Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Phenotypic variability and abnormal type I collagen unstable at body temperature in a family with mild dominant osteogenesis imperfecta.

Journal of inherited metabolic disease - 1 Jan 1991

Tenni R, Biglino P, Dyne K, Rossi A, Filocamo M, Pendola F, Brunelli P, Buttitta P, Borrone C, Cetta G

Abstract excerpt

Autosomal dominant inheritance of a mild form of osteogenesis imperfecta (osteogenesis imperfecta type I) with different phenotypic expression was found in a family. Phenotypic expression was different for the affected mother and son, in the presence of the same biochemical results. Dermal fibroblast cultures synthesized normal and mutant type I collagen alpha chains. Collagen heterotrimers containing abnormal...

Topics

Body Temperature
Cells, Cultured
Child, Preschool
Collagen
Cyanogen Bromide
Female
Fibroblasts
Humans
Macromolecular Substances
Male
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Osteogenesis Imperfecta

Pedigree

Phenotype

Protein Conformation

Protein Denaturation

Source

Identifiers

PMID: 1886404
DOI: 10.1007/BF01800591

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1886404-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phenotypic variability and abnormal type I collagen unstable at body temperature in a family with mild dominant osteogenesis imperfecta.PMID 1886404Read ↗

Moderately severe osteogenesis imperfecta: biochemical studies showing variable defect localization in the triple-helical domain of type I collagen.Semantic proximity Read ↗

Guilty by association: some collagen II mutants alter the formation of ECM as a result of atypical interaction with fibronectin.Semantic proximity Read ↗

Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene.Semantic proximity Read ↗

Phenotype variability in a daughter and father with mild osteogenesis imperfecta correlated with collagen and prolidase levels in cultured skin fibroblasts.Semantic proximity Read ↗

Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding.Semantic proximity Read ↗

Somatic cell mosaicism: another source of phenotypic heterogeneity in nuclear families with osteogenesis imperfecta.Semantic 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 ↗

Splice site mutation causing deletion of exon 21 sequences from the pro alpha 2(I) chain of type I collagen in a patient with severe dentinogenesis imperfecta but very mild osteogenesis imperfecta.Semantic proximity Read ↗

Recurrence of lethal osteogenesis imperfecta due to parental mosaicism for a mutation in the COL1A2 gene of type I collagen. The mosaic parent exhibits phenotypic features of a mild form of the disease.Semantic proximity Read ↗

A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase.Semantic proximity Read ↗

Reducing the effects of intracellular accumulation of thermolabile collagen II mutants by increasing their thermostability in cell culture conditions.Semantic proximity Read ↗

Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.