{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T21:39:02Z","timestamp":1791668342183,"version":"4.3.4"},"reference-count":27,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2005,4,5]],"date-time":"2005-04-05T00:00:00Z","timestamp":1112659200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European J of Haematology"],"published-print":{"date-parts":[[2005,5]]},"abstract":"<jats:p><jats:bold>Abstract:\u2002<\/jats:bold> A case of type II recessive congenital methaemoglobinaemia (RCM) observed in a Lebanese subject with a novel mutation in NADH\u2010cytochrome b5 reductase gene is described. A homozygous mutation CAC to AA identified at Thr 295 with an out\u2010of\u2010frame 1\u2010bp deletion leads to a frameshift with translational read\u2010through of the natural stop codon. The molecular mechanism is demonstrated by an <jats:italic>in vitro<\/jats:italic> translation study. The model of mutated cytochrome b5 reductase protein possessing 46 additional amino acids was obtained by homology modelling. The mutation causes an alteration of hydrophobicity in the carboxyl\u2010terminal portion, resulting in the conformation being drastically disturbed by the presence of 46 supplementary amino acids. The identical mutation was found in the heterozygous state in the patient's parents and sister. Identification of this new mutation enabled us to perform the molecular prenatal diagnosis of type II RCM at the DNA level.<\/jats:p>","DOI":"10.1111\/j.1600-0609.2004.00388.x","type":"journal-article","created":{"date-parts":[[2005,4,5]],"date-time":"2005-04-05T15:41:26Z","timestamp":1112715686000},"page":"389-395","source":"Crossref","is-referenced-by-count":23,"title":["Prenatal diagnosis of recessive congenital methaemoglobinaemia type II: novel mutation in the NADH\u2010cytochrome b5 reductase gene leading to stop codon read\u2010through"],"prefix":"10.1111","volume":"74","author":[{"given":"Alena","family":"Leroux","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"France","family":"Leturcq","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathalie","family":"Deburgrave","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie\u2010France","family":"Szajnert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,4,5]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.71.11.4565"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(71)90186-X"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/229252a0"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2744(77)90136-X"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2744(78)90288-7"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1042\/0264-6021:3550529"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/258619a0"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1002\/pd.1970010106"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00431-004-1409-x"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2002-05-1405"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1034\/j.1600-0609.2003.00070.x"},{"key":"e_1_2_7_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.thj.6200380"},{"key":"e_1_2_7_14_2","doi-asserted-by":"crossref","first-page":"20414","DOI":"10.1016\/S0021-9258(19)88718-5","article-title":"Enzymatic instability of NADH\u2010cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type)","volume":"267","author":"Shirabe K","year":"1992","journal-title":"J Biol Chem"},{"key":"e_1_2_7_15_2","doi-asserted-by":"crossref","first-page":"2254","DOI":"10.1182\/blood.V85.8.2254.bloodjournal8582254","article-title":"Four new mutations in the NADH\u2010cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II","volume":"85","author":"Mota Vieira L","year":"1995","journal-title":"Blood"},{"key":"e_1_2_7_16_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V97.4.1106"},{"key":"e_1_2_7_17_2","first-page":"339","article-title":"New method for determining ferrihemoglobin reductase (NADH\u2010methemoglobine reductase) in erythrocytes","volume":"73","author":"Hegesh E","year":"1968","journal-title":"J Lab Clin Med"},{"key":"e_1_2_7_18_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2141.1977.tb00589.x"},{"key":"e_1_2_7_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)52451-6"},{"key":"e_1_2_7_20_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/17.8.752"},{"key":"e_1_2_7_21_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(89)90299-0"},{"key":"e_1_2_7_22_2","doi-asserted-by":"publisher","DOI":"10.1002\/humu.31"},{"key":"e_1_2_7_23_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V95.10.3250"},{"key":"e_1_2_7_24_2","first-page":"34","article-title":"A compound heterozygote in the NADH\u2010cytochrome b5 reductase gene from a Chinese patient with hereditary methemoglobinemia type I","volume":"72","author":"Wu YS","year":"2000","journal-title":"Int J Hematol"},{"key":"e_1_2_7_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.15.3.1769"},{"key":"e_1_2_7_26_2","doi-asserted-by":"crossref","first-page":"5952","DOI":"10.1016\/S0021-9258(17)37554-3","article-title":"An in\u2010frame deletion of codon 298 of NADH\u2010cytochrome b5 reductase gene in hereditary methemoglobinemia type II (generalized type). 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