| pubmed-article:19133737 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19133737 | lifeskim:mentions | umls-concept:C0023690 | lld:lifeskim |
| pubmed-article:19133737 | lifeskim:mentions | umls-concept:C0162340 | lld:lifeskim |
| pubmed-article:19133737 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:19133737 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19133737 | pubmed:dateCreated | 2009-1-27 | lld:pubmed |
| pubmed-article:19133737 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19133737 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19133737 | pubmed:abstractText | Members of the genus Trypanosoma, which include the pathogenic species Trypanosoma brucei and Trypanosoma cruzi, edit their post-transcriptional mitochondrial RNA via a multiprotein complex called the editosome. In T. brucei, the RNA is nicked prior to uridylate insertion and deletion. Following editing, nicked RNA is religated by one of two RNA-editing ligases (TbREL). This study describes a recent 70 ns molecular dynamics simulation of TbREL1, an ATP-dependent RNA-editing ligase of the nucleotidyltransferase superfamily that is required for the survival of T. brucei insect and bloodstream forms. In this work, a model of TbREL1 in complex with its full double-stranded RNA (dsRNA) substrate is created on the basis of the homologous relation between TbREL1 and T4 Rnl2. The simulation captures TbREL1 dynamics in the state immediately preceding RNA ligation, providing insights into the functional dynamics and catalytic mechanism of the kinetoplastid ligation reaction. Important features of RNA binding and specificity are revealed for kinetoplastid ligases and the broader nucleotidyltransferase superfamily. | lld:pubmed |
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| pubmed-article:19133737 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19133737 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19133737 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19133737 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19133737 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19133737 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19133737 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19133737 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19133737 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19133737 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19133737 | pubmed:author | pubmed-author:McCammonJ... | lld:pubmed |
| pubmed-article:19133737 | pubmed:author | pubmed-author:AmaroRommie... | lld:pubmed |
| pubmed-article:19133737 | pubmed:author | pubmed-author:SwiftRobert... | lld:pubmed |
| pubmed-article:19133737 | pubmed:author | pubmed-author:DurrantJacobJ | lld:pubmed |
| pubmed-article:19133737 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19133737 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:19133737 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19133737 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19133737 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19133737 | pubmed:pagination | 709-19 | lld:pubmed |
| pubmed-article:19133737 | pubmed:dateRevised | 2011-3-17 | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
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| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:meshHeading | pubmed-meshheading:19133737... | lld:pubmed |
| pubmed-article:19133737 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19133737 | pubmed:articleTitle | Toward understanding the conformational dynamics of RNA ligation. | lld:pubmed |
| pubmed-article:19133737 | pubmed:affiliation | Department of Chemistry and Biochemistry, NSF Center for Theoretical Biological Physics, University of California at San Diego, La Jolla, California 92093-0365, USA. | lld:pubmed |
| pubmed-article:19133737 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19133737 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19133737 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19133737 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
