| pubmed-article:11884397 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C0024501 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C1956015 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11884397 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11884397 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:11884397 | pubmed:dateCreated | 2002-5-20 | lld:pubmed |
| pubmed-article:11884397 | pubmed:abstractText | Ribosome biogenesis is a conserved process in eukaryotes that requires a large number of small nucleolar RNAs and trans-acting proteins. The Saccharomyces cerevisiae MRD1 (multiple RNA-binding domain) gene encodes a novel protein that contains five consensus RNA-binding domains. Mrd1p is essential for viability. Mrd1p partially co-localizes with the nucleolar protein Nop1p. Depletion of Mrd1p leads to a selective reduction of 18 S rRNA and 40 S ribosomal subunits. Mrd1p associates with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs and is necessary for the initial processing at the A(0)-A(2) cleavage sites in pre-rRNA. The presence of five RNA-binding domains in Mrd1p suggests that Mrd1p may function to correctly fold pre-rRNA, a requisite for proper cleavage. Sequence comparisons suggest that Mrd1p homologues exist in all eukaryotes. | lld:pubmed |
| pubmed-article:11884397 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11884397 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11884397 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11884397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11884397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11884397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11884397 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11884397 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11884397 | pubmed:month | May | lld:pubmed |
| pubmed-article:11884397 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11884397 | pubmed:author | pubmed-author:ZhaoJianJ | lld:pubmed |
| pubmed-article:11884397 | pubmed:author | pubmed-author:JinShao-BoSB | lld:pubmed |
| pubmed-article:11884397 | pubmed:author | pubmed-author:WieslanderLar... | lld:pubmed |
| pubmed-article:11884397 | pubmed:author | pubmed-author:BjorkPetraP | lld:pubmed |
| pubmed-article:11884397 | pubmed:author | pubmed-author:SchmekelKarin... | lld:pubmed |
| pubmed-article:11884397 | pubmed:author | pubmed-author:LjungdahlPer... | lld:pubmed |
| pubmed-article:11884397 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11884397 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:11884397 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11884397 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11884397 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11884397 | pubmed:pagination | 18431-9 | lld:pubmed |
| pubmed-article:11884397 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:meshHeading | pubmed-meshheading:11884397... | lld:pubmed |
| pubmed-article:11884397 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11884397 | pubmed:articleTitle | Mrd1p is required for processing of pre-rRNA and for maintenance of steady-state levels of 40 S ribosomal subunits in yeast. | lld:pubmed |
| pubmed-article:11884397 | pubmed:affiliation | Department of Molecular Biology and Functional Genomics, Stockholm University, SE-106 91 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:11884397 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11884397 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:856228 | entrezgene:pubmed | pubmed-article:11884397 | lld:entrezgene |
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