Mayer, M P <br/><br/>
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.  [electronic resource] 

 -  Nature structural biology  Jul 2000 
 - 586-93 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1072-8368 
<br/><br/><label>Standard No.: </label>10.1038/76819  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Diphosphate--metabolism<br/>Adenosine Triphosphatases--chemistry<br/>Adenosine Triphosphate--metabolism<br/>Allosteric Site--drug effects<br/>Bacterial Proteins--chemistry<br/>Catalytic Domain<br/>Enzyme Activation<br/>Escherichia coli--chemistry<br/>Escherichia coli Proteins<br/>Genetic Complementation Test<br/>HSP70 Heat-Shock Proteins--chemistry<br/>Heat-Shock Proteins--metabolism<br/>Hydrolysis--drug effects<br/>Kinetics<br/>Models, Biological<br/>Models, Molecular<br/>Molecular Chaperones--chemistry<br/>Mutation--genetics<br/>Phenotype<br/>Protein Binding--drug effects<br/>Protein Structure, Secondary--drug effects<br/>Sigma Factor<br/>Thermodynamics<br/>Transcription Factors--metabolism