Characterization of purified insulin receptor subunits.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. The subunit structure of rat liver insulin receptor. Antibodies directed against the insulin-binding subunit.
2. Photoaffinity labeling of insulin receptor proteins of liver plasma membrane preparations
3. The subunit structure of the high affinity insulin receptor. Evidence for a disulfide-linked receptor complex in fat cell and liver plasma membranes.
4. The structure of insulin receptor and its subunits. Evidence for multiple nonreduced forms and a 210,000 possible proreceptor.
5. Subunit structure of insulin receptor of rat adipocytes as demonstrated by photoaffinity labeling
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1. Placental metabolism and its regulation in health and diabetes;Molecular Aspects of Medicine;1994-01
2. Differential insertion of insulin receptor complexes into Triton X-114 bilayer membranes. Evidence for a differential accessibility of the membrane-exposed receptor domain;European Journal of Biochemistry;1993-01
3. The cellular and physiological actions of insulin in the central nervous system;Neurochemistry International;1993-01
4. The native α2β2 tetramer is the only subunit structure of the insulin receptor in intact cells and purified receptor preparations;Archives of Biochemistry and Biophysics;1991-10
5. Substructural analysis of the insulin receptor by microsequence analyses of limited tryptic fragments isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence or presence of dithiothreitol.;Journal of Biological Chemistry;1990-10
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