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Serine for glycine substitutions in the C-terminal third of the α1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta

✍ Scribed by Allan M. Lund; Flemming Skovby; Marianne Schwartz

Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
192 KB
Volume
9
Category
Article
ISSN
1059-7794

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(G586V) substitutions in the α1 and α2 c
(G586V) substitutions in the α1 and α2 chains of collagen I: Effect of α-chain stoichiometry on the phenotype of osteogenesis imperfecta?
✍ Allan M. Lund; Flemming Skovby; Marianne Schwartz 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 166 KB

Osteogenesis imperfecta (OI) is a congenital disease of connective tissue, most often caused by single amino acid substitutions of glycine residues within the triple helical region of collagen I. Collagen I consists of two alpha 1 chains and one alpha 2 chain. Thus, a substitution in the alpha 1(I)

Substitution of arginine for glycine at
Substitution of arginine for glycine at position 154 of the α1 chain of type I collagen in a variant of osteogenesis imperfecta: Comparison to previous cases with the same mutation
✍ Zhuang, Jiapiao; Tromp, Gerard; Kuivaniemi, Helena; Castells, Salvador; Prockop, 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 33 KB 👁 1 views

A substitution of arginine for glycine at amino acid position 154 of the al(1) collagen chain was found in a father and his three children. The phenotype of the patients includes manifestations of types I and IIUIV osteogenesis imperfecta, but appears to be milder than that of the previously describ