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NMR Meets Tau: Insights into Its Function and Pathology

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 bot...

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Autores principales: Lippens, Guy, Landrieu, Isabelle, Smet, Caroline, Huvent, Isabelle, Gandhi, Neha S., Gigant, Benoît, Despres, Clément, Qi, Haoling, Lopez, Juan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4919923/
https://www.ncbi.nlm.nih.gov/pubmed/27338491
http://dx.doi.org/10.3390/biom6020028
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author Lippens, Guy
Landrieu, Isabelle
Smet, Caroline
Huvent, Isabelle
Gandhi, Neha S.
Gigant, Benoît
Despres, Clément
Qi, Haoling
Lopez, Juan
author_facet Lippens, Guy
Landrieu, Isabelle
Smet, Caroline
Huvent, Isabelle
Gandhi, Neha S.
Gigant, Benoît
Despres, Clément
Qi, Haoling
Lopez, Juan
author_sort Lippens, Guy
collection PubMed
description 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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spelling pubmed-49199232016-06-24 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 Biomolecules Review 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. MDPI 2016-06-07 /pmc/articles/PMC4919923/ /pubmed/27338491 http://dx.doi.org/10.3390/biom6020028 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. 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/).
spellingShingle Review
Lippens, Guy
Landrieu, Isabelle
Smet, Caroline
Huvent, Isabelle
Gandhi, Neha S.
Gigant, Benoît
Despres, Clément
Qi, Haoling
Lopez, Juan
NMR Meets Tau: Insights into Its Function and Pathology
title NMR Meets Tau: Insights into Its Function and Pathology
title_full NMR Meets Tau: Insights into Its Function and Pathology
title_fullStr NMR Meets Tau: Insights into Its Function and Pathology
title_full_unstemmed NMR Meets Tau: Insights into Its Function and Pathology
title_short NMR Meets Tau: Insights into Its Function and Pathology
title_sort nmr meets tau: insights into its function and pathology
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4919923/
https://www.ncbi.nlm.nih.gov/pubmed/27338491
http://dx.doi.org/10.3390/biom6020028
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