Subunit structure of the purified human placental insulin receptor. Intramolecular subunit dissociation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Open Access
- 1 July 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (14) , 8593-8600
- https://doi.org/10.1016/s0021-9258(17)39514-5
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Insulin Receptor Phosphorylation May Not Be a Prerequisite for Acute Insulin ActionScience, 1984
- Insulin receptor: insulin-modulated interconversion between distinct molecular forms involving disulfide sulfhydryl exchangeBiochemistry, 1983
- Insulin ReceptorsAnnual Review of Pharmacology and Toxicology, 1983
- Insulin receptor phosphorylation in intact adipocytes and in a cell-free systemBiochemical and Biophysical Research Communications, 1982
- Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own ReceptorScience, 1982
- The insulin receptor: structural featuresTrends in Biochemical Sciences, 1981
- Hormone Binding Alters the Conformation of the Insulin ReceptorScience, 1980
- Photoaffinity labeling of insulin receptor proteins of liver plasma membrane preparationsBiochemistry, 1980
- Insulin-induced dissociation of its receptor into subunits: Possible molecular concomitant of negative cooperativityBiochemical and Biophysical Research Communications, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970