A heterozygous defect for structurally altered pro-alpha 2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinase.
Open Access
- 1 November 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (22) , 14094-14100
- https://doi.org/10.1016/s0021-9258(18)89861-1
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Heritable Diseases of CollagenNew England Journal of Medicine, 1984
- 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
- Internal deletion in a collagen gene in a perinatal lethal form of osteogenesis imperfectaNature, 1983
- Abnormal alpha 2-chain in type I collagen from a patient with a form of osteogenesis imperfecta.Journal of Clinical Investigation, 1983
- Procollagen N‐ProteinaseEuropean Journal of Biochemistry, 1982
- A new type of osteogenesis imperfecta.Journal of Medical Genetics, 1982
- Formation of the Triple Helix of Type I Procollagen in cellulo. A Kinetic Model Based on cis-trans Isomerization of Peptide BondsEuropean Journal of Biochemistry, 1981
- Familial dentinogenesis imperfecta, blue sclerae, and wormian bones without fractures: another type of osteogenesis imperfecta?Journal of Medical Genetics, 1981
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- The estimation of two collagens from human dermis by interrupted gel electrophoresisBiochemical and Biophysical Research Communications, 1976