Studies of the very Early Responses of a Receptor Tyrosine Kinase to Growth Factor Binding and their Application to the Purification and Identification of Proteins that are Tyrosine Phosphorylated in the Growth Factor Response
- 1 January 1993
- book chapter
- Published by Springer Science and Business Media LLC
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences.Molecular and Cellular Biology, 1992
- Peptide antisera to human colony-stimulating factor 1 receptor detect ligand-induced conformational changes and a binding site for phosphatidylinositol 3-kinase.Molecular and Cellular Biology, 1991
- cDNA cloning of a Novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptorCell, 1991
- Alterations in CSF-1 Receptor Expression and Protein Tyrosine Phosphorylation in Autonomous Mutants of a CSF-1 Dependent Macrophage Cell LineGrowth Factors, 1991
- Direct activation of the serine/threonine kinase activity of raf-1 through tyrosine phosphorylation by the PDGF β-receptorCell, 1989
- Ligand and protein kinase C downmodulate the colony-stimulating factor 1 receptor by independent mechanisms.Molecular and Cellular Biology, 1989
- Signal transduction from membrane to cytoplasm: growth factors and membrane-bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity.Proceedings of the National Academy of Sciences, 1988
- Isolation and characterization of a cloned growth factor dependent macrophage cell line, BAC1.2F5Journal of Cellular Physiology, 1987
- Structural alteration of viral homologue of receptor proto-oncogene fms at carboxyl terminusNature, 1986
- Chemical crosslinking of the mononuclear phagocyte specific growth factor CSF-1 to its receptor at the cell surfaceBiochemical and Biophysical Research Communications, 1984