Lietha, D <br/><br/>
Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.  [electronic resource] 

 -  The EMBO journal  Oct 2001 
 - 5543-55 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0261-4189 
<br/><br/><label>Standard No.: </label>10.1093/emboj/20.20.5543  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Binding Sites<br/>Cell Line<br/>Crystallography, X-Ray<br/>Dimerization<br/>Dogs<br/>Drug Design<br/>Heparin--chemistry<br/>Heparitin Sulfate--metabolism<br/>Hepatocyte Growth Factor--chemistry<br/>Humans<br/>Kidney<br/>Kringles<br/>Macromolecular Substances<br/>Models, Molecular<br/>Mutagenesis, Site-Directed<br/>Peptide Fragments--chemistry<br/>Protein Binding<br/>Protein Conformation<br/>Protein Structure, Tertiary<br/>Proto-Oncogene Proteins c-met--antagonists & inhibitors<br/>RNA Splicing<br/>Recombinant Fusion Proteins--chemistry<br/>Structure-Activity Relationship