The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
Open Access
- 1 December 1997
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 91 (7), 961-971
- https://doi.org/10.1016/s0092-8674(00)80487-0
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- 14-3-3 Is Phosphorylated by Casein Kinase I on Residue 233Published by Elsevier BV ,1997
- Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase AktScience, 1997
- Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death MachineryCell, 1997
- 14-3-3 (ϵ) Interacts with the Insulin-like Growth Factor I Receptor and Insulin Receptor Substrate I in a Phosphoserine-dependent MannerJournal of Biological Chemistry, 1997
- 14-3-3 and its possible role in co-ordinating multiple signalling pathwaysTrends in Cell Biology, 1996
- Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells.Proceedings of the National Academy of Sciences of the United States of America, 1995
- Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase CMolecular and Cellular Biochemistry, 1995
- 14-3-3 α and δ Are the Phosphorylated Forms of Raf-activating 14-3-3 β and ζPublished by Elsevier BV ,1995
- Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen.Proceedings of the National Academy of Sciences of the United States of America, 1994
- RIBBONS 2.0Journal of Applied Crystallography, 1991