c-Abl Has High Intrinsic Tyrosine Kinase Activity That Is Stimulated by Mutation of the Src Homology 3 Domain and by Autophosphorylation at Two Distinct Regulatory Tyrosines
Open Access
- 1 November 2000
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 275 (45), 35631-35637
- https://doi.org/10.1074/jbc.m005401200
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine KinaseScience, 2000
- The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genesOncogene, 1998
- An intramolecular SH3-domain interaction regulates c-Abl activityNature Genetics, 1998
- Crystal structure of the Src family tyrosine kinase HckNature, 1997
- Three-dimensional structure of the tyrosine kinase c-SrcNature, 1997
- An Activating Mutation in the ATP Binding Site of the ABL Kinase DomainOnline Journal of Public Health Informatics, 1996
- Catalytic specificity of protein-tyrosine kinases is critical for selective signallingNature, 1995
- A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycleCell, 1993
- Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-srcCell, 1987
- Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylationCell, 1987