The Interaction Between Sillence Type and BMD in Osteogenesis Imperfecta
β Scribed by D. J. Kok; C. S. P. M. Uiterwaal; A. J. Dongen; P. P. G. Kramer; H. E. H. Pruijs; R. H. H. Engelbert; A. J. Verbout; D. H. Schweitzer; R. J. B. Sakkers
- Book ID
- 105913089
- Publisher
- Springer
- Year
- 2003
- Tongue
- English
- Weight
- 188 KB
- Volume
- 73
- Category
- Article
- ISSN
- 1432-0827
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## Communicated by Peter Byers Osteogenesis imperfecta (OI) is caused by mutations in COL1A1 and COL1A2 that code for the a1 and a2 chains of type I collagen. Phenotypes correlate with the mutation types in that COL1A1 null mutations lead to OI type I, and structural mutations in a1(I) or a2(I) lea
The original article to which this Erratum refers was published in Human Mutation 24: 147-154 (2004). In Table 1 of the published original article, the fourth mutation should be c.913G4C (not c.913G4A as originally printed) and it should be bolded as it is a novel mutation. In addition, the last mu
Non-lethal OI III (OMIM 259420) is caused by structural aberrations of collagen I. We report four novel glycine substitutions, one in the Ξ± Ξ±1(I) chain of collagen I (G688S) and three in the Ξ± Ξ±2(I) chain (G241D, G247C, G883V). In each of two families (G241D and G883V), we found parental mosaicism f