Duran, Ivan <br/><br/>
A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.  [electronic resource] 

 -  Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research  Jun 2017 
 - 1309-1319 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>1523-4681 
<br/><br/><label>Standard No.: </label>10.1002/jbmr.3095  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Cell Line<br/>Collagen Type I--metabolism<br/>Endoplasmic Reticulum Chaperone BiP<br/>Enzyme Stability<br/>HSP47 Heat-Shock Proteins--metabolism<br/>Heat-Shock Proteins--metabolism<br/>Humans<br/>Hydroxylation<br/>Lysine--metabolism<br/>Mass Spectrometry<br/>Mice<br/>Models, Biological<br/>Multiprotein Complexes--metabolism<br/>Mutation--genetics<br/>Peptides--metabolism<br/>Procollagen--metabolism<br/>Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase--metabolism<br/>Surface Plasmon Resonance<br/>Tacrolimus Binding Proteins--metabolism