Fujita-Yamaguchi, Y <br/><br/>
In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate.  [electronic resource] 

 -  Proceedings of the National Academy of Sciences of the United States of America  Oct 1989 
 - 7306-10 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0027-8424 
<br/><br/><label>Standard No.: </label>10.1073/pnas.86.19.7306  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Calmodulin--metabolism<br/>Cell Membrane--metabolism<br/>Female<br/>Humans<br/>Oncogene Protein p21(ras)--metabolism<br/>Phosphorylation<br/>Placenta--metabolism<br/>Polylysine--metabolism<br/>Pregnancy<br/>Protein-Tyrosine Kinases--isolation & purification<br/>Receptor, Insulin--metabolism<br/>Tyrosine