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.

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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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1 citations in Scopus
2 citations in Web of Science®
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ID Code: 98431
Item Type: Journal Article
Refereed: Yes
Keywords: Tau protein, Alzheimer's disease, NMR spectroscopy, intrinsically disordered protein, tubulin, aggregation, phosphorylation, protein/protein interactions
DOI: 10.3390/biom6020028
ISSN: 2218-273X
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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