Induction of hyperphosphorylation and activation of the p56lck protein tyrosine kinase by phenylarsine oxide, a phosphotyrosine phosphatase inhibitor
- 31 December 1994
- journal article
- Published by Elsevier in Molecular Immunology
- Vol. 31 (17) , 1295-1302
- https://doi.org/10.1016/0161-5890(94)90047-7
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- T cell antigen receptor signaling: Three families of tyrosine kinases and a phosphataseImmunity, 1994
- Regulation of src family tyrosine kinases in lymphocytesTrends in Biochemical Sciences, 1993
- Reduced tyrosine phosphorylation in polyamine-starved cellsExperimental Cell Research, 1992
- Phenylarsine oxide augments tyrosine phosphorylation in hematopoietic cellsEuropean Journal of Haematology, 1992
- The retarded electrophoretic migration of p56lck induced by vanadate in lymphoma cells correlates with modified kinase activityBiochimie, 1990
- The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lckCell, 1988
- Correlation between phosphorylation and kinase activity of a tyrosine protein kinase: P56 lckBiochemical and Biophysical Research Communications, 1987
- Demonstration that LSTRA cells have an elevated level of proteins phosphorylated on tyrosine residuesFEBS Letters, 1987
- Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertionNature, 1986
- A lymphocyte-specific protein-tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRACell, 1985