Wang, Huanchen <br/><br/>
Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities.  [electronic resource] 

 -  The Journal of biological chemistry  11 2017 
 - 18192-18202 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Intramural 
<br/><br/><label>ISSN: </label>1083-351X 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M117.801845  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Amino Acid Substitution<br/>Binding Sites<br/>Carbohydrate Conformation<br/>Catalytic Domain<br/>Conserved Sequence<br/>Crystallography, X-Ray<br/>Humans<br/>Inositol 1,4,5-Trisphosphate--chemistry<br/>Inositol Phosphates--chemistry<br/>Models, Molecular<br/>Mutagenesis, Site-Directed<br/>Mutation<br/>Phosphotransferases (Alcohol Group Acceptor)--chemistry<br/>Protein Conformation<br/>Protein Interaction Domains and Motifs<br/>Protein Structure, Secondary<br/>Recombinant Proteins--chemistry<br/>Sequence Alignment<br/>Substrate Specificity