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={John F Bateman and Ines Moeller and M Hannagan and Daniel W.M. Chan and William G. Cole},
  journal={The Biochemical journal},
  year={1992},
  volume={288 ( Pt 1)},
  pages={
          131-5
        }
}
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

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-9 OF 9 CITATIONS

Variable expressivity of osteogenesis imperfecta in a Brazilian family due to p.G1079S mutation in the COL1A1 gene.

VIEW 5 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED