Sung, Nuri <br/><br/>
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.  [electronic resource] 

 -  Proceedings of the National Academy of Sciences of the United States of America  Mar 2016 
 - 2952-7 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. 
<br/><br/><label>ISSN: </label>1091-6490 
<br/><br/><label>Standard No.: </label>10.1073/pnas.1516167113  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphate--chemistry<br/>Allosteric Regulation<br/>Allosteric Site<br/>Amino Acid Motifs<br/>Amino Acid Sequence<br/>Amino Acid Substitution<br/>Animals<br/>Binding Sites<br/>Computer Simulation<br/>Crystallography, X-Ray<br/>HSP70 Heat-Shock Proteins--metabolism<br/>HSP90 Heat-Shock Proteins--chemistry<br/>Humans<br/>Mitochondria--metabolism<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Protein Binding<br/>Protein Conformation<br/>Protein Folding<br/>Rabbits<br/>Recombinant Fusion Proteins--chemistry<br/>Sequence Homology, Amino Acid