Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. Comparison to epidermal growth factor-stimulated phosphorylation.
Open Access
- 1 December 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (24), 15162-15166
- https://doi.org/10.1016/s0021-9258(18)33407-0
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- The insulin-directed phosphorylation site on ATP-citrate lyase is identical with the site phosphorylated by the cAMP-dependent protein kinase in vitro.Published by Elsevier ,1982
- Epidermal growth factor stimulates the phosphorylation of synthetic tyrosine-containing peptides by A431 cell membranes.Proceedings of the National Academy of Sciences, 1982
- A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles.Journal of Biological Chemistry, 1982
- Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own ReceptorScience, 1982
- THE INSULIN-DIRECTED PHOSPHORYLATION SITE ON ATP-CITRATE LYASE IS IDENTICAL WITH THE SITE PHOSPHORYLATED BY THE CAMP-DEPENDENT PROTEIN-KINASE INVITRO1982
- A rapid and convenient method for preparing salt-free [γ-32P]ATPAnalytical Biochemistry, 1981
- Regulation of plasma membrane protein phosphorylation in two mammalian cell typesJournal of Cellular Physiology, 1976
- Isolation of the Insulin Receptor of Liver and Fat-Cell MembranesProceedings of the National Academy of Sciences, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970