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Additional file 6: of Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain

Authors :
Sottejeau, Yoann
Bretteville, Alexis
François-Xavier Cantrelle
Malmanche, Nicolas
Demiaute, Florie
Mendes, Tiago
Delay, Charlotte
Alves, Harmony Alves Dos
Flaig, Amandine
Davies, Peter
Dourlen, Pierre
Dermaut, Bart
Laporte, Jocelyn
Amouyel, Philippe
Lippens, Guy
Chapuis, Julien
Landrieu, Isabelle
Jean-Charles Lambert
Publication Year :
2019
Publisher :
figshare, 2019.

Abstract

Tau phosphorylation precludes the BIN1-Tau interaction in vitro. 2D [1H, 15N] HSQC spectra of 125 μM 15N CDK-phosphorylated Tau-F5[165–245] free in solution (gray) and with a 1 molar amount of GST-BIN1/SH3 (red, superimposed). No CS perturbations or peak broadening were observed - indicating the absence of interaction between BIN1 and Tau-F5. (PDF 67 kb)

Details

Database :
OpenAIRE
Accession number :
edsair.doi.dedup.....4b9476e69ac0298de037d2da3c185127
Full Text :
https://doi.org/10.6084/m9.figshare.10040495