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Reports that maintenance of the prion state depends on the interplay of two different chaperones. This represents a significant step towards identifying intermolecular interactions that are critical for maintenance.
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Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol Cell Biol. 19:1999;1325-1333. Reports that maintenance of the prion state depends on the interplay of two different chaperones. This represents a significant step towards identifying intermolecular interactions that are critical for maintenance.
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(1999)
Mol Cell Biol
, vol.19
, pp. 1325-1333
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Newnam, G.P.1
Wegrzyn, R.D.2
Lindquist, S.L.3
Chernoff, Y.O.4
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51
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0033118934
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Translation termination efficiency can be regulated in saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
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Explores the interrelation of prion state and stress tolerance for [PSI+]. The authors favour models based on alterations in translation termination efficiency and subsequent effects on the stress response. Provides an important additional perspective on the prion phenotype.
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Eaglestone SS, Cox BS, Tuite MF Translation termination efficiency can be regulated in saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J. 18:1999;1974-1981. Explores the interrelation of prion state and stress tolerance for [PSI+]. The authors favour models based on alterations in translation termination efficiency and subsequent effects on the stress response. Provides an important additional perspective on the prion phenotype.
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(1999)
EMBO J
, vol.18
, pp. 1974-1981
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Eaglestone, S.S.1
Cox, B.S.2
Tuite, M.F.3
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52
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0033605278
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Prion domain initiation of amyloid formation in vitro from native Ure2p
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Demonstrates that Ure2p prion domain can polymerise to amyloid filaments and recruit native Ure2p. Filaments are congophilic and have high β-sheet content. See also [53].
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Taylor KL, Cheng N, Williams RW, Steven AC, Wickner RB Prion domain initiation of amyloid formation in vitro from native Ure2p. Science. 283:1999;1339-1343. Demonstrates that Ure2p prion domain can polymerise to amyloid filaments and recruit native Ure2p. Filaments are congophilic and have high β-sheet content. See also [53].
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(1999)
Science
, vol.283
, pp. 1339-1343
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Taylor, K.L.1
Cheng, N.2
Williams, R.W.3
Steven, A.C.4
Wickner, R.B.5
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53
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0033532192
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Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2
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Thual C, Komar AA, Bousset L, Fernandez-Bellot E, Cullin C, Melki R Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J Biol Chem. 274:1999;13666-13674.
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J Biol Chem
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, pp. 13666-13674
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Thual, C.1
Komar, A.A.2
Bousset, L.3
Fernandez-Bellot, E.4
Cullin, C.5
Melki, R.6
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54
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0033574042
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The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
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Reports the detection of Ure2p-GFP aggregates in [URE3], but also provides evidence that various Ure2p fragments can cure prion aggregates. This could be the basis for a therapeutic strategy.
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Edskes HK, Gray VT, Wickner RB The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci USA. 96:1999;1498-1503. Reports the detection of Ure2p-GFP aggregates in [URE3], but also provides evidence that various Ure2p fragments can cure prion aggregates. This could be the basis for a therapeutic strategy.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 1498-1503
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Edskes, H.K.1
Gray, V.T.2
Wickner, R.B.3
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55
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0033105389
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Characterization of the interaction domains of Ure2p, a prion-like protein of yeast
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Fernandez-Bellot E, Guillemet E, Baudin-Baillieu A, Gaumer S, Komar AA, Cullin C Characterization of the interaction domains of Ure2p, a prion-like protein of yeast. Biochem J. 338:1999;403-407.
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(1999)
Biochem J
, vol.338
, pp. 403-407
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Fernandez-Bellot, E.1
Guillemet, E.2
Baudin-Baillieu, A.3
Gaumer, S.4
Komar, A.A.5
Cullin, C.6
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56
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0032974451
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Two prion-inducing regions of Ure2p are nonoverlapping
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This progressive deletion analysis of Ure2p reveals a number of regions promoting or inhibiting prion formation. The idea that the amino-terminal domain is sufficient as well as necessary in this context appears too simplistic.
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Maddelein ML, Wickner RB Two prion-inducing regions of Ure2p are nonoverlapping. Mol Cell Biol. 19:1999;4516-4524. This progressive deletion analysis of Ure2p reveals a number of regions promoting or inhibiting prion formation. The idea that the amino-terminal domain is sufficient as well as necessary in this context appears too simplistic.
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(1999)
Mol Cell Biol
, vol.19
, pp. 4516-4524
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Maddelein, M.L.1
Wickner, R.B.2
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57
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0030885650
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The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
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Coustou V, Deleu C, Saupe S, Begueret J The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci USA. 94:1997;9773-9778.
