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111 related items for PubMed ID: 19647741
1. Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta. Sluchanko NN, Seit-Nebi AS, Gusev NB. FEBS Lett; 2009 Sep 03; 583(17):2739-42. PubMed ID: 19647741 [Abstract] [Full Text] [Related]
2. Effect of phosphorylation on interaction of human tau protein with 14-3-3zeta. Sluchanko NN, Seit-Nebi AS, Gusev NB. Biochem Biophys Res Commun; 2009 Feb 20; 379(4):990-4. PubMed ID: 19138662 [Abstract] [Full Text] [Related]
4. Phosphomimicking mutations of human 14-3-3ζ affect its interaction with tau protein and small heat shock protein HspB6. Sluchanko NN, Sudnitsyna MV, Chernik IS, Seit-Nebi AS, Gusev NB. Arch Biochem Biophys; 2011 Feb 01; 506(1):24-34. PubMed ID: 21081103 [Abstract] [Full Text] [Related]
6. Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction. Tugaeva KV, Tsvetkov PO, Sluchanko NN. PLoS One; 2017 Feb 01; 12(6):e0178933. PubMed ID: 28575131 [Abstract] [Full Text] [Related]
8. Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers. Hernández F, Cuadros R, Avila J. Neurosci Lett; 2004 Mar 04; 357(2):143-6. PubMed ID: 15036595 [Abstract] [Full Text] [Related]
11. 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. Neves JF, Petrvalská O, Bosica F, Cantrelle FX, Merzougui H, O'Mahony G, Hanoulle X, Obšil T, Landrieu I. FEBS J; 2021 Mar 04; 288(6):1918-1934. PubMed ID: 32979285 [Abstract] [Full Text] [Related]
18. Properties of the monomeric form of human 14-3-3ζ protein and its interaction with tau and HspB6. Sluchanko NN, Sudnitsyna MV, Seit-Nebi AS, Antson AA, Gusev NB. Biochemistry; 2011 Nov 15; 50(45):9797-808. PubMed ID: 21978388 [Abstract] [Full Text] [Related]