Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
- 1 March 1996
- Vol. 84 (6), 889-897
- https://doi.org/10.1016/s0092-8674(00)81067-3
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Isoforms of 14‐3‐3 protein can form homo‐ and heterodimers in vivo and in vitro: implications for function as adapter proteinsFEBS Letters, 1995
- Binding of 14-3-3 Proteins to the Protein Kinase Raf and Effects on Its ActivationScience, 1994
- Phosphorylated CREB binds specifically to the nuclear protein CBPNature, 1993
- Requirement for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytesThe Journal of cell biology, 1993
- Demonstration of the Phosphorylation-Dependent Interaction of Tryptophan Hydroxylase with the 14-3-3 ProteinBiochemical and Biophysical Research Communications, 1993
- Protein kinase Cα activates RAF-1 by direct phosphorylationNature, 1993
- Activation of protein kinase C by the 14‐3‐3 proteins homologous with Exol protein that stimulates calcium‐dependent exocytosisFEBS Letters, 1992
- BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent mannerCell, 1991
- Protein kinase C inhibitor proteinsEuropean Journal of Biochemistry, 1990
- Reconstruction of the immunogenic peptide RNase(43-56) by identification and transfer of the critical residues into an unrelated peptide backbone.The Journal of Experimental Medicine, 1989