| pubmed-article:17115051 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17115051 | lifeskim:mentions | umls-concept:C0318593 | lld:lifeskim |
| pubmed-article:17115051 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:17115051 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17115051 | lifeskim:mentions | umls-concept:C1512886 | lld:lifeskim |
| pubmed-article:17115051 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17115051 | pubmed:dateCreated | 2006-12-5 | lld:pubmed |
| pubmed-article:17115051 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17115051 | pubmed:abstractText | Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initiation factors and initiator transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral IRES bound to the 80S ribosome. The resolution of the cryo-EM reconstruction, in the subnanometer range, allowed the molecular structure of the complete IRES in its active, ribosome-bound state to be solved. The structure, harboring three pseudoknot-containing domains, each with a specific functional role, shows how defined elements of the IRES emerge from a compactly folded core and interact with the key ribosomal components that form the A, P and E sites, where tRNAs normally bind. Our results exemplify the molecular strategy for recruitment of an IRES and reveal the dynamic features necessary for internal initiation. | lld:pubmed |
| pubmed-article:17115051 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17115051 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17115051 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17115051 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17115051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17115051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17115051 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17115051 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17115051 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:WesthofEricE | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:MielkeThorste... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:SpahnChristia... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:PenczekPawel... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:ConnellSean... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:SchroeerBirgi... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:SchülerMartin... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:LescouteAurel... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:GiesebrechtJa... | lld:pubmed |
| pubmed-article:17115051 | pubmed:author | pubmed-author:DabrowskiMary... | lld:pubmed |
| pubmed-article:17115051 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17115051 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:17115051 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17115051 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17115051 | pubmed:pagination | 1092-6 | lld:pubmed |
| pubmed-article:17115051 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
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| pubmed-article:17115051 | pubmed:meshHeading | pubmed-meshheading:17115051... | lld:pubmed |
| pubmed-article:17115051 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17115051 | pubmed:articleTitle | Structure of the ribosome-bound cricket paralysis virus IRES RNA. | lld:pubmed |
| pubmed-article:17115051 | pubmed:affiliation | Institut für Medizinische Physik und Biophysik, Charite-Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117-Berlin, Germany. | lld:pubmed |
| pubmed-article:17115051 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17115051 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17115051 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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