| pubmed-article:16518398 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C0670496 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:16518398 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:16518398 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16518398 | pubmed:dateCreated | 2006-5-22 | lld:pubmed |
| pubmed-article:16518398 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518398 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518398 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518398 | pubmed:abstractText | The highly conserved ribonuclease RNase Z catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Here we present the structure of the complex between Bacillus subtilis RNase Z and tRNA(Thr), the first structure of a ribonucleolytic processing enzyme bound to tRNA. Binding of tRNA to RNase Z causes conformational changes in both partners to promote reorganization of the catalytic site and tRNA cleavage. | lld:pubmed |
| pubmed-article:16518398 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16518398 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518398 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16518398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16518398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518398 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16518398 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:16518398 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:16518398 | pubmed:author | pubmed-author:CondonCiaránC | lld:pubmed |
| pubmed-article:16518398 | pubmed:author | pubmed-author:MathyNathalie... | lld:pubmed |
| pubmed-article:16518398 | pubmed:author | pubmed-author:PellegriniOli... | lld:pubmed |
| pubmed-article:16518398 | pubmed:author | pubmed-author:Li de la... | lld:pubmed |
| pubmed-article:16518398 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16518398 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:16518398 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16518398 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16518398 | pubmed:pagination | 376-7 | lld:pubmed |
| pubmed-article:16518398 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:meshHeading | pubmed-meshheading:16518398... | lld:pubmed |
| pubmed-article:16518398 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16518398 | pubmed:articleTitle | Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA. | lld:pubmed |
| pubmed-article:16518398 | pubmed:affiliation | Centre National de la Recherche (CNRS) FRC550, Institut de Biologie Physico-Chimique, Paris, France. | lld:pubmed |
| pubmed-article:16518398 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16518398 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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