NMR meets Tau: Insights into its function and pathology
Lippens, Guy, Landrieu, Isabelle, Smet, Caroline, Huvent, Isabelle, Gandhi, Neha S., Gigant, Benoît, Despres, Clément, Qi, Haoling, & Lopez, Juan (2016) NMR meets Tau: Insights into its function and pathology. Biomolecules, 6(2), Article no. 28.
In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.
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|Item Type:||Journal Article|
|Keywords:||Tau protein, Alzheimer's disease, NMR spectroscopy, intrinsically disordered protein, tubulin, aggregation, phosphorylation, protein/protein interactions|
|Divisions:||Current > Schools > School of Mathematical Sciences
Current > QUT Faculties and Divisions > Science & Engineering Faculty
|Copyright Owner:||Copyright 2016 by the authors; licensee MDPI, Basel, Switzerland|
|Copyright Statement:||This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/)|
|Deposited On:||28 Aug 2016 23:19|
|Last Modified:||29 Aug 2016 23:05|
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