Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotype.

Samankaltaisia teoksia

• An osteopenic nonfracture syndrome with features of mild osteogenesis imperfecta associated with the substitution of a cysteine for glycine at triple helix position 43 in the pro alpha 1(I) chain of type I collagen.
  Tekijä: Shapiro, J R, et al.
  Julkaistu: (1992)
• Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.
  Tekijä: Culbert, A A, et al.
  Julkaistu: (1995)
• 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
  Tekijä: Makareeva, Elena, et al.
  Julkaistu: (2018)
• Substitution of cysteine for glycine at residue 415 of one allele of the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis imperfecta.
  Tekijä: Nicholls, A C, et al.
  Julkaistu: (1991)
• Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions.
  Tekijä: Baker, A T, et al.
  Julkaistu: (1989)