Di Paolo, G <br/><br/>
Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin.  [electronic resource] 

 -  FEBS letters  Oct 1997 
 - 149-52 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0014-5793 
<br/><br/><label>Standard No.: </label>10.1016/s0014-5793(97)01188-5  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Binding Sites<br/>Brain--ultrastructure<br/>Calcium-Calmodulin-Dependent Protein Kinases--metabolism<br/>Cell Cycle<br/>Cloning, Molecular<br/>Cross-Linking Reagents<br/>Cyclic AMP-Dependent Protein Kinases--metabolism<br/>Cyclin-Dependent Kinases--metabolism<br/>Humans<br/>Kinetics<br/>Microtubule Proteins<br/>Microtubules--physiology<br/>Phosphoproteins--metabolism<br/>Phosphorylation<br/>Phosphoserine<br/>Proline<br/>Protein Kinases--metabolism<br/>Recombinant Proteins--metabolism<br/>Serine<br/>Stathmin<br/>Swine<br/>Tubulin--metabolism