{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,8]],"date-time":"2026-02-08T00:09:38Z","timestamp":1770509378948,"version":"3.49.0"},"reference-count":58,"publisher":"BMJ","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Med Genet"],"published-print":{"date-parts":[[1995,4]]},"abstract":"<jats:p>Perinatal lethal osteogenesis imperfecta is the result of heterozygous mutations of the COL1A1 and COL1A2 genes that encode the alpha 1(I) and alpha 2(I) chains of type I collagen, respectively. Point mutations resulting in the substitution of Gly residues in Gly-X-Y amino acid triplets of the triple helical domain of the alpha 1(I) or alpha 2(I) chains are the most frequent mutations. They interrupt the repetitive Gly-X-Y structure that is mandatory for the formation of a stable triple helix. Most babies have their own private de novo mutation. However, the recurrence rate is about 7% owing to germline mosaicism in one parent. The mutations act in a dominant negative manner as the mutant pro alpha chains are incorporated into type I procollagen molecules that also contain normal pro alpha chains. The abnormal molecules are poorly secreted, more susceptible to degradation, and impair the formation of the extracellular matrix. The collagen fibres are abnormally organised and mineralisation is impaired. The severity of the clinical phenotype appears to be related to the type of mutation, its location in the alpha chain, the surrounding amino acid sequences, and the level of expression of the mutant allele.<\/jats:p>","DOI":"10.1136\/jmg.32.4.284","type":"journal-article","created":{"date-parts":[[2008,11,10]],"date-time":"2008-11-10T15:23:16Z","timestamp":1226330596000},"page":"284-289","source":"Crossref","is-referenced-by-count":52,"title":["Perinatal lethal osteogenesis imperfecta."],"prefix":"10.1136","volume":"32","author":[{"given":"W G","family":"Cole","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R","family":"Dalgleish","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"239","published-online":{"date-parts":[[1995,4,1]]},"reference":[{"key":"ref_1","article-title":"type I collagen that is laid down in the ex-II (table). They alter sequences that are imtracellular matrix of the dermis, bone, dentine, portant in chain association, disulphide linking sclera, ligaments, and fascia, the tissues affected of the chains, and interactions with in OI","unstructured":"type I collagen that is laid down in the ex-II (table). They alter sequences that are imtracellular matrix of the dermis, bone, dentine, portant in chain association, disulphide linking sclera, ligaments, and fascia, the tissues affected of the chains, and interactions with in OI."},{"key":"ref_2","first-page":"101","article-title":"Genetic heterogeneity Med Genet","volume":"16","author":"D.M.","year":"1979","unstructured":"DM. Genetic heterogeneity Med Genet 1979;16:101-16."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"14751","DOI":"10.1016\/S0021-9258(17)36689-9","article-title":"Substitution of an aspartic acid for glycine 700 in the a2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone","volume":"269","author":"Cohen-Solal, L.; Zylberberg, L.; Sangalli, A.; Gomez Lira, M.; Mottes, M.","year":"1994","unstructured":"Cohen-Solal L, Zylberberg L, Sangalli A, Gomez Lira M, Mottes M. 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