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.

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 cys...

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Detalhes bibliográficos

Publicado no:	J Clin Invest
Principais autores:	Starman, B J, Eyre, D, Charbonneau, H, Harrylock, M, Weis, M A, Weiss, L, Graham, J M, Byers, P H
Formato:	Artigo
Idioma:	Inglês
Publicado em:	American Society for Clinical Investigation 1989
Assuntos:	Research Article
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC329779/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2794057/ https://ncbi.nlm.nih.govhttps://doi.org/10.1172/JCI114286
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