Catalytic activation of the membrane distal domain of protein tyrosine phosphatase ϵ, but not CD45, by two point mutations
- 1 October 1999
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1434 (2) , 275-283
- https://doi.org/10.1016/s0167-4838(99)00189-2
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- The Second Domain of the CD45 Protein Tyrosine Phosphatase Is Critical for Interleukin-2 Secretion and Substrate Recruitment of TCR-ζ in VivoJournal of Biological Chemistry, 1998
- Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domainsTrends in Biochemical Sciences, 1998
- Anti-phosphatases take the stageNature Genetics, 1998
- Kinetic Analysis of two Closely Related Receptor‐Like Protein‐Tyrosine‐Phosphatases, PTPα and PTPεEuropean Journal of Biochemistry, 1997
- Comparative Kinetic Analysis and Substrate Specificity of the Tandem Catalytic Domains of the Receptor-like Protein-tyrosine Phosphatase αJournal of Biological Chemistry, 1997
- Form and Function in Protein DephosphorylationCell, 1996
- From Form to Function: Signaling by Protein Tyrosine PhosphatasesCell, 1996
- Protein tyrosine phosphatases in signalingCurrent Opinion in Cell Biology, 1996
- Purification and characterization of the cytoplasmic domain of human receptorlike protein tyrosine phosphatase RPTP.mu.Biochemistry, 1993
- A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila.Proceedings of the National Academy of Sciences, 1989