Toledo, Franck <br/><br/>
Mouse mutants reveal that putative protein interaction sites in the p53 proline-rich domain are dispensable for tumor suppression.  [electronic resource] 

 -  Molecular and cellular biology  Feb 2007 
 - 1425-32 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0270-7306 
<br/><br/><label>Standard No.: </label>10.1128/MCB.00999-06  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Apoptosis<br/>Binding Sites<br/>Cell Cycle<br/>Cell Proliferation<br/>Cell Transformation, Neoplastic<br/>Conserved Sequence<br/>DNA Damage<br/>Fibroblasts--cytology<br/>Gene Targeting<br/>Mice<br/>Mice, Mutant Strains<br/>Molecular Sequence Data<br/>Mutant Proteins--metabolism<br/>Neoplasms--pathology<br/>Point Mutation--genetics<br/>Proline--metabolism<br/>Protein Binding<br/>Protein Structure, Tertiary<br/>Recombination, Genetic--genetics<br/>Structure-Activity Relationship<br/>Transcriptional Activation--genetics<br/>Tumor Suppressor Protein p53--chemistry