ArticleBone reports2026
Post-translational modifications of collagen type I in osteogenesis imperfecta: Systematic review and meta-analysis.
Article in Bone reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Collagen secretion and maturation in osteogenesis imperfecta: Systematic review and meta-analysis.Bone reports · 2026Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Osteogenesis imperfecta (OI) is a rare genetic disorder most often caused by mutations in genes that encode collagen type I. OI collagen-I differs from healthy collagen-I due to the underlying mutation and altered post-translational modifications (PTMs). The objective of this study was to use knowledge synthesis to quantify the levels of selected PTMs, hydroxylysine (HYL), hydroxyproline (HYP) and glycosylation (GLY) in OI collagen-I. A systematic search in Medline, Ovid and Web of Science, identified 701 studies reporting on PTM outcomes for OI patients with collagen-I mutation. We excluded animal studies, and reports for OI patients with mutations other than in collagen-I. After screening, we included 36 qualitative studies and 25 quantitative studies for meta-analysis. All qualitative studies reported that OI collagen-I was overmodified. Meta-analysis of studies with quantitative data was performed using normalized mean difference as a study-level effect size and a random-effects model with the Hunter and Smith with sample size correction. The hydroxylysine dataset included 150 patients across 20 studies and had an effect size of 0.33 (confidence interval (CI) 0.21, 0.45). HYL levels were higher in bone-derived collagen-I than in fibroblast- or dentine-derived. The hydroxyproline dataset included 141 patients across 17 studies and had an effect size of 0.00 (CI: -0.02, 0.02). The glycosylation dataset included 17 patients across 5 studies and had an effect size of 0.55 (CI: 0.38, 0.71). Patients with the most severe form of OI (type 2) had the highest levels of collagen-I HYL and GLY. Our study provides new insights into collagen-I pathophysiology in OI, generating new hypotheses regarding the role of PTM in mediating disease presentation in different tissues and overall severity.
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