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Bradley, M.E.1
Liebman, S.W.2
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51
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3442889359
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Synthetic mammalian prions
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G. Legname, I.V. Baskakov, H.O. Nguyen, D. Riesner, F.E. Cohen, S.J. DeArmond, and S.B. Prusiner Synthetic mammalian prions Science 305 2004 673 676 This paper has demonstrated that in vitro generated amyloid fibres of the deletion derivative of PrP cause development of the neurological disease in the transgenic mice expressing the same deletion version of PrP. Moreover, brain extracts of sick mice were capable of infecting other mice with high levels of PrP production.
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(2004)
Science
, vol.305
, pp. 673-676
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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
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52
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4444312783
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+] prion in yeast and aggregation of Sup35 in vitro
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+] prion in yeast and aggregation of Sup35 in vitro Proc Natl Acad Sci USA 101 2004 12934 12939 This work shows that newly induced aggregates of the prion-forming protein Sup35 co-localize with pre-existing prion aggregates of another QN-rich protein, Rnq1, and that non-QN-rich aggregates do not facilitate Sup35 aggregation.
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(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 12934-12939
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Derkatch, I.L.1
Uptain, S.M.2
Outeiro, T.F.3
Krishnan, R.4
Lindquist, S.L.5
Liebman, S.W.6
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53
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3543022080
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Scrambled prion domains form prions and amyloid
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E.D. Ross, U. Baxa, and R.B. Wickner Scrambled prion domains form prions and amyloid Mol Cell Biol 24 2004 7206 7213 This work shows that five derivatives of the Ure2 PrD, generated by random shuffling of amino acids, retain prion-forming potential in vivo and amyloid-generating potential in vitro.
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(2004)
Mol Cell Biol
, vol.24
, pp. 7206-7213
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Ross, E.D.1
Baxa, U.2
Wickner, R.B.3
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