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Journal Abstract Search

150 related items for PubMed ID: 23125123

  • 1. Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity.
    Morris VK, Linser R, Wilde KL, Duff AP, Sunde M, Kwan AH.
    Angew Chem Int Ed Engl; 2012 Dec 07; 51(50):12621-5. PubMed ID: 23125123
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  • 2. Probing Structural Changes during Self-assembly of Surface-Active Hydrophobin Proteins that Form Functional Amyloids in Fungi.
    Pham CLL, Rodríguez de Francisco B, Valsecchi I, Dazzoni R, Pillé A, Lo V, Ball SR, Cappai R, Wien F, Kwan AH, Guijarro JI, Sunde M.
    J Mol Biol; 2018 Oct 12; 430(20):3784-3801. PubMed ID: 30096347
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  • 3. The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures.
    Mackay JP, Matthews JM, Winefield RD, Mackay LG, Haverkamp RG, Templeton MD.
    Structure; 2001 Feb 07; 9(2):83-91. PubMed ID: 11250193
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  • 4. The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity.
    Kwan AH, Macindoe I, Vukasin PV, Morris VK, Kass I, Gupte R, Mark AE, Templeton MD, Mackay JP, Sunde M.
    J Mol Biol; 2008 Oct 10; 382(3):708-20. PubMed ID: 18674544
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  • 9. 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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  • 11. Water-soluble beta-sheet models which self-assemble into fibrillar structures.
    Janek K, Behlke J, Zipper J, Fabian H, Georgalis Y, Beyermann M, Bienert M, Krause E.
    Biochemistry; 1999 Jun 29; 38(26):8246-52. PubMed ID: 10387070
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  • 12. Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry.
    Wang X, Permentier HP, Rink R, Kruijtzer JA, Liskamp RM, Wösten HA, Poolman B, Robillard GT.
    Biophys J; 2004 Sep 29; 87(3):1919-28. PubMed ID: 15345568
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