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Article

Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta.

Human mutation - 1 Jan 1997

Lund A M, Skovby F, Schwartz M

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 9101304
DOI: 10.1002/(SICI)1098-1004(1997)9:4<378::AID-HUMU16>3.0.CO;2-#

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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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Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta.PMID 9101304Read ↗

Substitution of glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III.Semantic proximity Read ↗

Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity.Semantic proximity Read ↗

Osteogenesis imperfecta phenotypes resulting from serine for glycine substitutions in the alpha2(I) collagen chain.Semantic proximity Read ↗

Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology.Semantic proximity Read ↗

Genotype-phenotype correlations in nonlethal osteogenesis imperfecta caused by mutations in the helical domain of collagen type I.Semantic 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 ↗

A novel G1006A substitution in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III.Semantic proximity Read ↗

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

Mutational and structural characteristics of four novel heterozygous C-propeptide mutations in the proα1(I) collagen gene in Chinese osteogenesis imperfecta patients.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 ↗

Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype.Semantic proximity Read ↗

Disrupted growth plates and progressive deformities in osteogenesis imperfecta as a result of the substitution of glycine 585 by valine in the alpha 2 (I) chain of type I collagen.Semantic proximity Read ↗

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