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Article

Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta.

PLoS genetics - 1 Jun 2014

Cabral Wayne A, Perdivara Irina, Weis MaryAnn, Terajima Masahiko, Blissett Angela R, Chang Weizhong, Perosky Joseph E, Makareeva Elena N, Mertz Edward L, Leikin Sergey, Tomer Kenneth B, Kozloff Kenneth M, Eyre David R, Yamauchi Mitsuo, Marini Joan C

Abstract excerpt

Cyclophilin B (CyPB), encoded by PPIB, is an ER-resident peptidyl-prolyl cis-trans isomerase (PPIase) that functions independently and as a component of the collagen prolyl 3-hydroxylation complex. CyPB is proposed to be the major PPIase catalyzing the rate-limiting step in collagen folding. Mutations in PPIB cause recessively inherited osteogenesis imperfecta type IX, a moderately severe to lethal bone...

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Share to Collagen
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Extracellular Matrix

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Source

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Identifiers

PMID: 24968150
DOI: 10.1371/journal.pgen.1004465
PMCID: PMC4072593

Genes

PPIB

Provenance

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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Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta.PMID 24968150Read ↗

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