Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-6-6
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arginine, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response..., http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/SMN Complex Proteins, http://linkedlifedata.com/resource/pubmed/chemical/dimethylarginine, http://linkedlifedata.com/resource/pubmed/chemical/tud protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/valois protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1077-89
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:16753561-Animals, pubmed-meshheading:16753561-Animals, Genetically Modified, pubmed-meshheading:16753561-Arginine, pubmed-meshheading:16753561-Carrier Proteins, pubmed-meshheading:16753561-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:16753561-Drosophila Proteins, pubmed-meshheading:16753561-Drosophila melanogaster, pubmed-meshheading:16753561-Female, pubmed-meshheading:16753561-Fertility, pubmed-meshheading:16753561-Germ Cells, pubmed-meshheading:16753561-Male, pubmed-meshheading:16753561-Membrane Transport Proteins, pubmed-meshheading:16753561-Methylation, pubmed-meshheading:16753561-Methyltransferases, pubmed-meshheading:16753561-Nerve Tissue Proteins, pubmed-meshheading:16753561-Ovary, pubmed-meshheading:16753561-Protein Methyltransferases, pubmed-meshheading:16753561-RNA-Binding Proteins, pubmed-meshheading:16753561-Ribonucleoproteins, Small Nuclear, pubmed-meshheading:16753561-SMN Complex Proteins
pubmed:year
2006
pubmed:articleTitle
The Sm-protein methyltransferase, dart5, is essential for germ-cell specification and maintenance.
pubmed:affiliation
Department of Genetics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4955, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural