These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Journal Abstract Search


197 related items for PubMed ID: 21094164

  • 1. 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
    [Abstract] [Full Text] [Related]

  • 2.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 3. 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
    [Abstract] [Full Text] [Related]

  • 4. 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
    [Abstract] [Full Text] [Related]

  • 5.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8. 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
    [Abstract] [Full Text] [Related]

  • 9.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 10.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 13. Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling.
    Tycko R, Ishii Y.
    J Am Chem Soc; 2003 Jun 04; 125(22):6606-7. PubMed ID: 12769550
    [Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15. Energy barriers for HET-s prion forming domain amyloid formation.
    Sabaté R, Castillo V, Espargaró A, Saupe SJ, Ventura S.
    FEBS J; 2009 Sep 04; 276(18):5053-64. PubMed ID: 19682303
    [Abstract] [Full Text] [Related]

  • 16.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 18.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 19.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 20. 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
    [Abstract] [Full Text] [Related]


    Page: [Next] [New Search]
    of 10.