| pubmed-article:11707413 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1526985 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:11707413 | lifeskim:mentions | umls-concept:C1447535 | lld:lifeskim |
| pubmed-article:11707413 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:11707413 | pubmed:dateCreated | 2001-11-14 | lld:pubmed |
| pubmed-article:11707413 | pubmed:abstractText | The RNA-binding protein Y14 binds preferentially to mRNAs produced by splicing and is a component of a multiprotein complex that assembles approximately 20 nucleotides upstream of exon-exon junctions. This complex probably has important functions in post-splicing events including nuclear export and nonsense-mediated decay of mRNA. We show that Y14 binds to two previously reported components, Aly/REF and RNPS1, and to the mRNA export factor TAP. Moreover, we identified magoh, a human homolog of the Drosophila mago nashi gene product, as a novel component of the complex. Magoh binds avidly and directly to Y14 and TAP, but not to other known components of the complex, and is found in Y14-containing mRNPs in vivo. Importantly, magoh also binds to mRNAs produced by splicing upstream (approximately 20 nucleotides) of exon- exon junctions and its binding to mRNA persists after export. These experiments thus reveal specific protein-protein interactions among the proteins of the splicing-dependent mRNP complex and suggest an important role for the highly evolutionarily conserved magoh protein in this complex. | lld:pubmed |
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| pubmed-article:11707413 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11707413 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11707413 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11707413 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11707413 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11707413 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11707413 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11707413 | pubmed:author | pubmed-author:KataokaNN | lld:pubmed |
| pubmed-article:11707413 | pubmed:author | pubmed-author:DreyfussGG | lld:pubmed |
| pubmed-article:11707413 | pubmed:author | pubmed-author:YongJJ | lld:pubmed |
| pubmed-article:11707413 | pubmed:author | pubmed-author:KimV NVN | lld:pubmed |
| pubmed-article:11707413 | pubmed:author | pubmed-author:DiemM DMD | lld:pubmed |
| pubmed-article:11707413 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11707413 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11707413 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11707413 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11707413 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11707413 | pubmed:pagination | 6424-33 | lld:pubmed |
| pubmed-article:11707413 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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