Calpain and other cytosolic proteases can contribute to the degradation of retro-translocated prion protein in the cytosol. J. Biol. Chem. 280 (2005) 317-325
    • (2005) J. Biol. Chem. , vol.280 , pp. 317-325
    • Wang, X.1    Wang, F.2    Sy, M.S.3    Ma, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.