A Carboxyl-terminal Mutation of the Epidermal Growth Factor Receptor Alters Tyrosine Kinase Activity and Substrate Specificity as Measured by a Fluorescence Polarization Assay
Open Access
- 1 July 2003
- journal article
- Published by Elsevier
- Vol. 278 (29), 26810-26816
- https://doi.org/10.1074/jbc.m301397200
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Untangling the ErbB signalling networkNature Reviews Molecular Cell Biology, 2001
- Development of High Throughput Screening Assays Using Fluorescence Polarization: Nuclear Receptor-Ligand–Binding and Kinase /Phosphatase AssaysSLAS Discovery, 2000
- Epidermal Growth Factor-stimulated Tyrosine Phosphorylation of Caveolin-1Published by Elsevier ,2000
- Tandem duplication of the epidermal growth factor receptor tyrosine kinase and calcium internalization domains in A-172 glioma cellsOncogene, 1998
- Constitutive Activation of Phosphatidylinositol 3-Kinase by a Naturally Occurring Mutant Epidermal Growth Factor ReceptorJournal of Biological Chemistry, 1998
- Involvement of ErbB2 in the Signaling Pathway Leading to Cell Cycle Progression from a Truncated Epidermal Growth Factor Receptor Lacking the C-terminal Autophosphorylation SitesPublished by Elsevier ,1996
- Fluorescence polarization — a new tool for cell and molecular biologyNature, 1995
- Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails.Proceedings of the National Academy of Sciences, 1992
- Ligand-Induced Transformation by a Noninternalizing Epidermal Growth Factor ReceptorScience, 1990
- Activation of c-erbB in avian leukosis virus-induced erythroblastosis leads to the expression of a truncated EGF receptor kinase.The EMBO Journal, 1985