Effect of phenylarsine oxide on insulin-dependent protein phosphorylation and glucose transport in 3T3-L1 adipocytes.
Open Access
- 1 July 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (20) , 9872-9876
- https://doi.org/10.1016/s0021-9258(18)48014-3
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.Proceedings of the National Academy of Sciences, 1987
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- Kinetic evidence for activating and non-activating components of autophosphorylation of the insulin receptor protein kinaseBiochemical and Biophysical Research Communications, 1986
- Insulin action is blocked by a monoclonal antibody that inhibits the insulin receptor kinase.Proceedings of the National Academy of Sciences, 1986
- Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cellsNature, 1985
- Phosphorylation activates the insulin receptor tyrosine protein kinase.Proceedings of the National Academy of Sciences, 1983
- The .beta. subunit of the insulin receptor kinase is an insulin-activated proteinBiochemistry, 1983
- [42] Detection and quantification of phosphotyrosine in proteinsPublished by Elsevier ,1983
- Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site.Proceedings of the National Academy of Sciences, 1980
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959