Structural Basis for the Requirement of Two Phosphotyrosine Residues in Signaling Mediated by Syk Tyrosine Kinase
- 1 March 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 356 (5) , 1222-1236
- https://doi.org/10.1016/j.jmb.2005.11.095
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Structural and Thermodynamic Basis for the Interaction of the Src SH2 Domain with the Activated Form of the PDGF β-receptorJournal of Molecular Biology, 2003
- Phosphorylation of Tyr342 in the Linker Region of Syk Is Critical for FcεRI Signaling in Mast CellsMolecular and Cellular Biology, 2002
- Regulation of Signaling in B Cells through the Phosphorylation of Syk on Linker Region TyrosinesPublished by Elsevier ,2002
- Crystal structures of the SH2 domain of grb2: highlight on the binding of a new high-affinity inhibitorJournal of Molecular Biology, 2002
- Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinaseJournal of Molecular Biology, 1999
- Cbl-mediated Negative Regulation of the Syk Tyrosine KinaseJournal of Biological Chemistry, 1998
- Solution structure of the C-terminal SH2 domain of the p85α regulatory subunit of phosphoinositide 3-kinaseJournal of Molecular Biology, 1998
- Selective Inhibition of the Growth of ras-Transformed Human Bronchial Epithelial Cells by Emodin, a Protein-Tyrosine Kinase InhibitorBiochemical and Biophysical Research Communications, 1993
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993
- Polyacrylamide gel electrophoresis of small peptidesElectrophoresis, 1984