BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

209 related articles for article (PubMed ID: 21300906)

  • 1. Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy.
    Mizuno N; Baxa U; Steven AC
    Proc Natl Acad Sci U S A; 2011 Feb; 108(8):3252-7. PubMed ID: 21300906
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils.
    Sen A; Baxa U; Simon MN; Wall JS; Sabate R; Saupe SJ; Steven AC
    J Biol Chem; 2007 Feb; 282(8):5545-50. PubMed ID: 17178708
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Correlation of structural elements and infectivity of the HET-s prion.
    Ritter C; Maddelein ML; Siemer AB; Lührs T; Ernst M; Meier BH; Saupe SJ; Riek R
    Nature; 2005 Jun; 435(7043):844-8. PubMed ID: 15944710
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).
    Wan W; Bian W; McDonald M; Kijac A; Wemmer DE; Stubbs G
    J Biol Chem; 2013 Oct; 288(41):29604-12. PubMed ID: 23986444
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.
    Wasmer C; Lange A; Van Melckebeke H; Siemer AB; Riek R; Meier BH
    Science; 2008 Mar; 319(5869):1523-6. PubMed ID: 18339938
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility.
    Saupe SJ
    Semin Cell Dev Biol; 2011 Jul; 22(5):460-8. PubMed ID: 21334447
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Prion and non-prion amyloids of the HET-s prion forming domain.
    Sabaté R; Baxa U; Benkemoun L; Sánchez de Groot N; Coulary-Salin B; Maddelein ML; Malato L; Ventura S; Steven AC; Saupe SJ
    J Mol Biol; 2007 Jul; 370(4):768-83. PubMed ID: 17532341
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry.
    Nazabal A; Maddelein ML; Bonneu M; Saupe SJ; Schmitter JM
    J Biol Chem; 2005 Apr; 280(14):13220-8. PubMed ID: 15647259
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Molecular structures of amyloid and prion fibrils: consensus versus controversy.
    Tycko R; Wickner RB
    Acc Chem Res; 2013 Jul; 46(7):1487-96. PubMed ID: 23294335
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Fibril elongation mechanisms of HET-s prion-forming domain: topological evidence for growth polarity.
    Baiesi M; Seno F; Trovato A
    Proteins; 2011 Nov; 79(11):3067-81. PubMed ID: 21989930
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils.
    Dos Reis S; Coulary-Salin B; Forge V; Lascu I; Bégueret J; Saupe SJ
    J Biol Chem; 2002 Feb; 277(8):5703-6. PubMed ID: 11733532
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity.
    Wasmer C; Zimmer A; Sabaté R; Soragni A; Saupe SJ; Ritter C; Meier BH
    J Mol Biol; 2010 Sep; 402(2):311-25. PubMed ID: 20600104
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.
    Balguerie A; Dos Reis S; Coulary-Salin B; Chaignepain S; Sabourin M; Schmitter JM; Saupe SJ
    J Cell Sci; 2004 May; 117(Pt 12):2599-610. PubMed ID: 15159455
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity.
    Benkemoun L; Sabaté R; Malato L; Dos Reis S; Dalstra H; Saupe SJ; Maddelein ML
    Methods; 2006 May; 39(1):61-7. PubMed ID: 16750391
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.
    Daskalov A; Gantner M; Wälti MA; Schmidlin T; Chi CN; Wasmer C; Schütz A; Ceschin J; Clavé C; Cescau S; Meier B; Riek R; Saupe SJ
    PLoS Pathog; 2014 Jun; 10(6):e1004158. PubMed ID: 24945274
    [TBL] [Abstract][Full Text] [Related]  

  • 16. On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2.
    Sabaté R; Lascu I; Saupe SJ
    J Struct Biol; 2008 Jun; 162(3):387-96. PubMed ID: 18406172
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Infectious fold and amyloid propagation in Podospora anserina.
    Maddelein ML
    Prion; 2007; 1(1):44-7. PubMed ID: 19164904
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Two structurally similar fungal prions efficiently cross-seed in vivo but form distinct polymers when coexpressed.
    Benkemoun L; Ness F; Sabaté R; Ceschin J; Breton A; Clavé C; Saupe SJ
    Mol Microbiol; 2011 Dec; 82(6):1392-405. PubMed ID: 22050595
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Energy barriers for HET-s prion forming domain amyloid formation.
    Sabaté R; Castillo V; Espargaró A; Saupe SJ; Ventura S
    FEBS J; 2009 Sep; 276(18):5053-64. PubMed ID: 19682303
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids.
    Gendoo DM; Harrison PM
    PLoS One; 2011; 6(11):e27342. PubMed ID: 22096554
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 11.