Ranganathan, R <br/><br/>
Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.  [electronic resource] 

 -  Cell  Jun 1997 
 - 875-86 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0092-8674 
<br/><br/><label>Standard No.: </label>10.1016/s0092-8674(00)80273-1  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Isomerases--chemistry<br/>Binding Sites--physiology<br/>Carrier Proteins--chemistry<br/>Cell Cycle--physiology<br/>Crystallography<br/>DNA-Binding Proteins--chemistry<br/>Endodeoxyribonucleases--chemistry<br/>Heat-Shock Proteins--chemistry<br/>Humans<br/>Mitosis--physiology<br/>Molecular Sequence Data<br/>NIMA-Interacting Peptidylprolyl Isomerase<br/>Peptidylprolyl Isomerase<br/>Phosphorylation<br/>Protein Conformation<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity<br/>Tacrolimus Binding Proteins