Pincus, David <br/><br/>
BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response.  [electronic resource] 

 -  PLoS biology  Jul 2010 
 - e1000415 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. 
<br/><br/><label>ISSN: </label>1545-7885 
<br/><br/><label>Standard No.: </label>10.1371/journal.pbio.1000415  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Computational Biology<br/>Computer Simulation<br/>Endoplasmic Reticulum--enzymology<br/>Enzyme Activation<br/>Fluorescence Resonance Energy Transfer<br/>Fungal Proteins--metabolism<br/>HSP70 Heat-Shock Proteins--metabolism<br/>Homeostasis<br/>Kinetics<br/>Membrane Glycoproteins--chemistry<br/>Models, Biological<br/>Protein Binding<br/>Protein Serine-Threonine Kinases--chemistry<br/>Protein Structure, Quaternary<br/>Reproducibility of Results<br/>Saccharomyces cerevisiae--enzymology<br/>Saccharomyces cerevisiae Proteins--chemistry<br/>Stress, Physiological<br/>Time Factors<br/>Unfolded Protein Response