A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta
- 1 August 1992
- journal article
- Published by Springer Nature in Human Genetics
- Vol. 89 (6) , 640-646
- https://doi.org/10.1007/bf00221955
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Brittle bones - fragile molecules: disorders of collagen gene structure and expressionPublished by Elsevier ,2002
- Bone disease cracks geneticsNature, 1990
- The clinical features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by arginine in the pro alpha 1(I) chain of type I procollagen.Journal of Medical Genetics, 1990
- Fibrillar Collagen Genes.Annals of the New York Academy of Sciences, 1990
- 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.Journal of Clinical Investigation, 1989
- Type I procollagen: The gene‐protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissueAmerican Journal of Medical Genetics, 1989
- A new lethal brittle bone syndrome with increased amount of type V collagen in a patientAmerican Journal of Medical Genetics, 1989
- Perinatal lethal osteogenesis imperfecta in transgenic mice bearing an engineered mutant pro-α1(I) collagen geneNature, 1988
- Abnormal procollagen synthesis in fibroblasts from three patients of the same family with a severe form of osteogenesis imperfecta (type III)Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1986
- Nucleotide sequences of complementary deoxyribonucleic acids for the pro.alpha.1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolutionBiochemistry, 1983