Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells.
J Zhang(National Institute of Dental and Craniofacial Research), Reuben P. Siraganian(National Institutes of Health)
Cited by 263
Related Papers
Downstream Signaling Molecules Bind to Different Phosphorylated Immunoreceptor Tyrosine-based Activation Motif (ITAM) Peptides of the High Affinity IgE Receptor
|Journal of Biological Chemistry|1996|82
Aggregation of the High Affinity IgE Receptor Results in the Tyrosine Phosphorylation of the Surface Adhesion Protein PECAM-1 (CD31)
|Journal of Biological Chemistry|1997|56
The anti-ganglioside monoclonal antibody AA4 induces protein tyrosine phosphorylations, but not degranulation, in rat basophilic leukemia cells.
|Journal of Biological Chemistry|1994|42
The Limited Contribution of Fyn and Gab2 to the High Affinity IgE Receptor Signaling in Mast Cells
|Journal of Biological Chemistry|2010|37
Tyrosines in the Carboxyl Terminus Regulate Syk Kinase Activity and Function
|Journal of Biological Chemistry|2010|36