Spiess, C <br/><br/>
A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.  [electronic resource] 

 -  Cell  Apr 1999 
 - 339-47 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0092-8674 
<br/><br/><label>Standard No.: </label>10.1016/s0092-8674(00)80743-6  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amylases--chemistry<br/>Bacterial Proteins--chemistry<br/>Chaperonins--metabolism<br/>DNA Primers<br/>Endopeptidases--metabolism<br/>Escherichia coli--chemistry<br/>Escherichia coli Proteins<br/>Gene Deletion<br/>Gene Expression Regulation, Bacterial<br/>Gene Expression Regulation, Enzymologic<br/>Heat-Shock Proteins<br/>In Vitro Techniques<br/>Lac Operon<br/>Mutation--physiology<br/>Periplasmic Proteins<br/>Protein Disulfide-Isomerases--genetics<br/>Protein Folding<br/>Serine Endopeptidases--chemistry<br/>Substrate Specificity<br/>Temperature<br/>Transcription, Genetic--physiology<br/>alpha-Amylases--metabolism