| pubmed-article:7912128 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C0059017 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C1882417 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
| pubmed-article:7912128 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:7912128 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7912128 | pubmed:dateCreated | 1994-7-28 | lld:pubmed |
| pubmed-article:7912128 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:abstractText | Electron transfer flavoprotein (ETF) is a heterodimeric enzyme composed of an alpha-subunit and a beta-subunit and contains a single equivalent of FAD per dimer. ETF deficiency can be demonstrated in individuals affected by a severe metabolic disorder, glutaric acidemia type II (GAII). In this study, we have investigated for the first time the molecular basis of beta-ETF deficiency in three GAII patients: two Japanese brothers, P411 and P412, and a third unrelated patient, P485. Molecular analysis of the beta-ETF gene in P411 and P412 demonstrated that both these patients are compound heterozygotes. One allele is carrying a G to A transition at nucleotide 518, causing a missense mutation at codon 164. This point mutation is maternally derived and is not detected in 42 unrelated controls. The other allele carries a G to C transversion at the first nucleotide of the intron donor site, downstream of an exon that is skipped during the splicing event. The sequence analysis of the beta-ETF coding sequence in P485 showed only a C to T transition at nucleotide 488 that causes a Thr154 to Met substitution and the elimination of a HgaI restriction site. HgaI restriction analysis on 63 unrelated controls' genomic DNA demonstrated that the C488T transition identifies a polymorphic site. Finally, transfection of wild-type beta-ETF cDNA into P411 fibroblasts suggests that wild-type beta-ETF cDNA complements the genetic defect and restores the beta-oxidation flux to normal levels. | lld:pubmed |
| pubmed-article:7912128 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7912128 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7912128 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7912128 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7912128 | pubmed:issn | 0964-6906 | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:DiDonatoSS | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:FrermanF EFE | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:YamaguchiSS | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:BerraBB | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:FinocchiaroGG | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:ColomboII | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:GaravagliaBB | lld:pubmed |
| pubmed-article:7912128 | pubmed:author | pubmed-author:GarbuglioNN | lld:pubmed |
| pubmed-article:7912128 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7912128 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:7912128 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7912128 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7912128 | pubmed:pagination | 429-35 | lld:pubmed |
| pubmed-article:7912128 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:meshHeading | pubmed-meshheading:7912128-... | lld:pubmed |
| pubmed-article:7912128 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7912128 | pubmed:articleTitle | Mutations and polymorphisms of the gene encoding the beta-subunit of the electron transfer flavoprotein in three patients with glutaric acidemia type II. | lld:pubmed |
| pubmed-article:7912128 | pubmed:affiliation | Istituto di Fisiologia Generale e Chimica Biologica, Facoltà di Farmacia, Università degli Studi di Milano, Italy. | lld:pubmed |
| pubmed-article:7912128 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:2109 | entrezgene:pubmed | pubmed-article:7912128 | lld:entrezgene |
| entrez-gene:292845 | entrezgene:pubmed | pubmed-article:7912128 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7912128 | lld:pubmed |