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Proc Natl Acad Sci USA
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Coustou, V.1
Deleu, C.2
Saupe, S.3
Begueret, J.4
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58
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0033119401
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Non-conventional infectious elements in filamentous fungi
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Presents analysis of potential prion phenomena in filamentous fungi. Particularly valuable for analysis of older literature on modifications of hyphal morphology which propagate through cultures.
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Silar P, Daboussi MJ Non-conventional infectious elements in filamentous fungi. Trends Genet. 15:1999;141-145. Presents analysis of potential prion phenomena in filamentous fungi. Particularly valuable for analysis of older literature on modifications of hyphal morphology which propagate through cultures.
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(1999)
Trends Genet
, vol.15
, pp. 141-145
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Silar, P.1
Daboussi, M.J.2
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59
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0030613755
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Prion (PrPSc)-specific epitope defined by a monoclonal antibody
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Korth C, Stierli B, Streit P, Moser M, Schaller O, Fischer R, Schulz-Schaeffer W, Kretzschmar H, Raeber A, Braun Uet al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature. 390:1997;74-77.
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(1997)
Nature
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, pp. 74-77
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Korth, C.1
Stierli, B.2
Streit, P.3
Moser, M.4
Schaller, O.5
Fischer, R.6
Schulz-Schaeffer, W.7
Kretzschmar, H.8
Raeber, A.9
Braun, U.10
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60
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0033102301
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A novel epitope for the specific detection of exogenous prion proteins in transgenic mice and transfected murine cell lines
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Vorberg I, Buschmann A, Harmeyer S, Saalmuller A, Pfaff E, Groschup MH A novel epitope for the specific detection of exogenous prion proteins in transgenic mice and transfected murine cell lines. Virology. 255:1999;26-31.
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Virology
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, pp. 26-31
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Vorberg, I.1
Buschmann, A.2
Harmeyer, S.3
Saalmuller, A.4
Pfaff, E.5
Groschup, M.H.6
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61
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13144256747
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Prion protein expression in different species: Analysis with a panel of new mAbs
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Zanusso G, Liu D, Ferrari S, Hegyi I, Yin X, Aguzzi A, Hornemann S, Liemann S, Glockshuber R, Manson JCet al. Prion protein expression in different species: analysis with a panel of new mAbs. Proc Natl Acad Sci USA. 95:1998;8812-8816.
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Zanusso, G.1
Liu, D.2
Ferrari, S.3
Hegyi, I.4
Yin, X.5
Aguzzi, A.6
Hornemann, S.7
Liemann, S.8
Glockshuber, R.9
Manson, J.C.10
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62
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0031592937
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A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
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Peretz D, Williamson RA, Matsunaga Y, Serban H, Pinilla C, Bastidas RB, Rozenshteyn R, James TL, Houghten RA, Cohen FEet al. A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J Mol Biol. 273:1997;614-622.
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Peretz, D.1
Williamson, R.A.2
Matsunaga, Y.3
Serban, H.4
Pinilla, C.5
Bastidas, R.B.6
Rozenshteyn, R.7
James, T.L.8
Houghten, R.A.9
Cohen, F.E.10
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63
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0031710237
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Mapping the prion protein using recombinant antibodies
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sc-specific reagents. An important pointer for continuing attempts to derive specific antibodies.
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sc-specific reagents. An important pointer for continuing attempts to derive specific antibodies.
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(1998)
J Virol
, vol.72
, pp. 9413-9418
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Williamson, R.A.1
Peretz, D.2
Pinilla, C.3
Ball, H.4
Bastidas, R.B.5
Rozenshteyn, R.6
Houghten, R.A.7
Prusiner, S.B.8
Burton, D.R.9
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64
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0023499868
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Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins
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Kascsak RJ, Rubenstein R, Merz PA, Tonna-DeMasi M, Fersko R, Carp RI, Wisniewski HM, Diringer H Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol. 61:1987;3688-3693.
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J Virol
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Kascsak, R.J.1
Rubenstein, R.2
Merz, P.A.3
Tonna-Demasi, M.4
Fersko, R.5
Carp, R.I.6
Wisniewski, H.M.7
Diringer, H.8
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65
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Eight prion strains have PrP(Sc) molecules with different conformations
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Nat Med
, vol.4
, pp. 1157-1165
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Safar, J.1
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Cohen, F.E.7
Prusiner, S.B.8
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