Taipale, Mikko <br/><br/>
Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells.  [electronic resource] 

 -  Nature biotechnology  Jul 2013 
 - 630-7 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>1546-1696 
<br/><br/><label>Standard No.: </label>10.1038/nbt.2620  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Cell Cycle Proteins--genetics<br/>Crizotinib<br/>Drug Approval<br/>Drug Interactions<br/>HSP90 Heat-Shock Proteins--metabolism<br/>Humans<br/>Mice<br/>Molecular Chaperones--metabolism<br/>Neoplasms--drug therapy<br/>Phosphotransferases--antagonists & inhibitors<br/>Protein Binding<br/>Protein Kinase Inhibitors--therapeutic use<br/>Proto-Oncogene Proteins c-ets--metabolism<br/>Pyrazoles--therapeutic use<br/>Pyridines--therapeutic use<br/>Receptor, trkC--metabolism<br/>Repressor Proteins--metabolism<br/>Substrate Specificity<br/>Xenograft Model Antitumor Assays<br/>ETS Translocation Variant 6 Protein