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

Autor: Jeremy Gunawardena, Caroline Smet-Nocca, Isabelle Landrieu, François-Xavier Cantrelle, Haoling Qi, Béatrice Chambraud, Clément Despres, Guy Lippens, Sudhakaran Prabakaran

Publikováno v: Tau protein : methods and protocols
Nocca Smet, Caroline. Tau protein : methods and protocols, 1523, Springer New York, pp.179-213, 2017, 978-1-4939-6596-0. ⟨10.1007/978-1-4939-6598-4_11⟩
Methods in Molecular Biology ISBN: 9781493965960

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba7fc211acda10d6bf5a058e9c4f3303
https://hal.univ-lille.fr/hal-03235823