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dc.contributor.authorGandhi, Neha
dc.contributor.authorLandrieu, I.
dc.contributor.authorByrne, C.
dc.contributor.authorKukic, P.
dc.contributor.authorAmniai, L.
dc.contributor.authorCantrelle, F.
dc.contributor.authorWieruszeski, J.
dc.contributor.authorMancera, Ricardo
dc.contributor.authorJacquot, Y.
dc.contributor.authorLippens, G.
dc.identifier.citationGandhi, N. and Landrieu, I. and Byrne, C. and Kukic, P. and Amniai, L. and Cantrelle, F. and Wieruszeski, J. et al. 2015. A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein. Angewandte Chemie - International Edition. 54 (23): pp. 6819-6823.

Post mortem biochemical staging of Alzheimer’s disease is currently based on immunochemical analysis of brain slices with the AT8 antibody. The epitope of AT8 is described around the pSer202/pThr205 region of the hyperphosphorylated form of the neuronal protein tau. In this study, NMR spectroscopy was used to precisely map the AT8 epitope on phosphorylated tau, and derive its defining structural features by a combination of NMR analyses and molecular dynamics. A particular turn conformation is stabilized by a hydrogen bond of the phosphorylated Thr205 residue to the amide proton of Gly207, and is further stabilized by the two Arg residues opposing the pSer202/pThr205.

dc.publisherWiley-VCH Verlag
dc.titleA phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein
dc.typeJournal Article
dcterms.source.titleAngewandte Chemie - International Edition
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available

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