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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., Barbra J. Starman, David Eyre, Harry Charbonneau, Maria Harrylock, Mary Ann Weis, Lester Weiss, John M. Graham Jr., Peter H. Byers
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., Barbra J. Starman, David Eyre, Harry Charbonneau, Maria Harrylock, Mary Ann Weis, Lester Weiss, John M. Graham Jr., Peter H. Byers
Dartmouth Scholarship
Skin fibroblasts grown from three individuals with osteogenesis imperfecta (OI) each synthesized a population of normal type I collagen molecules and additional molecules that had one or two alpha 1(I) chains that contained a cysteine residue within the triple-helical domain, a region from which cysteine normally is excluded. The patients had very different phenotypes. One patient with OI type I had a population of alpha 1(I) chains in which glycine at position 94 of the triple helix was substituted by cysteine; a patient with OI type III had a population of alpha 1(I) chains in which glycine at position 526 …