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Journal Abstract Search

390 related items for PubMed ID: 19712107

  • 1. Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins.
    Tompa P.
    FEBS J; 2009 Oct; 276(19):5406-15. PubMed ID: 19712107
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  • 2. Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins.
    Meredith SC.
    Ann N Y Acad Sci; 2005 Dec; 1066():181-221. PubMed ID: 16533927
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  • 5. A molecular dynamics approach to the structural characterization of amyloid aggregation.
    Cecchini M, Curcio R, Pappalardo M, Melki R, Caflisch A.
    J Mol Biol; 2006 Apr 07; 357(4):1306-21. PubMed ID: 16483608
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  • 6. Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy.
    Margittai M, Langen R.
    Q Rev Biophys; 2008 Apr 07; 41(3-4):265-97. PubMed ID: 19079806
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  • 7. Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein.
    Walsh P, Simonetti K, Sharpe S.
    Structure; 2009 Mar 11; 17(3):417-26. PubMed ID: 19278656
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  • 8. 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 Mar 11; 48(26):4858-60. PubMed ID: 19472238
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  • 9. 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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  • 10. Observation of highly flexible residues in amyloid fibrils of the HET-s prion.
    Siemer AB, Arnold AA, Ritter C, Westfeld T, Ernst M, Riek R, Meier BH.
    J Am Chem Soc; 2006 Oct 11; 128(40):13224-8. PubMed ID: 17017802
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  • 12. 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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  • 13. 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 14; 162(3):387-96. PubMed ID: 18406172
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  • 14. Molecular structures of amyloid and prion fibrils: consensus versus controversy.
    Tycko R, Wickner RB.
    Acc Chem Res; 2013 Jul 16; 46(7):1487-96. PubMed ID: 23294335
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  • 16. Spin labeling analysis of amyloids and other protein aggregates.
    Margittai M, Langen R.
    Methods Enzymol; 2006 Jul 16; 413():122-39. PubMed ID: 17046394
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  • 17. [Native globular and native partially or completely disordered proteins. Folding, supramolecular complex formation and aggregation].
    Turoverov KK, Uverskiĭ VN, Kuznetsova IM.
    Tsitologiia; 2009 Jul 16; 51(3):190-203. PubMed ID: 19435273
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  • 20. Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules.
    Loquet A, Bousset L, Gardiennet C, Sourigues Y, Wasmer C, Habenstein B, Schütz A, Meier BH, Melki R, Böckmann A.
    J Mol Biol; 2009 Nov 20; 394(1):108-18. PubMed ID: 19748512
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