Beggah, A <br/><br/>
Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP.  [electronic resource] 

 -  The Journal of biological chemistry  Aug 1996 
 - 20895-902 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.271.34.20895  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Base Sequence<br/>Biological Transport<br/>Carrier Proteins--metabolism<br/>Cell Compartmentation<br/>Cloning, Molecular<br/>DNA Primers--chemistry<br/>DNA, Complementary--genetics<br/>Endoplasmic Reticulum Chaperone BiP<br/>Endoplasmic Reticulum, Rough--metabolism<br/>H(+)-K(+)-Exchanging ATPase--metabolism<br/>Heat-Shock Proteins<br/>Macromolecular Substances<br/>Molecular Chaperones--metabolism<br/>Molecular Sequence Data<br/>Oocytes<br/>Precipitin Tests<br/>Protein Binding<br/>Protein Folding<br/>Rats<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Sodium-Potassium-Exchanging ATPase--chemistry<br/>Xenopus laevis