Mutants of collagen-specific molecular chaperone Hsp47 causing osteogenesis imperfecta are structurally unstable with weak binding affinity to collagen.

doi:10.1016/j.bbrc.2015.12.028

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Article

Mutants of collagen-specific molecular chaperone Hsp47 causing osteogenesis imperfecta are structurally unstable with weak binding affinity to collagen.

Biochemical and biophysical research communications - 15 Jan 2016

Ito Shinya, Nagata Kazuhiro

Abstract excerpt

Osteogenesis imperfecta (OI) is a genetic disorder characterized by fragile bones. Most OI cases are caused by defects in type I collagen structure or synthesis. Mutations in collagen specific molecular chaperone Hsp47, specifically L78P and L326P, lead to OI, yet these mutants are not fully characterized. Here, we found that both Hsp47 mutants were structurally unstable and formed high molecular weight...

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PMID: 26692483
DOI: 10.1016/j.bbrc.2015.12.028

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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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