Krajewski, Wojciech W <br/><br/>
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.  [electronic resource] 

 -  Journal of molecular biology  Jan 2008 
 - 217-28 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1089-8638 
<br/><br/><label>Standard No.: </label>10.1016/j.jmb.2007.10.029  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphate--metabolism<br/>Amino Acid Sequence<br/>Animals<br/>Apoenzymes--chemistry<br/>Binding Sites<br/>Catalytic Domain<br/>Cloning, Molecular<br/>Crystallography, X-Ray<br/>Dogs<br/>Drug Design<br/>Drug Interactions<br/>Glutamate-Ammonia Ligase--chemistry<br/>Herbicides--chemical synthesis<br/>Humans<br/>Hydrogen Bonding<br/>Kinetics<br/>Ligands<br/>Magnesium--metabolism<br/>Models, Chemical<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Pharmaceutical Preparations--chemical synthesis<br/>Protein Binding<br/>Protein Conformation<br/>Protein Structure, Tertiary<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity<br/>Temperature