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175 related items for PubMed ID: 20339590

  • 1. Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context.
    Bousset L, Bonnefoy J, Sourigues Y, Wien F, Melki R.
    PLoS One; 2010 Mar 22; 5(3):e9760. PubMed ID: 20339590
    [Abstract] [Full Text] [Related]

  • 2. Structure of the prion Ure2p in protein fibrils assembled in vitro.
    Fay N, Redeker V, Savistchenko J, Dubois S, Bousset L, Melki R.
    J Biol Chem; 2005 Nov 04; 280(44):37149-58. PubMed ID: 16131495
    [Abstract] [Full Text] [Related]

  • 3. Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.
    Fei L, Perrett S.
    J Biol Chem; 2009 Apr 24; 284(17):11134-41. PubMed ID: 19258323
    [Abstract] [Full Text] [Related]

  • 4. Hydrogen/deuterium exchange mass spectrometric analysis of conformational changes accompanying the assembly of the yeast prion Ure2p into protein fibrils.
    Redeker V, Halgand F, Le Caer JP, Bousset L, Laprévote O, Melki R.
    J Mol Biol; 2007 Jun 15; 369(4):1113-25. PubMed ID: 17482207
    [Abstract] [Full Text] [Related]

  • 5. The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils.
    Bousset L, Briki F, Doucet J, Melki R.
    J Struct Biol; 2003 Feb 15; 141(2):132-42. PubMed ID: 12615539
    [Abstract] [Full Text] [Related]

  • 6. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p.
    Bousset L, Redeker V, Decottignies P, Dubois S, Le Maréchal P, Melki R.
    Biochemistry; 2004 May 04; 43(17):5022-32. PubMed ID: 15109261
    [Abstract] [Full Text] [Related]

  • 7. The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein.
    Schlumpberger M, Wille H, Baldwin MA, Butler DA, Herskowitz I, Prusiner SB.
    Protein Sci; 2000 Mar 04; 9(3):440-51. PubMed ID: 10752606
    [Abstract] [Full Text] [Related]

  • 8. Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p.
    Thual C, Bousset L, Komar AA, Walter S, Buchner J, Cullin C, Melki R.
    Biochemistry; 2001 Feb 13; 40(6):1764-73. PubMed ID: 11327838
    [Abstract] [Full Text] [Related]

  • 9. The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.
    Kryndushkin DS, Wickner RB, Tycko R.
    J Mol Biol; 2011 Jun 03; 409(2):263-77. PubMed ID: 21497604
    [Abstract] [Full Text] [Related]

  • 10. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro.
    Bousset L, Thomson NH, Radford SE, Melki R.
    EMBO J; 2002 Jun 17; 21(12):2903-11. PubMed ID: 12065404
    [Abstract] [Full Text] [Related]

  • 11. Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p.
    Catharino S, Buchner J, Walter S.
    Biol Chem; 2005 Jul 17; 386(7):633-41. PubMed ID: 16207084
    [Abstract] [Full Text] [Related]

  • 12. Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterization.
    Fay N, Inoue Y, Bousset L, Taguchi H, Melki R.
    J Biol Chem; 2003 Aug 08; 278(32):30199-205. PubMed ID: 12777380
    [Abstract] [Full Text] [Related]

  • 13. Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions.
    Sabaté R, Villar-Piqué A, Espargaró A, Ventura S.
    Biomacromolecules; 2012 Feb 13; 13(2):474-83. PubMed ID: 22176525
    [Abstract] [Full Text] [Related]

  • 14. Molecular chaperones and the assembly of the prion Ure2p in vitro.
    Savistchenko J, Krzewska J, Fay N, Melki R.
    J Biol Chem; 2008 Jun 06; 283(23):15732-9. PubMed ID: 18400756
    [Abstract] [Full Text] [Related]

  • 15. Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.
    Edskes HK, Wickner RB.
    Proc Natl Acad Sci U S A; 2002 Dec 10; 99 Suppl 4(Suppl 4):16384-91. PubMed ID: 12177423
    [Abstract] [Full Text] [Related]

  • 16. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae.
    Bousset L, Belrhali H, Janin J, Melki R, Morera S.
    Structure; 2001 Jan 10; 9(1):39-46. PubMed ID: 11342133
    [Abstract] [Full Text] [Related]

  • 17. In vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion.
    Immel F, Jiang Y, Wang YQ, Marchal C, Maillet L, Perrett S, Cullin C.
    J Biol Chem; 2007 Mar 16; 282(11):7912-20. PubMed ID: 17234629
    [Abstract] [Full Text] [Related]

  • 18. The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.
    Wang K, Redeker V, Madiona K, Melki R, Kabani M.
    PLoS One; 2015 Mar 16; 10(6):e0131789. PubMed ID: 26115123
    [Abstract] [Full Text] [Related]

  • 19. Prion generation in vitro: amyloid of Ure2p is infectious.
    Brachmann A, Baxa U, Wickner RB.
    EMBO J; 2005 Sep 07; 24(17):3082-92. PubMed ID: 16096644
    [Abstract] [Full Text] [Related]

  • 20. Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae.
    Shewmaker F, Mull L, Nakayashiki T, Masison DC, Wickner RB.
    Genetics; 2007 Jul 07; 176(3):1557-65. PubMed ID: 17507672
    [Abstract] [Full Text] [Related]

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