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Journal Abstract Search

347 related items for PubMed ID: 12769550

  • 21. The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance.
    Tycko R, Savtchenko R, Ostapchenko VG, Makarava N, Baskakov IV.
    Biochemistry; 2010 Nov 09; 49(44):9488-97. PubMed ID: 20925423
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  • 23. beta Sheet structure in amyloid beta fibrils and vibrational dipolar coupling.
    Paul C, Axelsen PH.
    J Am Chem Soc; 2005 Apr 27; 127(16):5754-5. PubMed ID: 15839650
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  • 29. Structural analysis of alanine tripeptide with antiparallel and parallel beta-sheet structures in relation to the analysis of mixed beta-sheet structures in Samia cynthia ricini silk protein fiber using solid-state NMR spectroscopy.
    Asakura T, Okonogi M, Nakazawa Y, Yamauchi K.
    J Am Chem Soc; 2006 May 10; 128(18):6231-8. PubMed ID: 16669693
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  • 31. Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy.
    Whittemore NA, Mishra R, Kheterpal I, Williams AD, Wetzel R, Serpersu EH.
    Biochemistry; 2005 Mar 22; 44(11):4434-41. PubMed ID: 15766273
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  • 35. Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide.
    Petkova AT, Buntkowsky G, Dyda F, Leapman RD, Yau WM, Tycko R.
    J Mol Biol; 2004 Jan 02; 335(1):247-60. PubMed ID: 14659754
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  • 36. Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L).
    Lim KH, Nguyen TN, Damo SM, Mazur T, Ball HL, Prusiner SB, Pines A, Wemmer DE.
    Solid State Nucl Magn Reson; 2006 Feb 02; 29(1-3):183-90. PubMed ID: 16256316
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  • 38. 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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  • 39. Probing the strand orientation and registry alignment in the propagation of amyloid fibrils.
    Wallace JA, Shen JK.
    Biochemistry; 2010 Jun 29; 49(25):5290-8. PubMed ID: 20491446
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  • 40. The intact human acetylcholinesterase C-terminal oligomerization domain is alpha-helical in situ and in isolation, but a shorter fragment forms beta-sheet-rich amyloid fibrils and protofibrillar oligomers.
    Cottingham MG, Voskuil JL, Vaux DJ.
    Biochemistry; 2003 Sep 16; 42(36):10863-73. PubMed ID: 12962511
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