Activation and internalization of p56lck upon CD45 triggering of Jurkat cells
- 1 June 1994
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 24 (6) , 1255-1261
- https://doi.org/10.1002/eji.1830240603
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Four CD45/P56lck‐associated phosphorproteins (pp29‐pp32) undergo alterations in human T cell activationEuropean Journal of Immunology, 1992
- Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane trafficCell, 1991
- A functional complex is formed in human T lymphocytes between the protein tyrosine phosphatase CD45, the protein tyrosine kinase p56lck and pp32, a possible common substrateEuropean Journal of Immunology, 1991
- The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2–6 sialyltransferase, CD75, on B cellsCell, 1991
- The tyrosine kinase activity of p56lck is increased in human T cells activated via CD2European Journal of Immunology, 1991
- The Leukocyte Common Antigen FamilyAnnual Review of Immunology, 1989
- Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p56lckNature, 1989
- Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ERCell, 1989
- Demonstration that the leukocyte common antigen (CD45) is a protein tyrosine phosphataseBiochemistry, 1988
- Polyacrylamide gel electrophoresis of small peptidesElectrophoresis, 1984