Vaughan, Cara K <br/><br/>
Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.  [electronic resource] 

 -  Molecular cell  Sep 2008 
 - 886-95 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1097-4164 
<br/><br/><label>Standard No.: </label>10.1016/j.molcel.2008.07.021  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Antibody Specificity<br/>Cell Cycle Proteins--metabolism<br/>Chaperonins--metabolism<br/>Cyclin-Dependent Kinase 4--metabolism<br/>Enzyme Activation<br/>HCT116 Cells<br/>HSP90 Heat-Shock Proteins--metabolism<br/>Humans<br/>Models, Biological<br/>Mutation--genetics<br/>Nuclear Proteins--metabolism<br/>Phosphoprotein Phosphatases--metabolism<br/>Phosphorylation<br/>Phosphoserine--metabolism<br/>Protein Binding<br/>Protein Kinases--metabolism<br/>Protein Phosphatase 1--metabolism<br/>Proto-Oncogene Proteins c-raf--metabolism<br/>Saccharomyces cerevisiae<br/>Substrate Specificity