Kubo, Y <br/><br/>
Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system.  [electronic resource] 

 -  Journal of molecular biology  Feb 1999 
 - 447-64 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.1998.2465  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphate--physiology<br/>Bacterial Proteins--genetics<br/>Calcium-Transporting ATPases<br/>Cell-Free System<br/>Cytosol--metabolism<br/>Escherichia coli Proteins<br/>Fungal Proteins--chemistry<br/>Genes, Reporter<br/>HSP40 Heat-Shock Proteins<br/>HSP70 Heat-Shock Proteins--genetics<br/>Heat-Shock Proteins--genetics<br/>Hot Temperature<br/>Kinetics<br/>Luciferases--chemistry<br/>Macromolecular Substances<br/>Membrane Proteins--genetics<br/>Membrane Transport Proteins<br/>Mitochondria--chemistry<br/>Mitochondrial Membrane Transport Proteins<br/>Models, Biological<br/>Molecular Chaperones--physiology<br/>Protein Conformation<br/>Protein Denaturation<br/>Protein Folding<br/>Recombinant Fusion Proteins--chemistry<br/>Saccharomyces cerevisiae--physiology<br/>Saccharomyces cerevisiae Proteins