• DOI:10.1042/BJ2880131
Corpus ID: 31305884

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

@article{Bateman1992CharacterizationOT,
  title={Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity.},
  author={J. Bateman and I. Moeller and M. Hannagan and D. Chan and W. Cole},
  journal={The Biochemical journal},
  year={1992},
  volume={288 ( Pt 1)},
  pages={
          131-5
        }
}

J. Bateman, I. Moeller, +2 authors W. Cole

Published 1992

Biology, Medicine

The Biochemical journal

Type I collagen alpha 1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI). The Gly substitutions displayed a gradient of phenotypic severity according to the location of the mutation in the collagen triple helix. The most C-terminal of these, Gly565 to Ser, led to the lethal perinatal (type II) form of OI, whereas the more N-terminal mutations, Gly415 and Gly352 to Ser, led to severe OI (type III/IV) and moderate OI… CONTINUE READING

View on PubMed

europepmc.org

Save to Library

Create Alert

Cite

Launch Research Feed