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Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase.
Lightfoot SJ, Atkinson MS, Murphy G, Byers PH, Kadler KE. Lightfoot SJ, et al. Among authors: atkinson ms. J Biol Chem. 1994 Dec 2;269(48):30352-7. J Biol Chem. 1994. PMID: 7982948 Free article.
Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.
Culbert AA, Lowe MP, Atkinson M, Byers PH, Wallis GA, Kadler KE. Culbert AA, et al. Among authors: atkinson m. Biochem J. 1995 Nov 1;311 ( Pt 3)(Pt 3):815-20. doi: 10.1042/bj3110815. Biochem J. 1995. PMID: 7487936 Free PMC article.
Ehlers-Danlos syndrome type VIIA and VIIB result from splice-junction mutations or genomic deletions that involve exon 6 in the COL1A1 and COL1A2 genes of type I collagen.
Byers PH, Duvic M, Atkinson M, Robinow M, Smith LT, Krane SM, Greally MT, Ludman M, Matalon R, Pauker S, Quanbeck D, Schwarze U. Byers PH, et al. Among authors: atkinson m. Am J Med Genet. 1997 Oct 3;72(1):94-105. doi: 10.1002/(sici)1096-8628(19971003)72:1<94::aid-ajmg20>3.0.co;2-o. Am J Med Genet. 1997. PMID: 9295084
1,933 results