Zavilgelsky, G B <br/><br/>
Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB) chaperones in refolding and increased thermal stability of bacterial luciferases in Escherichia coli cells.  [electronic resource] 

 -  Biochemistry. Biokhimiia  Sep 2002 
 - 986-92 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-2979 
<br/><br/><label>Standard No.: </label>10.1023/a:1020565701210  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphatases--metabolism<br/>Bacterial Proteins--metabolism<br/>Carbonyl Cyanide m-Chlorophenyl Hydrazone--pharmacology<br/>Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone--pharmacology<br/>Enzyme Stability<br/>Escherichia coli--enzymology<br/>HSP70 Heat-Shock Proteins--metabolism<br/>Heat-Shock Proteins--genetics<br/>Hot Temperature<br/>Kinetics<br/>Luciferases--metabolism<br/>Luminescent Measurements<br/>Molecular Chaperones--metabolism<br/>Oxidative Phosphorylation--drug effects<br/>Photorhabdus--enzymology<br/>Plasmids<br/>Protein Renaturation