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The Interaction Between Sillence Type and BMD in Osteogenesis Imperfecta

✍ 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

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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

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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