{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T11:49:16Z","timestamp":1785152956621,"version":"3.55.0"},"reference-count":23,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,7,19]],"date-time":"2013-07-19T00:00:00Z","timestamp":1374192000000},"content-version":"vor","delay-in-days":534,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The American Journal of Human Genetics"],"published-print":{"date-parts":[[2012,2]]},"DOI":"10.1016\/j.ajhg.2011.12.024","type":"journal-article","created":{"date-parts":[[2012,2,2]],"date-time":"2012-02-02T19:22:57Z","timestamp":1328210577000},"page":"363-368","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":67,"title":["DDOST Mutations Identified by Whole-Exome Sequencing Are Implicated in Congenital Disorders of Glycosylation"],"prefix":"10.1016","volume":"90","author":[{"given":"Melanie\u00a0A.","family":"Jones","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bobby\u00a0G.","family":"Ng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shruti","family":"Bhide","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ephrem","family":"Chin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Devin","family":"Rhodenizer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ping","family":"He","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-Estelle","family":"Losfeld","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miao","family":"He","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kimiyo","family":"Raymond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerard","family":"Berry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hudson\u00a0H.","family":"Freeze","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Madhuri\u00a0R.","family":"Hegde","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ajhg.2011.12.024_bib1","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/j.bbadis.2008.11.002","article-title":"Glycosylation diseases: Quo vadis?","volume":"1792","author":"Schachter","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ajhg.2011.12.024_bib2","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1007\/s10545-011-9299-3","article-title":"Congenital disorders of glycosylation (CDG): It's (nearly) all in it!","volume":"34","author":"Jaeken","year":"2011","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.ajhg.2011.12.024_bib3","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev.genom.8.080706.092327","article-title":"Congenital disorders of glycosylation: A rapidly expanding disease family","volume":"8","author":"Jaeken","year":"2007","journal-title":"Annu. Rev. Genomics Hum. Genet."},{"key":"10.1016\/j.ajhg.2011.12.024_bib4","doi-asserted-by":"crossref","DOI":"10.1007\/s10545-009-1262-1","article-title":"Cardiomyopathy in the congenital disorders of glycosylation (CDG): A case of late presentation and literature review","author":"Footitt","year":"2009","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.ajhg.2011.12.024_bib5","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/nrg1894","article-title":"Genetic defects in the human glycome","volume":"7","author":"Freeze","year":"2006","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.ajhg.2011.12.024_bib6","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1136\/adc.85.3.236","article-title":"Congenital disorder of glycosylation type Ia (CDG-Ia): Phenotypic spectrum of the R141H\/F119L genotype","volume":"85","author":"Kjaergaard","year":"2001","journal-title":"Arch. Dis. Child."},{"key":"10.1016\/j.ajhg.2011.12.024_bib7","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1002\/1098-1004(200011)16:5<386::AID-HUMU2>3.0.CO;2-Y","article-title":"Mutations in PMM2 that cause congenital disorders of glycosylation, type Ia (CDG-Ia)","volume":"16","author":"Matthijs","year":"2000","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.ajhg.2011.12.024_bib8","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1097\/GIM.0b013e318226fbf2","article-title":"Targeted polymerase chain reaction-based enrichment and next generation sequencing for diagnostic testing of congenital disorders of glycosylation","volume":"13","author":"Jones","year":"2011","journal-title":"Genet. Med."