Chapple, J Paul <br/><br/>
The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation.  [electronic resource] 

 -  The Journal of biological chemistry  May 2003 
 - 19087-94 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M212349200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphatases--metabolism<br/>Alternative Splicing<br/>Amino Acid Sequence<br/>Brain Chemistry<br/>Cell Fractionation<br/>Cell Line<br/>Cytoplasm--chemistry<br/>Endoplasmic Reticulum--chemistry<br/>Fluorescent Antibody Technique<br/>Gene Expression<br/>Green Fluorescent Proteins<br/>HSP40 Heat-Shock Proteins<br/>HSP70 Heat-Shock Proteins--metabolism<br/>Heat-Shock Proteins--chemistry<br/>Humans<br/>Immunosorbent Techniques<br/>Inclusion Bodies<br/>Luminescent Proteins--genetics<br/>Microscopy, Confocal<br/>Molecular Chaperones--chemistry<br/>Molecular Sequence Data<br/>Mutagenesis<br/>Photoreceptor Cells--chemistry<br/>Protein Folding<br/>Protein Isoforms--analysis<br/>Protein Prenylation<br/>Protein Processing, Post-Translational<br/>Recombinant Proteins<br/>Retina--chemistry<br/>Rhodopsin--chemistry<br/>Spinal Cord--chemistry<br/>Tissue Distribution<br/>Transfection