{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T17:51:24Z","timestamp":1788285084337,"version":"build-2803163510"},"reference-count":17,"publisher":"BMJ","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Med Genet"],"published-print":{"date-parts":[[2000,5,1]]},"abstract":"<jats:p>We report a unique glycine substitution in type I collagen and highlight the clinical and biochemical consequences. The proband is a 9 year old Turkish boy with severely deforming osteogenesis imperfecta (OI). Biochemical analysis of (pro) collagen type I from a skin fibroblast culture showed both normal and overmodified \u03b1 chains. Molecular analysis showed a G&gt;T transversion in the<jats:italic>COL1A2<\/jats:italic> gene, resulting in the substitution of glycine by tryptophan at position 277 of the \u03b12(I) collagen chain. Glycine substitutions in type I collagen are the most frequent cause of the severe and lethal forms of OI. The phenotypic severity varies according to the nature and localisation of the mutation. Substitutions of glycine by tryptophan, which is the most voluminous amino acid, have not yet been identified in type I collagen or any other fibrillar collagen. The severe, though non-lethal OI phenotype associated with this mutation may appear surprising in view of the huge size of the tryptophan residue. The fact that the mutation resides within a so called \u201cnon-lethal\u201d region of the \u03b12(I) collagen chain supports a regional model in phenotypic severity for \u03b12(I) collagen mutations, in which the phenotype is determined primarily by the nature of the collagen domain rather than the type of glycine substitution involved.<\/jats:p>","DOI":"10.1136\/jmg.37.5.371","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T06:38:40Z","timestamp":1027751920000},"page":"371-375","source":"Crossref","is-referenced-by-count":13,"title":["Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation"],"prefix":"10.1136","volume":"37","author":[{"given":"Lieve","family":"Nuytinck","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Turgut","family":"T\u00fckel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H\u00fclya","family":"Kayserili","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Memnune Y\u00fcksel","family":"Apak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"De Paepe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"239","published-online":{"date-parts":[[2000,5,1]]},"reference":[{"key":"2025101723475817000_37.5.371.1","doi-asserted-by":"publisher","DOI":"10.1136\/jmg.16.2.101"},{"key":"2025101723475817000_37.5.371.2","doi-asserted-by":"publisher","DOI":"10.1136\/jmg.29.6.375"},{"key":"2025101723475817000_37.5.371.3","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(81)90204-9"},{"key":"2025101723475817000_37.5.371.4","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/3.12.2201"},{"key":"2025101723475817000_37.5.371.5","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.21.10325"},{"key":"2025101723475817000_37.5.371.6","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/26.1.253"},{"key":"2025101723475817000_37.5.371.7","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/2.12.2175"},{"key":"2025101723475817000_37.5.371.8","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1159\/000484752","article-title":"Osteogenesis imperfecta phenotypes resulting from serine for glycine substitutions in the \u03b12(I) collagen chain.","volume":"5","author":"Nuytinck","year":"1997","journal-title":"Eur J Hum Genet"},{"key":"2025101723475817000_37.5.371.9","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1042\/bj2890195","article-title":"Two cysteine substitutions in procollagen I: a glycine replacement near the N-terminus of \u03b11(I) chain causes lethal osteogenesis imperfecta and a glycine replacement in the \u03b12(I) chain markedly destabilizes the triple helix.","volume":"289","author":"Fertala","year":"1993","journal-title":"Biochem J"},{"key":"2025101723475817000_37.5.371.10","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/2.8.1155"},{"key":"2025101723475817000_37.5.371.11","doi-asserted-by":"crossref","first-page":"10083","DOI":"10.1016\/S0021-9258(18)81769-0","article-title":"RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation.","volume":"264","author":"Patterson","year":"1989","journal-title":"J Biol Chem"},{"key":"2025101723475817000_37.5.371.12","doi-asserted-by":"publisher","DOI":"10.1136\/jmg.28.7.433"},{"key":"2025101723475817000_37.5.371.13","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1002\/(SICI)1098-1004(1999)13:6<503::AID-HUMU11>3.0.CO;2-L","article-title":"Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III. 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