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Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.
Angew Chem Int Ed Engl. 2015 Jan 2;54(1):331-5. doi: 10.1002/anie.201408598. Epub 2014 Nov 13.
Angew Chem Int Ed Engl. 2015.
PMID: 25395337
Free PMC article.
Direct evidence for self-propagation of different amyloid-β fibril conformations.
Spirig T, Ovchinnikova O, Vagt T, Glockshuber R.
Spirig T, et al.
Neurodegener Dis. 2014;14(3):151-9. doi: 10.1159/000363623. Epub 2014 Oct 4.
Neurodegener Dis. 2014.
PMID: 25300967
Free article.
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The Osaka FAD mutation E22Δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity.
Ovchinnikova OY, Finder VH, Vodopivec I, Nitsch RM, Glockshuber R.
Ovchinnikova OY, et al.
J Mol Biol. 2011 May 13;408(4):780-91. doi: 10.1016/j.jmb.2011.02.049. Epub 2011 Mar 21.
J Mol Biol. 2011.
PMID: 21402079
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Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22Δ) fibrils.
Huber M, Ovchinnikova OY, Schütz AK, Glockshuber R, Meier BH, Böckmann A.
Huber M, et al. Among authors: ovchinnikova oy.
Biomol NMR Assign. 2015 Apr;9(1):7-14. doi: 10.1007/s12104-013-9535-x. Epub 2014 Jan 7.
Biomol NMR Assign. 2015.
PMID: 24395155
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