Single base mutation in the type III procollagen gene that converts the codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos syndrome IV
Open Access
- 1 November 1989
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 264 (32) , 19313-19317
- https://doi.org/10.1016/s0021-9258(19)47303-1
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Osteogenesis Imperfecta: The Molecular Basis of Clinical HeterogeneityaAnnals of the New York Academy of Sciences, 1988
- Fidelity of DNA synthesis by the Thermus aquaticus DNA polymeraseBiochemistry, 1988
- Impaired secretion of type III procollagen in Ehlers-Danlos syndrome type IV fibroblasts: Correction of the defect by incubation at reduced temperature and demonstration of subtle alterations in the triple-helical region of the moleculeBiochemical and Biophysical Research Communications, 1988
- Enzymatic Amplification of β-Globin Genomic Sequences and Restriction Site Analysis for Diagnosis of Sickle Cell AnemiaScience, 1985
- A simple and very efficient method for generating cDNA librariesGene, 1983
- Conformational stability of type I collagen triple helix: Evidence for temporary and local relaxation of the protein conformation using a proteolytic probeArchives of Biochemistry and Biophysics, 1983
- Stability of ProteinsPublished by Elsevier ,1982
- Proteolytic enzymes as probes for the triple-helical conformation of procollagenAnalytical Biochemistry, 1981
- Thermal stability of type I and type III procollagens from normal human fibroblasts and from a patient with osteogenesis imperfecta.Proceedings of the National Academy of Sciences, 1980
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977