Wilson, Richard <br/><br/>
Misfolding of collagen X chains harboring Schmid metaphyseal chondrodysplasia mutations results in aberrant disulfide bond formation, intracellular retention, and activation of the unfolded protein response.  [electronic resource] 

 -  The Journal of biological chemistry  Apr 2005 
 - 15544-52 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.M410758200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Collagen Type X--genetics<br/>Cystine--genetics<br/>Endoplasmic Reticulum--metabolism<br/>Exostoses, Multiple Hereditary--genetics<br/>Genetic Markers<br/>Humans<br/>Molecular Sequence Data<br/>Mutation<br/>Protein Folding<br/>Protein Structure, Tertiary<br/>Tumor Cells, Cultured