Genotoxic Drugs Induce Interaction of the c-Abl Tyrosine Kinase and the Tumor Suppressor Protein p53
Open Access
- 1 October 1996
- journal article
- Published by Elsevier
- Vol. 271 (43) , 26457-26460
- https://doi.org/10.1074/jbc.271.43.26457
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- The stress response to ionizing radiation involoves c-Abl-dependent phosphorylation of SHPTP1.Proceedings of the National Academy of Sciences, 1996
- Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity.Genes & Development, 1995
- Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity.Genes & Development, 1995
- Src homology 2 domain as a specificity determinant in the c-Abl-mediated tyrosine phosphorylation of the RNA polymerase II carboxyl-terminal repeated domain.Proceedings of the National Academy of Sciences, 1995
- The nuclear tyrosine kinase c-abl negatively regulates cell growthCell, 1994
- Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites.Genes & Development, 1994
- The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity [published erratum appears in J Cell Biol 1994 Mar;124(5):865]The Journal of cell biology, 1994
- Tyrosine phosphorylation of mammalian RNA polymerase II carboxyl-terminal domain.Proceedings of the National Academy of Sciences, 1993
- Cell Cycle—Regulated Binding of c-Abl Tyrosine Kinase to DNAScience, 1992
- The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localizationCell, 1989