Separate effects of Mg2+, MgATP, and ATP4− on the kinetic mechanism for insulin receptor tyrosine kinase
- 1 April 1990
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 278 (1) , 99-105
- https://doi.org/10.1016/0003-9861(90)90236-r
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Design of a selective insulin receptor tyrosine kinase inhibitor and its effect on glucose uptake and metabolism in intact cellsBiochemistry, 1989
- Role of divalent metals in the kinetic mechanism of insulin receptor tyrosine kinaseArchives of Biochemistry and Biophysics, 1988
- Role of divalent metals in the activation and regulation of insulin receptor tyrosine kinaseBiosystems, 1988
- Phosphorylation of glycolytic and gluconeogenic enzymes by the insulin receptor kinaseJournal of Cellular Biochemistry, 1987
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- Phosphorylation of fodrin (nonerythroid spectrin) by the purified insulin receptor kinaseBiochemical and Biophysical Research Communications, 1985
- Substrate specificities of insulin and epidermal growth factor receptor kinasesBiochemical and Biophysical Research Communications, 1985
- Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own ReceptorScience, 1982
- Binding of insulin receptors to lectins: evidence for common carbohydrate determinants on several membrane receptorsBiochemistry, 1981
- METAL CHELATES OF ADENOSINE TRIPHOSPHATE1The Journal of Physical Chemistry, 1962