Kinetics of Tyrosine Phosphorylation When IgE Dimers Bind to FC∊ Receptors on Rat Basophilic Leukemia Cells
Open Access
- 1 September 1995
- journal article
- Published by Elsevier
- Vol. 270 (35) , 20264-20272
- https://doi.org/10.1074/jbc.270.35.20264
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- The B-cell antigen receptor complex: structure and signal transductionImmunology Today, 1994
- Signal transduction by lymphocyte antigen receptorsCell, 1994
- Multichain immune recognition receptors: similarities in structure and signaling pathwaysImmunology Today, 1992
- Aggregation of IgE-receptor complexes on rat basophilic leukemia cells does not change the intrinsic affinity but can alter the kinetics of the ligand-IgE interactionBiochemistry, 1992
- Protein-tyrosine phosphorylation: an essential component of FcεRI signalingImmunology Today, 1992
- DNP‐phycobiliproteins, fluorescent antigens to study dynamic properties of antigen‐IgE‐receptor complexes on RBL‐2H3 rat mast cellsCytometry, 1987
- Kinetic analysis of histamine release due to covalently linked ige dimersMolecular Immunology, 1982
- IgE‐induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clonesEuropean Journal of Immunology, 1981
- Interaction of IgE with rat basophilic leukemia cells—v. Binding properties of cell free particlesImmunochemistry, 1976
- Binding of histamine- and other ligand-conjugated macromolecules to lymphocytesMolecular and Cellular Biochemistry, 1975