A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.

Duran, Ivan

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

Publication Type: Journal Article

1523-4681

10.1002/jbmr.3095 doi


Animals
Cell Line
Collagen Type I--metabolism
Endoplasmic Reticulum Chaperone BiP
Enzyme Stability
HSP47 Heat-Shock Proteins--metabolism
Heat-Shock Proteins--metabolism
Humans
Hydroxylation
Lysine--metabolism
Mass Spectrometry
Mice
Models, Biological
Multiprotein Complexes--metabolism
Mutation--genetics
Peptides--metabolism
Procollagen--metabolism
Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase--metabolism
Surface Plasmon Resonance
Tacrolimus Binding Proteins--metabolism