Shohat, G <br/><br/>
The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism.  [electronic resource] 

 -  The Journal of biological chemistry  Dec 2001 
 - 47460-7 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>Standard No.: </label>10.1074/jbc.M105133200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Motifs<br/>Amino Acid Sequence<br/>Animals<br/>Apoptosis<br/>Apoptosis Regulatory Proteins<br/>Aspartic Acid--genetics<br/>Binding Sites<br/>Blotting, Western<br/>Calcium--metabolism<br/>Calcium-Calmodulin-Dependent Protein Kinases--chemistry<br/>Calmodulin--metabolism<br/>Catalysis<br/>Catalytic Domain<br/>Cell Death<br/>Cell Line<br/>Ceramides--chemistry<br/>Death-Associated Protein Kinases<br/>Electrophoresis, Polyacrylamide Gel<br/>Green Fluorescent Proteins<br/>HeLa Cells<br/>Humans<br/>Immunoblotting<br/>Luminescent Proteins--metabolism<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutation<br/>Phosphorylation<br/>Plasmids--metabolism<br/>Precipitin Tests<br/>Protein Binding<br/>Protein Structure, Tertiary<br/>Sequence Homology, Amino Acid<br/>Serine--chemistry<br/>Transfection