| pubmed-article:16753561 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16753561 | lifeskim:mentions | umls-concept:C0024501 | lld:lifeskim |
| pubmed-article:16753561 | lifeskim:mentions | umls-concept:C0025831 | lld:lifeskim |
| pubmed-article:16753561 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:16753561 | lifeskim:mentions | umls-concept:C2348235 | lld:lifeskim |
| pubmed-article:16753561 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:16753561 | pubmed:dateCreated | 2006-6-6 | lld:pubmed |
| pubmed-article:16753561 | pubmed:abstractText | The C-terminal tails of spliceosomal Sm proteins contain symmetrical dimethylarginine (sDMA) residues in vivo. The precise function of this posttranslational modification in the biogenesis of small nuclear ribonucleoproteins (snRNPs) and pre-mRNA splicing remains largely uncharacterized. Here, we examine the organismal and cellular consequences of loss of symmetric dimethylation of Sm proteins in Drosophila. | lld:pubmed |
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| pubmed-article:16753561 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16753561 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16753561 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16753561 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:16753561 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:16753561 | pubmed:author | pubmed-author:RajendraT KTK | lld:pubmed |
| pubmed-article:16753561 | pubmed:author | pubmed-author:MateraA... | lld:pubmed |
| pubmed-article:16753561 | pubmed:author | pubmed-author:TianLipingL | lld:pubmed |
| pubmed-article:16753561 | pubmed:author | pubmed-author:GonsalvezGray... | lld:pubmed |
| pubmed-article:16753561 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16753561 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:16753561 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:16753561 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16753561 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16753561 | pubmed:pagination | 1077-89 | lld:pubmed |
| pubmed-article:16753561 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:16753561 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16753561 | pubmed:articleTitle | The Sm-protein methyltransferase, dart5, is essential for germ-cell specification and maintenance. | lld:pubmed |
| pubmed-article:16753561 | pubmed:affiliation | Department of Genetics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4955, USA. | lld:pubmed |
| pubmed-article:16753561 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16753561 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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