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Journal Abstract Search

356 related items for PubMed ID: 19472238

  • 1. Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.
    Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, Wang L, Riek R, Saupe SJ, Meier BH.
    Angew Chem Int Ed Engl; 2009; 48(26):4858-60. PubMed ID: 19472238
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  • 3. 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 15; 117(Pt 12):2599-610. PubMed ID: 15159455
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  • 4. 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 17; 402(2):311-25. PubMed ID: 20600104
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  • 5. Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion.
    Sabaté R, Espargaró A, Saupe SJ, Ventura S.
    Microb Cell Fact; 2009 Oct 28; 8():56. PubMed ID: 19863787
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  • 6. 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 14; 319(5869):1523-6. PubMed ID: 18339938
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  • 7. The molecular organization of the fungal prion HET-s in its amyloid form.
    Wasmer C, Schütz A, Loquet A, Buhtz C, Greenwald J, Riek R, Böckmann A, Meier BH.
    J Mol Biol; 2009 Nov 20; 394(1):119-27. PubMed ID: 19748509
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  • 9. High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
    Siemer AB, Ritter C, Ernst M, Riek R, Meier BH.
    Angew Chem Int Ed Engl; 2005 Apr 15; 44(16):2441-4. PubMed ID: 15770629
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  • 10. Amyloid aggregates of the HET-s prion protein are infectious.
    Maddelein ML, Dos Reis S, Duvezin-Caubet S, Coulary-Salin B, Saupe SJ.
    Proc Natl Acad Sci U S A; 2002 May 28; 99(11):7402-7. PubMed ID: 12032295
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  • 11. 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 28; 39(1):61-7. PubMed ID: 16750391
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  • 12. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.
    Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, Forge V, Bathany K, Lascu I, Schmitter JM, Riek R, Saupe SJ.
    EMBO J; 2003 May 01; 22(9):2071-81. PubMed ID: 12727874
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  • 13. Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
    Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A.
    J Mol Biol; 2011 Jan 21; 405(3):765-72. PubMed ID: 21094164
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  • 14. Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
    Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH.
    J Am Chem Soc; 2010 Oct 06; 132(39):13765-75. PubMed ID: 20828131
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  • 15. Amyloid-like properties of bacterial inclusion bodies.
    Carrió M, González-Montalbán N, Vera A, Villaverde A, Ventura S.
    J Mol Biol; 2005 Apr 15; 347(5):1025-37. PubMed ID: 15784261
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  • 16. 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 11; 288(41):29604-12. PubMed ID: 23986444
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  • 17. Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins.
    Tompa P.
    FEBS J; 2009 Oct 11; 276(19):5406-15. PubMed ID: 19712107
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  • 19. Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry.
    Nazabal A, Dos Reis S, Bonneu M, Saupe SJ, Schmitter JM.
    Biochemistry; 2003 Jul 29; 42(29):8852-61. PubMed ID: 12873146
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  • 20. Fibril elongation mechanisms of HET-s prion-forming domain: topological evidence for growth polarity.
    Baiesi M, Seno F, Trovato A.
    Proteins; 2011 Nov 29; 79(11):3067-81. PubMed ID: 21989930
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