| pubmed-article:9790667 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C0055530 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C1413864 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C1622990 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9790667 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9790667 | pubmed:issue | 43 | lld:pubmed |
| pubmed-article:9790667 | pubmed:dateCreated | 1998-11-17 | lld:pubmed |
| pubmed-article:9790667 | pubmed:abstractText | A novel C to A mutation in the sterol 27-hydroxylase gene (CYP27) was identified by sequencing amplified CYP27 gene products from a patient with cerebrotendinous xanthomatosis (CTX). The mutation changed the adrenodoxin cofactor binding residue 362Arg to 362Ser (CGT 362Arg to AGT 362Ser), and was responsible for deficiency in the sterol 27-hydroxylase activity, as confirmed by expression of mutant cDNA into COS-1 cells. Quantitative analysis showed that the expression of CYP27 gene mRNA in the patient represented 52.5% of the normal level. As the mutation occurred at the penultimate nucleotide of exon 6 (-2 position of exon 6-intron 6 splice site) of the gene, we hypothesized that the mutation may partially affect the normal splicing efficiency in exon 6 and cause alternative splicing elsewhere, which resulted in decreased transcript in the patient. Transfection of constructed minigenes, with or without the mutation, into COS-1 cells confirmed that the mutant minigene was responsible for a mRNA species alternatively spliced at an activated cryptic 5' splice site 88 bp upstream from the 3' end of exon 6. Our data suggest that the C to A mutation at the penultimate nucleotide of exon 6 of the CYP27 gene not only causes the deficiency in the sterol 27-hydroxylase activity, but also partially leads to alternative pre-mRNA splicing of the gene. To our knowledge, this is the first report regarding effects on pre-mRNA splicing of a mutation at the -2 position of a 5' splice site. | lld:pubmed |
| pubmed-article:9790667 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9790667 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9790667 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9790667 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9790667 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9790667 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9790667 | pubmed:author | pubmed-author:KubotaSS | lld:pubmed |
| pubmed-article:9790667 | pubmed:author | pubmed-author:SeyamaYY | lld:pubmed |
| pubmed-article:9790667 | pubmed:author | pubmed-author:IshiharaTT | lld:pubmed |
| pubmed-article:9790667 | pubmed:author | pubmed-author:ChenWW | lld:pubmed |
| pubmed-article:9790667 | pubmed:author | pubmed-author:UjikeHH | lld:pubmed |
| pubmed-article:9790667 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9790667 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:9790667 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:9790667 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9790667 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9790667 | pubmed:pagination | 15050-6 | lld:pubmed |
| pubmed-article:9790667 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9790667 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9790667 | pubmed:articleTitle | A novel Arg362Ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity. | lld:pubmed |
| pubmed-article:9790667 | pubmed:affiliation | Department of Physiological Chemistry and Metabolism, Graduate School of Medicine, The University of Tokyo, Japan. | lld:pubmed |
| pubmed-article:9790667 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9790667 | pubmed:publicationType | Case Reports | lld:pubmed |
| pubmed-article:9790667 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1593 | entrezgene:pubmed | pubmed-article:9790667 | lld:entrezgene |
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