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Article

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

Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research - 1 Jun 2017

Duran Ivan, Martin Jorge H, Weis Mary Ann, Krejci Pavel, Konik Peter, Li Bing, Alanay Yasemin, Lietman Caressa, Lee Brendan, Eyre David, Cohn Daniel H, Krakow Deborah

Abstract excerpt

Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue, and these distinct hydroxylation patterns modulate collagen cross-linking to generate a unique extracellular matrix. Abnormalities in these patterns contribute to pathologies that include osteogenesis imperfecta (OI), fibrosis, and cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2); however,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 28177155
DOI: 10.1002/jbmr.3095
PMCID: PMC5466459

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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