Increasing the cAMP content of IM-9 cells alters the phosphorylation state and protein kinase activity of the insulin receptor.
Open Access
- 1 March 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (7) , 3402-3407
- https://doi.org/10.1016/s0021-9258(17)35797-6
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Human insulin receptor and its relationship to the tyrosine kinase family of oncogenesNature, 1985
- Dual regulation of glycogen metabolism by insulin and insulin-like growth factors in human hepatoma cells (HEP-G2). Analysis with an anti-receptor monoclonal antibody.Journal of Clinical Investigation, 1984
- Phosphorylation and dephosphorylation of the insulin receptor: evidence against an intrinsic phosphatase activityBiochemistry, 1984
- Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta.Proceedings of the National Academy of Sciences, 1982
- Human Hepatocellular Carcinoma Cell Lines Secrete the Major Plasma Proteins and Hepatitis B Surface AntigenScience, 1980
- Controlled synthesis of HBsAg in a differentiated human liver carcinoma-derived cell lineNature, 1979
- Cellular transformation and the ‘morphologic phenotype’ of transformed cellsNature, 1978
- Cyclic AMP increases the concentration of insulin receptors in cultured fibroblasts and lymphocytesBiochemical and Biophysical Research Communications, 1977
- Role of Cyclic Nucleotides in Growth ControlAnnual Review of Biochemistry, 1975
- Solid Phase Peptide Synthesis. I. The Synthesis of a TetrapeptideJournal of the American Chemical Society, 1963