• Biology, Medicine
  • Published in
    The Journal of biological…
    1988

Arginine for glycine substitution in the triple-helical domain of the products of one alpha 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype.

@article{Wenstrup1988ArginineFG,
  title={Arginine for glycine substitution in the triple-helical domain of the products of one alpha 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype.},
  author={Richard J. Wenstrup and Daniel H Cohn and Tova Cohen and Peter H Byers},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 16},
  pages={
          7734-40
        }
}
Skin fibroblasts from two affected members of a family with an autosomal dominant form of mild-moderate osteogenesis imperfecta produced two populations of type I collagen molecules. One population was normal and the other population contained alpha 2(I) chains which had a basic charge shift localized to a peptide from the carboxyl-terminal end of the triple-helical domain. The alpha chains in the abnormal molecules had increased post-translational modification along the entire triple-helical… CONTINUE READING

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References

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Metabolic and Genetic Diseases in Pediatrics

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