The Study of Posttranslational Modifications ...
Document type :
Partie d'ouvrage: Chapitre
Permalink :
Title :
The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein
Author(s) :
Qi, Haoling [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Despres, Clément [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Prabakaran, Sudhakaran [Auteur]
Harvard Medical School [Boston] [HMS]
Cantrelle, Francois-Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Chambraud, Béatrice [Auteur]
Petites Molécules de neuroprotection, neurorégénération et remyélinisation
Gunawardena, Jeremy [Auteur]
Harvard Medical School [Boston] [HMS]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Nocca Smet, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Landrieu, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Despres, Clément [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Prabakaran, Sudhakaran [Auteur]
Harvard Medical School [Boston] [HMS]
Cantrelle, Francois-Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Chambraud, Béatrice [Auteur]
Petites Molécules de neuroprotection, neurorégénération et remyélinisation
Gunawardena, Jeremy [Auteur]
Harvard Medical School [Boston] [HMS]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Nocca Smet, Caroline [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Landrieu, Isabelle [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Scientific editor(s) :
Nocca Smet, Caroline
Book title :
Tau protein : methods and protocols
Volume number :
1523
Pages :
179-213
Publisher :
Springer New York
Publication place :
New York, NY
Publication date :
2017
ISBN :
978-1-4939-6596-0
English keyword(s) :
Phosphorylation
Acetylation
ERK kinase
Creb-binding protein
Acetyltransferase
NMR spectroscopy
Recombinant proteins
Acetylation
ERK kinase
Creb-binding protein
Acetyltransferase
NMR spectroscopy
Recombinant proteins
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Nuclear magnetic resonance (NMR) spectroscopy can be used as an analytical tool to investigate posttranslational modifications of protein. NMR is a valuable tool to map the interaction regions of protein partners. Here, ...
Show more >Nuclear magnetic resonance (NMR) spectroscopy can be used as an analytical tool to investigate posttranslational modifications of protein. NMR is a valuable tool to map the interaction regions of protein partners. Here, we present protocols that have been developed in the course of our studies of the neuronal Tau protein. Tau is found aggregated in the neurons of Alzheimer’s disease patients. Development of the disease is accompanied by increased, abnormal phosphorylation and acetylation of Tau. We have used NMR to investigate how these posttranslational modifications of Tau affect the interactions with its partners. We present here detailed protocols of in vitro phosphorylation of Tau by recombinant kinase, ERK2, or kinase activity of rat brain extracts, and acetylation by recombinant Creb-binding protein (CBP) acetyltransferase. The analytical characterization of the modified Tau by NMR spectroscopy is additionally described.Show less >
Show more >Nuclear magnetic resonance (NMR) spectroscopy can be used as an analytical tool to investigate posttranslational modifications of protein. NMR is a valuable tool to map the interaction regions of protein partners. Here, we present protocols that have been developed in the course of our studies of the neuronal Tau protein. Tau is found aggregated in the neurons of Alzheimer’s disease patients. Development of the disease is accompanied by increased, abnormal phosphorylation and acetylation of Tau. We have used NMR to investigate how these posttranslational modifications of Tau affect the interactions with its partners. We present here detailed protocols of in vitro phosphorylation of Tau by recombinant kinase, ERK2, or kinase activity of rat brain extracts, and acetylation by recombinant Creb-binding protein (CBP) acetyltransferase. The analytical characterization of the modified Tau by NMR spectroscopy is additionally described.Show less >
Language :
Anglais
Audience :
Non spécifiée
ANR Project :
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
RMN et interactions moléculaires
Submission date :
2020-02-12T15:45:03Z
2021-05-26T06:55:26Z
2021-05-26T06:57:25Z
2021-05-26T06:55:26Z
2021-05-26T06:57:25Z