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Biomolecules 2016, 6(2), 28; doi:10.3390/biom6020028

NMR Meets Tau: Insights into Its Function and Pathology

1
Unité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d’Ascq CNRS UMR Lille 8576, France
2
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), University of Toulouse, CNRS, INRA, INSA, Toulouse 31400, France
3
School of Mathematical Sciences, Queensland University of Technology, Brisbane 4001 QLD, Australia
4
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette 91190, France
5
Sciences Department-Chemistry, Pontifical Catholic University of Peru (PUCP), Av. Universitaria 1801, Lima 32, Peru
*
Author to whom correspondence should be addressed.
Academic Editors: Claude M. Wischik and Charles Harrington
Received: 30 March 2016 / Revised: 2 May 2016 / Accepted: 26 May 2016 / Published: 7 June 2016
(This article belongs to the Special Issue Tau Protein and Alzheimer’s disease)
View Full-Text   |   Download PDF [2249 KB, uploaded 7 June 2016]   |  

Abstract

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. View Full-Text
Keywords: Tau; NMR spectroscopy; intrinsically disordered protein; tubulin; aggregation; phosphorylation; protein/protein interactions Tau; NMR spectroscopy; intrinsically disordered protein; tubulin; aggregation; phosphorylation; protein/protein interactions
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Lippens, G.; Landrieu, I.; Smet, C.; Huvent, I.; Gandhi, N.S.; Gigant, B.; Despres, C.; Qi, H.; Lopez, J. NMR Meets Tau: Insights into Its Function and Pathology. Biomolecules 2016, 6, 28.

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