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Journal Abstract Search

342 related items for PubMed ID: 22260056

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  • 24. Protein misfolding and amyloid formation for the peptide GNNQQNY from yeast prion protein Sup35: simulation by reaction path annealing.
    Lipfert J, Franklin J, Wu F, Doniach S.
    J Mol Biol; 2005 Jun 10; 349(3):648-58. PubMed ID: 15896350
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  • 25. The physical dimensions of amyloid aggregates control their infective potential as prion particles.
    Marchante R, Beal DM, Koloteva-Levine N, Purton TJ, Tuite MF, Xue WF.
    Elife; 2017 Sep 07; 6():. PubMed ID: 28880146
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  • 27. Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.
    Edskes HK, Khamar HJ, Winchester CL, Greenler AJ, Zhou A, McGlinchey RP, Gorkovskiy A, Wickner RB.
    Genetics; 2014 Oct 07; 198(2):605-16. PubMed ID: 25081567
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  • 28. Structure of the cross-beta spine of amyloid-like fibrils.
    Nelson R, Sawaya MR, Balbirnie M, Madsen AØ, Riekel C, Grothe R, Eisenberg D.
    Nature; 2005 Jun 09; 435(7043):773-8. PubMed ID: 15944695
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  • 29. [Selection of DNA aptamers, specifically interacting with fibrillar form of the yeast Sup35 protein].
    Surina ER, Morozkina EV, Marchenko EV, Ter-Avanesian MD, Benevolenskiĭ SV.
    Mol Biol (Mosk); 2009 Jun 09; 43(4):682-8. PubMed ID: 19807032
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  • 32. Growth phase-dependent changes in the size and infectivity of SDS-resistant Sup35p assemblies associated with the [PSI+ ] prion in yeast.
    Wang K, Melki R, Kabani M.
    Mol Microbiol; 2019 Sep 09; 112(3):932-943. PubMed ID: 31206803
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  • 33. Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells.
    Krammer C, Suhre MH, Kremmer E, Diemer C, Hess S, Schätzl HM, Scheibel T, Vorberg I.
    FASEB J; 2008 Mar 09; 22(3):762-73. PubMed ID: 17928365
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  • 34. Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
    Luckgei N, Schütz AK, Habenstein B, Bousset L, Sourigues Y, Melki R, Meier BH, Böckmann A.
    Biomol NMR Assign; 2014 Oct 09; 8(2):365-70. PubMed ID: 23934139
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  • 36. 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
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  • 38. Conformational variations in an infectious protein determine prion strain differences.
    Tanaka M, Chien P, Naber N, Cooke R, Weissman JS.
    Nature; 2004 Mar 18; 428(6980):323-8. PubMed ID: 15029196
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