pubmed-article:8943341 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C0040711 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C1136317 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
pubmed-article:8943341 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
pubmed-article:8943341 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:8943341 | pubmed:dateCreated | 1997-1-31 | lld:pubmed |
pubmed-article:8943341 | pubmed:abstractText | Translation of picornavirus RNA is initiated after ribosomal binding to an internal ribosomal entry site (IRES) within the 5' untranslated region. We have reconstituted IRES-mediated initiation on encephalomyocarditis virus RNA from purified components and used primer extension analysis to confirm the fidelity of 48S preinitiation complex formation. Eukaryotic initiation factor 2 (eIF2), eIF3, and eIF4F were required for initiation; eIF4B and to a lesser extent the pyrimidine tract-binding protein stimulated this process. We show that eIF4F binds to the IRES in a novel cap-independent manner and suggest that cap- and IRES-dependent initiation mechanisms utilize different modes of interaction with this factor to promote ribosomal attachment to mRNA. | lld:pubmed |
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pubmed-article:8943341 | pubmed:language | eng | lld:pubmed |
pubmed-article:8943341 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8943341 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8943341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8943341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8943341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8943341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8943341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8943341 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8943341 | pubmed:month | Dec | lld:pubmed |
pubmed-article:8943341 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:8943341 | pubmed:author | pubmed-author:ShatskyI NIN | lld:pubmed |
pubmed-article:8943341 | pubmed:author | pubmed-author:HellenC UCU | lld:pubmed |
pubmed-article:8943341 | pubmed:author | pubmed-author:PestovaT VTV | lld:pubmed |
pubmed-article:8943341 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8943341 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:8943341 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8943341 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8943341 | pubmed:pagination | 6859-69 | lld:pubmed |
pubmed-article:8943341 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:8943341 | pubmed:meshHeading | pubmed-meshheading:8943341-... | lld:pubmed |