Maegawa, Ken-Ichi <br/><br/>
The Highly Dynamic Nature of ERdj5 Is Key to Efficient Elimination of Aberrant Protein Oligomers through ER-Associated Degradation.  [electronic resource] 

 -  Structure (London, England : 1993)  06 2017 
 - 846-857.e4 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>1878-4186 
<br/><br/><label>Standard No.: </label>10.1016/j.str.2017.04.001  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Crystallography, X-Ray<br/>Disulfides--chemistry<br/>Endoplasmic Reticulum Chaperone BiP<br/>Endoplasmic Reticulum-Associated Degradation--physiology<br/>HSP40 Heat-Shock Proteins--chemistry<br/>Heat-Shock Proteins--metabolism<br/>Humans<br/>Membrane Proteins--metabolism<br/>Microscopy, Atomic Force<br/>Models, Molecular<br/>Molecular Chaperones--chemistry<br/>Mutation<br/>Protein Conformation