Insulin-induced Ca2+ entry in hepatocytes is important for PI 3-kinase activation, but not for insulin receptor and IRS-1 tyrosine phosphorylation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology
Reference67 articles.
1. After Insulin Binds
2. Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own Receptor
3. Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
4. Insulin receptors with defective tyrosine kinase inhibit normal receptor function at the level of substrate phosphorylation.
5. Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.
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3. Multiple Cross Talk between Angiotensin II, Bradykinin, and Insulin Signaling in the Cortical Thick Ascending Limb of Rat Kidney;Endocrinology;2010-07
4. Ca2+-permeable channels in the hepatocyte plasma membrane and their roles in hepatocyte physiology;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2008-05
5. Effects of tyroserleutide on gene expression of calmodulin and PI3K in hepatocellular carcinoma;Journal of Cellular Biochemistry;2008
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