English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Fibroblasts from two affected members of a large pedigree in which osteogenesis imperfecta (OI) type IV is genetically linked to the pro alpha 2(I) gene of type I collagen synthesize two populations of pro alpha 2(I) chains. One population is normal; the second population appears to have a deletion of about 10 amino acid residues from the middle of the triple helical domain. The mutation in pro alpha 2(I) causes increased posttranslational modification in the amino-terminal half of some pro alpha 1(I) chains, lowers the melting temperature of type I collagen molecules that incorporate a mutant pro alpha 2(I) chain, and prevents or delays the secretion of those molecules from fibroblasts in cell culture. On the basis of this study and linkage studies in additional families, it appears that the OI type IV phenotype is often the result of heterozygosity for mutations in pro alpha 2(I) that alter the triple helical structure of type I collagen.

Osteogenesis imperfecta type IV. Biochemical confirmation of genetic linkage to the pro alpha 2(I) gene of type I collagen.