Substrate specificities of insulin and epidermal growth factor receptor kinases
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference26 articles.
1. Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine.
2. Epidermal growth factor-receptor-protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity.
3. Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factor
4. The .beta. subunit of the insulin receptor kinase is an insulin-activated protein
5. Insulin-stimulated tyrosine protein kinase. Characterization and relation to the insulin receptor.
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1. Epidermal growth factor receptor-protein kinase interactions in hepatic membranes of rainbow trout (Oncorhynchus mykiss);Fish Physiology and Biochemistry;2000
2. Protein Phosphorylation and Dephosphorylation in Physiologic and Oncologic Processes;Critical Reviews™ in Oncogenesis;1996
3. Elevation of serum insulin concentration during euglycemic hyperinsulinemic clamp studies leads to similar activation of insulin receptor kinase in skeletal muscle of subjects with and without NIDDM;Diabetes;1995-11-01
4. Polyunsaturated fatty acid regulation of lipogenic enzyme gene expression in liver of genetically obese rat;Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism;1995-03
5. Stimulation of insulin receptor tyrosine kinase activity by an amino terminal sequence of human growth hormone;Life Sciences;1994-01
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