-
2
-
-
0020321767
-
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
-
3
-
-
3442889359
-
Synthetic mammalian prions
-
Legname G., Baskakov I.V., Nguyen H.O., Riesner D., Cohen F.E., DeArmond S.J., and Prusiner S.B. Synthetic mammalian prions. Science 305 (2004) 673-676
-
(2004)
Science
, vol.305
, pp. 673-676
-
-
Legname, G.1
Baskakov, I.V.2
Nguyen, H.O.3
Riesner, D.4
Cohen, F.E.5
DeArmond, S.J.6
Prusiner, S.B.7
-
4
-
-
17444413067
-
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
-
5
-
-
0027956109
-
Cell-free formation of protease-resistant prion protein
-
Kocisko D.A., Come J.H., Priola S.A., Chesebro B., Raymond G.J., Lansbury P.T., and Caughey B. Cell-free formation of protease-resistant prion protein. Nature 370 (1994) 471-474
-
(1994)
Nature
, vol.370
, pp. 471-474
-
-
Kocisko, D.A.1
Come, J.H.2
Priola, S.A.3
Chesebro, B.4
Raymond, G.J.5
Lansbury, P.T.6
Caughey, B.7
-
6
-
-
0035859102
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
|