Phosphorylation of the insulin receptor by casein kinase I
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
1. Photoaffinity labeling of insulin receptor proteins of liver plasma membrane preparations
2. The subunit structure of rat liver insulin receptor. Antibodies directed against the insulin-binding subunit.
3. The subunit structure of the high affinity insulin receptor. Evidence for a disulfide-linked receptor complex in fat cell and liver plasma membranes.
4. Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries.
5. A unique proteolytic cleavage site on the beta subunit of the insulin receptor.
Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Serine Phosphorylation of the Ligand-activated β-Platelet-derived Growth Factor Receptor by Casein Kinase I-γ2 Inhibits the Receptor's Autophosphorylating Activity;Journal of Biological Chemistry;1999-07
2. A casein kinase I motif present in the cytoplasmic domain of members of the tumour necrosis factor ligand family is implicated in `reverse signalling';The EMBO Journal;1999-04-15
3. Casein Kinase I;Cellular Signalling;1998-11
4. Substrates for Protein Kinase CK2 in Insulin Receptor Preparations from Rat Liver Membranes: Identification of a 210-kDa Protein Substrate as the Dimeric Form of Endoplasmin;Archives of Biochemistry and Biophysics;1997-08
5. A Casein Kinase I Activity Is Constitutively Associated with Nck;Journal of Biological Chemistry;1997-01
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