{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,25]],"date-time":"2023-10-25T05:46:54Z","timestamp":1698212814201},"reference-count":11,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,6,7]],"date-time":"2005-06-07T00:00:00Z","timestamp":1118102400000},"content-version":"vor","delay-in-days":4526,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Am. J. Med. Genet."],"published-print":{"date-parts":[[1993,1,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We have examined the type I collagen protein, RNA, and cDNA of 2 children with moderately severe (type IV) osteogenesis imperfecta (OI). They have in common a non\u2010lethal form of OI with ambulatory potential, over\u2010modification of type I collagen protein, and a substitution of serine for glycine in the collagen chain produced by one \u03b11(I) allele.<\/jats:p><jats:p>The first child (Marini et al.: <jats:italic>J Biol Chem<\/jats:italic> 264:11893\u201011900, 1989) is now 7 years old, with the height of a 3\u2010year\u2010old. Her course includes significant remodeling of lower long bones and 4 femur fractures. She walks independently. A mishmatch was detected in her \u03b11(I) mRNA using RNA\/RNA hybrids; it was demonstrated to be due to a G\u2192A point mutation in one allele of \u03b11(I), resulting in the substitution of serine for glycine 832.<\/jats:p><jats:p>The second child is now 6\u00bd years old, with the height of 1\u00bd\u2010year\u2010old. Her history includes significant bowing of femurs and tibias, 6 femur fractures, S\u2010curve scoliosis, compression of all lumbar vertebrae, and limited short\u2010distance walking with braces. Her \u03b11(I) mRNA has also been studied by RNA hybrid analysis; there is a single G\u2192A change in one \u03b11(I) allele causing the substitution of serine for gly 352.<\/jats:p><jats:p>Both children have moderately severe OI. However, the serine substitution at gly 352 is associated with a more severe phenotype then is the serine substitution at gly 832. Compared to substitutions described in other cases of OI, the serine 352 is located in the middle of a cluster of cysteine substitutions associated with non\u2010lethal OI. The ser 832 is located near another non\u2010lethal substitution of serine for glycine but is otherwise flanked by lethal sub\u2010stitutions. These data support a model of OI cause in which crucial and non\u2010crucial regions are interspersed along the type I collagen chain. Whether a mutation located in a particular region causes OI type II or OI type IV would then depend on the importance of that region for the interaction of type I collagen with other matrix components or for intracellular processing.<\/jats:p>","DOI":"10.1002\/ajmg.1320450217","type":"journal-article","created":{"date-parts":[[2005,6,11]],"date-time":"2005-06-11T16:39:13Z","timestamp":1118507953000},"page":"241-245","source":"Crossref","is-referenced-by-count":3,"title":["Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the \u03b11(I) chain of type I collagen"],"prefix":"10.1002","volume":"45","author":[{"given":"Joan C.","family":"Marini","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mary Beth","family":"Lewis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kathleen","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,6,7]]},"reference":[{"key":"e_1_2_1_2_1","first-page":"503","article-title":"A single base mutation that converts the codon for glycine 907 of the \u03b1 2(I) chain of type I procollagen to aspartate. The single amino acid substitution in itself destabilizes the triple helix","volume":"8","author":"Baldwin CT","year":"1988","journal-title":"Collagen Relat Res"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"1734","DOI":"10.1016\/S0021-9258(18)89655-7","article-title":"Altered triplical helical structure of type I procollagen is associated with prolonged survival in lethal perinatal osteogenesis imperfecta","volume":"260","author":"Bonadio J","year":"1985","journal-title":"J Biol Chem"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/18.14.4227"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)71548-2"},{"key":"e_1_2_1_6_1","doi-asserted-by":"crossref","first-page":"11893","DOI":"10.1016\/S0021-9258(18)80150-8","article-title":"Osteogenesis Imperfecta Type IV","volume":"264","author":"Marini JC","year":"1989","journal-title":"J Biol Chem."},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"19694","DOI":"10.1016\/S0021-9258(19)47168-8","article-title":"Substitution of serine for \u03b1 1(I) glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen","volume":"264","author":"Pack M","year":"1989","journal-title":"J Biol Chem"},{"key":"e_1_2_1_8_1","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1016\/S0021-9258(18)94257-2","article-title":"Decreased thermal denaturation of osteogenesis imperfecta mutant collagen is independent of post\u2010translational overmodificatiuon of lysine and hydroxylysine","volume":"264","author":"Rao VH","year":"1989","journal-title":"J Biol Chem"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2999980"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI114286"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0934-8832(11)80133-2"},{"key":"e_1_2_1_12_1","doi-asserted-by":"crossref","first-page":"7734","DOI":"10.1016\/S0021-9258(18)68560-6","article-title":"Arginine for glycine substitution in the triple helical domain of the products of one \u03b1 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype","volume":"263","author":"Wenstrup RJ","year":"1988","journal-title":"J Biol Chem"}],"container-title":["American Journal of Medical Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fajmg.1320450217","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/ajmg.1320450217","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,24]],"date-time":"2023-10-24T19:46:00Z","timestamp":1698176760000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/ajmg.1320450217"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,1,15]]},"references-count":11,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1993,1,15]]}},"alternative-id":["10.1002\/ajmg.1320450217"],"URL":"https:\/\/doi.org\/10.1002\/ajmg.1320450217","archive":["Portico"],"relation":{},"ISSN":["0148-7299","1096-8628"],"issn-type":[{"value":"0148-7299","type":"print"},{"value":"1096-8628","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,1,15]]}}}