Inhibition of the activation and catalytic activity of insulin receptor kinase by zinc and other divalent metal ions.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference35 articles.
1. Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta.
2. Phosphorylation activates the insulin receptor tyrosine protein kinase.
3. Tyrosine-specific protein kinase activity is associated with the purified insulin receptor.
4. Receptor-mediated phosphorylation of the hepatic insulin receptor: Evidence that the Mr 95,000 receptor subunit is its own kinase
5. The .beta. subunit of the insulin receptor kinase is an insulin-activated protein
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1. Role of Zinc and Magnesium Ions in the Modulation of Phosphoryl Transfer in Protein Tyrosine Phosphatase 1B;Journal of the American Chemical Society;2018-03-07
2. Cell-type-specific roles of IGF-1R and EGFR in mediating Zn2+-induced ERK1/2 and PKB phosphorylation;JBIC Journal of Biological Inorganic Chemistry;2009-11-28
3. A Combination of Zinc and Pyridoxine Supplementation to the Diet of Laying Hens Improves Performance and Egg Quality;Biological Trace Element Research;2008-08-22
4. Zinc in a Combination with Magnesium Helps Reducing Negative Effects of Heat Stress in Quails;Biological Trace Element Research;2008-01-10
5. Potential interactions of zinc in the neuroendocrine-endocrine disturbances of diabetes mellitus type 2;Canadian Journal of Physiology and Pharmacology;1999-11-15
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