Phorbol ester-mediated protein kinase C interaction with wild-type and COOH-terminal truncated insulin receptors.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity.
2. Phorbol esters modulate insulin receptor phosphorylation and insulin action in cultured hepatoma cells.
3. Phosphorylation of receptors for insulin and insulin-like growth factor I. Effects of hormones and phorbol esters.
4. Tumour-promoting phorbol esters increase basal and inhibit insulin-stimulated lipogenesis in rat adipocytes without decreasing insulin binding
5. Phorbolesters enhance basal D-glucose transport but inhibit insulin stimulation of D-glucose transport and insulin binding in isolated rat adipocytes
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1. Insulin resistance and adipogenesis: Role of transcription and secreted factors;Biochemistry (Moscow);2013-01
2. Mechanisms for Insulin Resistance: Common Threads and Missing Links;Cell;2012-03
3. Lipid-induced insulin resistance: unravelling the mechanism;The Lancet;2010-06
4. C-Terminus or Juxtamembrane Deletions in the Insulin Receptor do not Affect the Glucose-Dependent Inhibition of the Tyrosine Kinase Activity;European Journal of Biochemistry;2008-06-28
5. Inhibition of protein kinase Cε prevents hepatic insulin resistance in nonalcoholic fatty liver disease;Journal of Clinical Investigation;2007-03-01
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