Allan, Rudi K <br/><br/>
Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization.  [electronic resource] 

 -  The Journal of biological chemistry  Mar 2006 
 - 7161-71 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M512406200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alanine--chemistry<br/>Amino Acid Sequence<br/>Aminocoumarins--chemistry<br/>Anti-Bacterial Agents--chemistry<br/>Binding Sites<br/>Coumarins--chemistry<br/>DNA, Complementary--metabolism<br/>Dimerization<br/>Dose-Response Relationship, Drug<br/>Enzyme Inhibitors--chemistry<br/>Enzyme-Linked Immunosorbent Assay<br/>Glutathione Transferase--metabolism<br/>HSP90 Heat-Shock Proteins--chemistry<br/>HeLa Cells<br/>Humans<br/>Immunophilins--chemistry<br/>Molecular Chaperones--chemistry<br/>Molecular Conformation<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Mutation<br/>Novobiocin--chemistry<br/>Plasmids--metabolism<br/>Point Mutation<br/>Protein Binding<br/>Protein Conformation<br/>Protein Structure, Tertiary<br/>Steroids--chemistry<br/>Substrate Specificity<br/>Tacrolimus Binding Proteins--chemistry<br/>Time Factors