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Article

Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations.

Biochemistry - 13 May 2008

Bodian Dale L, Madhan Balaraman, Brodsky Barbara, Klein Teri E

Abstract excerpt

Osteogenesis imperfecta (OI), or brittle bone disease, often results from missense mutation of one of the conserved glycine residues present in the repeating Gly-X-Y sequence characterizing the triple-helical region of type I collagen. A composite model was developed for predicting the clinical lethality resulting from glycine mutations in the alpha1 chain of type I collagen. The lethality of mutations in which...

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Source

Identifiers

PMID: 18412368
DOI: 10.1021/bi800026k

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations.PMID 18412368Read ↗

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged SiteSemantic proximity Read ↗

Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Semantic proximity Read ↗

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.Semantic proximity Read ↗

Novel Mutations Within Collagen Alpha1(I) and Alpha2(I) Ligand-Binding Sites, Broadening the Spectrum of Osteogenesis Imperfecta – Current Insights Into Collagen Type I Lethal RegionsSemantic proximity Read ↗

Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta.Semantic proximity Read ↗

Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine.Semantic proximity Read ↗

Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Semantic proximity Read ↗

Local amino acid sequence patterns dominate the heterogeneous phenotype for the collagen connective tissue disease Osteogenesis Imperfecta resulting from Gly mutations.Semantic proximity Read ↗

A C-Propeptide Variant in COL1A1 Potentially Perturbing Disulfide Bonding in Osteogenesis Imperfecta Type III.Semantic proximity Read ↗

Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix.Semantic proximity Read ↗

Local sequence context determines the effect of glycine substitutions in collagen triple helicesSemantic proximity Read ↗

Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.Semantic proximity Read ↗

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