NMR meets Tau: Insights into its function and pathology

Guy Lippens; Isabelle Landrieu; Caroline Smet; Isabelle Huvent; Neha S. Gandhi; Benoît Gigant; Clément Despres; Haoling Qi; Juan Lopez

NMR meets Tau: Insights into its function and pathology

Guy Lippens, Isabelle Landrieu, Caroline Smet, Isabelle Huvent, Neha S. Gandhi, Benoît Gigant, Clément Despres, Haoling Qi, Juan Lopez

Sección de Química

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

25 Citas (Scopus)

Resumen

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.

Idioma original	Español
Publicación	Biomolecules
Volumen	6
Estado	Publicada - 1 jun. 2016

Citar esto

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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.",

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T1 - NMR meets Tau: Insights into its function and pathology

AU - Lippens, Guy

AU - Landrieu, Isabelle

AU - Smet, Caroline

AU - Huvent, Isabelle

AU - Gandhi, Neha S.

AU - Gigant, Benoît

AU - Despres, Clément

AU - Qi, Haoling

AU - Lopez, Juan

PY - 2016/6/1

Y1 - 2016/6/1

N2 - 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.

AB - 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.

M3 - Artículo

VL - 6

JO - Biomolecules

JF - Biomolecules

ER -