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Journal Abstract Search

118 related items for PubMed ID: 23934139

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  • 2. Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
    Schütz AK, Habenstein B, Luckgei N, Bousset L, Sourigues Y, Nielsen AB, Melki R, Böckmann A, Meier BH.
    Biomol NMR Assign; 2014 Oct; 8(2):349-56. PubMed ID: 23943018
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  • 3. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure.
    Shewmaker F, Wickner RB, Tycko R.
    Proc Natl Acad Sci U S A; 2006 Dec 26; 103(52):19754-9. PubMed ID: 17170131
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  • 9. Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain.
    Krzewska J, Tanaka M, Burston SG, Melki R.
    J Biol Chem; 2007 Jan 19; 282(3):1679-86. PubMed ID: 17121860
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  • 10. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p.
    van der Wel PC, Lewandowski JR, Griffin RG.
    J Am Chem Soc; 2007 Apr 25; 129(16):5117-30. PubMed ID: 17397156
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  • 11. 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
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  • 16. 13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils.
    Theint T, Nadaud PS, Surewicz K, Surewicz WK, Jaroniec CP.
    Biomol NMR Assign; 2017 Apr 03; 11(1):75-80. PubMed ID: 28004358
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  • 17. Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro.
    Liu Y, Wei H, Wang J, Qu J, Zhao W, Tao H.
    Biochem Biophys Res Commun; 2007 Feb 02; 353(1):139-46. PubMed ID: 17166483
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  • 18. Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22Δ) fibrils.
    Huber M, Ovchinnikova OY, Schütz AK, Glockshuber R, Meier BH, Böckmann A.
    Biomol NMR Assign; 2015 Apr 02; 9(1):7-14. PubMed ID: 24395155
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