},{"key":"10.1016\/j.ajhg.2011.12.024_bib9","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1006\/geno.1997.4966","article-title":"Genome organization of human 48-kDa oligosaccharyltransferase (DDOST)","volume":"45","author":"Yamagata","year":"1997","journal-title":"Genomics"},{"key":"10.1016\/j.ajhg.2011.12.024_bib10","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1042\/bj3550245","article-title":"The efficiency of N-linked glycosylation of bovine DNase I depends on the Asn-Xaa-Ser\/Thr sequence and the tissue of origin","volume":"355","author":"Nishikawa","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.ajhg.2011.12.024_bib11","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1016\/j.bbrc.2009.10.047","article-title":"Screening for OST deficiencies in unsolved CDG-I patients","volume":"390","author":"Vleugels","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ajhg.2011.12.024_bib12","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1002\/humu.21085","article-title":"RFT1 deficiency in three novel CDG patients","volume":"30","author":"Vleugels","year":"2009","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.ajhg.2011.12.024_bib13","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1093\/glycob\/cwj006","article-title":"Hydrophobic Man-1-P derivatives correct abnormal glycosylation in Type I congenital disorder of glycosylation fibroblasts","volume":"15","author":"Eklund","year":"2005","journal-title":"Glycobiology"},{"key":"10.1016\/j.ajhg.2011.12.024_bib14","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1111\/j.1742-4658.2008.06246.x","article-title":"The relative contribution of mannose salvage pathways to glycosylation in PMI-deficient mouse embryonic fibroblast cells","volume":"275","author":"Fujita","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.ajhg.2011.12.024_bib15","doi-asserted-by":"crossref","first-page":"2071","DOI":"10.1002\/j.1460-2075.1992.tb05265.x","article-title":"The yeast WBP1 is essential for oligosaccharyl transferase activity in\u00a0vivo and in\u00a0vitro","volume":"11","author":"te Heesen","year":"1992","journal-title":"EMBO J."},{"key":"10.1016\/j.ajhg.2011.12.024_bib16","doi-asserted-by":"crossref","first-page":"6217","DOI":"10.1021\/jo0100345","article-title":"Substrate specificity of the glycosyl donor for oligosaccharyl transferase","volume":"66","author":"Tai","year":"2001","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.ajhg.2011.12.024_bib17","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1111\/j.1749-6632.2010.05840.x","article-title":"Congenital disorders of glycosylation","volume":"1214","author":"Jaeken","year":"2010","journal-title":"Ann. N Y Acad. Sci."},{"key":"10.1016\/j.ajhg.2011.12.024_bib18","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1007\/s10545-011-9337-1","article-title":"Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation","volume":"34","author":"Mohorko","year":"2011","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.ajhg.2011.12.024_bib19","doi-asserted-by":"crossref","first-page":"32513","DOI":"10.1074\/jbc.272.51.32513","article-title":"The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p","volume":"272","author":"Karaoglu","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ajhg.2011.12.024_bib20","doi-asserted-by":"crossref","first-page":"47R","DOI":"10.1093\/glycob\/cwj066","article-title":"An evolving view of the\u00a0eukaryotic oligosaccharyltransferase","volume":"16","author":"Kelleher","year":"2006","journal-title":"Glycobiology"},{"key":"10.1016\/j.ajhg.2011.12.024_bib21","doi-asserted-by":"crossref","first-page":"673","DOI":"10.18388\/abp.2007_3131","article-title":"Studies on oligosaccharyl transferase in yeast","volume":"54","author":"Lennarz","year":"2007","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.ajhg.2011.12.024_bib22","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1016\/j.ajhg.2008.03.021","article-title":"Oligosaccharyltransferase-subunit mutations in nonsyndromic mental retardation","volume":"82","author":"Molinari","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.ajhg.2011.12.024_bib23","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.bbadis.2009.08.005","article-title":"CDG nomenclature: Time for a change!","volume":"1792","author":"Jaeken","year":"2009","journal-title":"Biochim. Biophys. Acta"}],"container-title":["The American Journal of Human Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0002929712000419?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0002929712000419?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,11]],"date-time":"2025-09-11T07:11:33Z","timestamp":1757574693000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0002929712000419"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,2]]},"references-count":23,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2012,2]]}},"alternative-id":["S0002929712000419"],"URL":"https:\/\/doi.org\/10.1016\/j.ajhg.2011.12.024","relation":{},"ISSN":["0002-9297"],"issn-type":[{"value":"0002-9297","type":"print"}],"subject":[],"published":{"date-parts":[[2012,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"DDOST Mutations Identified by Whole-Exome Sequencing Are Implicated in Congenital Disorders of Glycosylation","name":"articletitle","label":"Article Title"},{"value":"The American Journal of Human Genetics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ajhg.2011.12.024","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2012 The American Society of Human Genetics. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}