Drees, B L <br/><br/>
The GCN4 leucine zipper can functionally substitute for the heat shock transcription factor's trimerization domain.  [electronic resource] 

 -  Journal of molecular biology  Oct 1997 
 - 61-74 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.1997.1283  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Binding Sites<br/>Cross-Linking Reagents--metabolism<br/>DNA--metabolism<br/>DNA-Binding Proteins--chemistry<br/>Electrophoresis, Polyacrylamide Gel<br/>Escherichia coli--genetics<br/>Fungal Proteins--chemistry<br/>Gene Expression<br/>Heat Shock Transcription Factors<br/>Leucine Zippers<br/>Models, Molecular<br/>Nucleic Acid Conformation<br/>Point Mutation<br/>Protein Conformation<br/>Protein Kinases--chemistry<br/>Protein Structure, Secondary<br/>Recombinant Fusion Proteins--chemistry<br/>Saccharomyces cerevisiae--chemistry<br/>Saccharomyces cerevisiae Proteins<br/>Succinimides--metabolism<br/>Transcription Factors--chemistry