A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.
about
FKBP65-dependent peptidyl-prolyl isomerase activity potentiates the lysyl hydroxylase 2-driven collagen cross-link switch.Heat shock protein 47 and 65 KDa FK506 binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.The fibrotic tumor stroma.Novel Mutations in PLOD2 Cause Rare Bruck Syndrome.FK506-binding protein 10 (FKBP10) regulates lung fibroblast migration via collagen VI synthesis.Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3
P2860
A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.
description
2017 nî lūn-bûn
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name
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@en
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@nl
type
label
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@en
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@nl
prefLabel
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@en
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@nl
P2093
P2860
P50
P356
P1476
A Chaperone Complex Formed by ...... ylation of Type I Procollagen.
@en
P2093
Brendan Lee
Caressa Lietman
Daniel H Cohn
David Eyre
Deborah Krakow
Jorge H Martin
Mary Ann Weis
Yasemin Alanay
P2860
P304
P356
10.1002/JBMR.3095
P577
2017-04-06T00:00:00Z