Megy, Simon <br/><br/>
STD and TRNOESY NMR studies for the epitope mapping of the phosphorylation motif of the oncogenic protein beta-catenin recognized by a selective monoclonal antibody.  [electronic resource] 

 -  FEBS letters  Oct 2006 
 - 5411-22 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/j.febslet.2006.08.084  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Motifs<br/>Antibodies, Monoclonal--chemistry<br/>Epitope Mapping--methods<br/>Epitopes--chemistry<br/>Humans<br/>Magnetic Resonance Spectroscopy--methods<br/>Models, Molecular<br/>Neoplasm Proteins--chemistry<br/>Neoplasms--metabolism<br/>Nuclear Magnetic Resonance, Biomolecular--methods<br/>Peptides--chemistry<br/>Phosphorylation<br/>Protein Processing, Post-Translational<br/>Protein Structure, Tertiary<br/>SKP Cullin F-Box Protein Ligases--chemistry<br/>Ubiquitin--metabolism<br/>beta Catenin--chemistry