| pubmed-article:11782436 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C2350332 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
| pubmed-article:11782436 | lifeskim:mentions | umls-concept:C2700400 | lld:lifeskim |
| pubmed-article:11782436 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11782436 | pubmed:dateCreated | 2002-1-9 | lld:pubmed |
| pubmed-article:11782436 | pubmed:abstractText | HeLa cytoplasmic extracts contain both 3'-5' and 5'-3' exonuclease activities that may play important roles in mRNA decay. Using an in vitro RNA deadenylation/decay assay, mRNA decay intermediates were trapped using phosphothioate-modified RNAs. These data indicate that 3'-5' exonucleolytic decay is the major pathway of RNA degradation following deadenylation in HeLa cytoplasmic extracts. Immunodepletion using antibodies specific for the exosomal protein PM-Scl75 demonstrated that the human exosome complex is required for efficient 3'-5' exonucleolytic decay. Furthermore, 3'-5' exonucleolytic decay was stimulated dramatically by AU-rich instability elements (AREs), implicating a role for the exosome in the regulation of mRNA turnover. Finally, PM-Scl75 protein was found to interact specifically with AREs. These data suggest that the interaction between the exosome and AREs plays a key role in regulating the efficiency of ARE-containing mRNA turnover. | lld:pubmed |
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| pubmed-article:11782436 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11782436 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11782436 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11782436 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11782436 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11782436 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11782436 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:MukherjeeDevi... | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:GaoMinM | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:O'ConnorJ... | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:RaijmakersRei... | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:PruijnGerG | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:LutzCarol SCS | lld:pubmed |
| pubmed-article:11782436 | pubmed:author | pubmed-author:WiluszJeffrey... | lld:pubmed |
| pubmed-article:11782436 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11782436 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11782436 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:11782436 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11782436 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11782436 | pubmed:pagination | 165-74 | lld:pubmed |
