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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]
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]
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]
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]