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Browsing by Subject "Genes, Lethal"

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    • Article  

      A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the α1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen 

      Constantinou-Deltas, Constantinos D.; Nielsen, K. B.; Prockop, D. J. (1989)
      A fraction of the proα1(I) and proα2(I) chains in type I procollagen synthesized by the fibroblasts from a proband with a lethal variant of osteogenesis imperfecta were overmodified by posttranslational reactions. After ...

    • Article  

      Phenotypic heterogeneity in osteogenesis imperfecta: The mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for α1-glycine 904 in a type I procollagen gene (COL1A1) 

      Constantinou-Deltas, Constantinos D.; Pack, M. A.; Young, S. B.; Prockop, D. J. (1990)
      A proband with a lethal variant of osteogenesis imperfecta (OI) has been shown to have, in one allele in a gene for type I procollagen (COL1A1), a single base mutation that converted the codon for α1-glycine 904 to a codon ...

    • Article  

      A single base mutation in type I procollagen (COL1A1) that converts glycine α1-541 to aspartate in a lethal variant of osteogenesis imperfecta: Detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR 

      Zhuang, J.; Constantinou-Deltas, Constantinos D.; Ganguly, A.; Prockop, D. J. (1991)
      Skin fibroblasts from a proband with a lethal variant of osteogenesis imperfecta synthesized both apparently normal type I procollagen and a type I procollagen that had slow electrophoretic mobility because of posttranslational ...

    • Article  

      A single base mutation that converts glycine 907 of the α2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix 

      Baldwin, C. T.; Constantinou-Deltas, Constantinos D.; Dumars, K. W.; Prockop, D. J. (1989)
      Type I procollagen was examined in cultured skin fibroblasts from a patient with a lethal variant of osteogenesis imperfecta. About half of the pro-α chains were post-translationally overmodified and had a decreased thermal ...

    • Article  

      Substitutions for glycine α1-637 and glycine α2-694 of type I procollagen in lethal osteogenesis imperfecta: The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix 

      Tsuneyoshi, T.; Westerhausen, A.; Constantinou-Deltas, Constantinos D.; Prockop, D. J. (1991)
      Two substitutions for glycine in the triple-helical domain were found in type I procollagen synthesized by skin fibroblasts from two probands with lethal osteogenesis imperfecta. One was a substitution of valine for glycine ...

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