Number of the records: 1
Phosphorylated full-length Tau interacts with 14-3-3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14-3-3 dimer
- 1.0541623 - FGÚ 2022 RIV GB eng J - Journal Article
Neves, J. F. - Petrvalská, Olivia - Bosica, F. - Cantrelle, F. X. - Merzougui, H. - O'Mahony, G. - Hanoulle, X. - Obšil, Tomáš - Landrieu, I.
Phosphorylated full-length Tau interacts with 14-3-3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14-3-3 dimer.
FEBS Journal. Roč. 288, č. 6 (2021), s. 1918-1934. ISSN 1742-464X. E-ISSN 1742-4658
Institutional support: RVO:67985823
Keywords : 14‐3‐3 proteins * Alzheimer’s disease * analytical ultracentrifugation * NMR spectroscopy * protein–protein interactions * Tau protein
OECD category: Biochemistry and molecular biology
Impact factor: 5.622, year: 2021
Method of publishing: Open access
https://doi.org/10.1111/febs.15574
Permanent Link: http://hdl.handle.net/11104/0319156
Number of the records: 1