Zhou, M <br/><br/>
Transient activation of a distinct serine protein kinase is responsible for 27-kDa heat shock protein phosphorylation in mitogen-stimulated and heat-shocked cells.  [electronic resource] 

 -  The Journal of biological chemistry  Jan 1993 
 - 35-43 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acid Phosphatase--metabolism<br/>Adenosine Triphosphate--metabolism<br/>Amino Acid Sequence<br/>Animals<br/>CHO Cells<br/>Chromatography<br/>Cricetinae<br/>Durapatite<br/>Enzyme Activation<br/>Fibroblast Growth Factor 2--pharmacology<br/>Heat-Shock Proteins--metabolism<br/>Hot Temperature<br/>Hydroxyapatites<br/>Intracellular Signaling Peptides and Proteins<br/>Kinetics<br/>Molecular Sequence Data<br/>Molecular Weight<br/>Peptides--pharmacology<br/>Phosphorylation<br/>Protein Serine-Threonine Kinases--antagonists & inhibitors<br/>Ribosomal Protein S6 Kinases<br/>Signal Transduction<br/>Substrate Specificity<br/>Thrombin--pharmacology<br/>Time Factors