| pubmed-article:2408148 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2408148 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
| pubmed-article:2408148 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:2408148 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:2408148 | lifeskim:mentions | umls-concept:C1519613 | lld:lifeskim |
| pubmed-article:2408148 | lifeskim:mentions | umls-concept:C0005495 | lld:lifeskim |
| pubmed-article:2408148 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:2408148 | pubmed:issue | 4946 | lld:pubmed |
| pubmed-article:2408148 | pubmed:dateCreated | 1990-4-4 | lld:pubmed |
| pubmed-article:2408148 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2408148 | pubmed:abstractText | Cold-sensitive mutations in the SPB genes (spb1-spb7) of Saccharomyces cerevisiae suppress the inhibition of translation initiation resulting from deletion of the poly(A)-binding protein gene (PAB1). The SPB4 protein belongs to a family of adenosine triphosphate (ATP)-dependent RNA helicases. The aberrant production of 25S ribosomal RNA (rRNA) occurring in spb4-1 mutants or the deletion of SPB2 (RPL46) permits the deletion of PAB1. These data suggest that mutations affecting different steps of 60S subunit formation can allow PAB-independent translation, and they indicate that further characterization of the spb mutations could lend insight into the biogenesis of the ribosome. | lld:pubmed |
| pubmed-article:2408148 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2408148 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2408148 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2408148 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2408148 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2408148 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2408148 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2408148 | pubmed:author | pubmed-author:DavisR WRW | lld:pubmed |
| pubmed-article:2408148 | pubmed:author | pubmed-author:SachsA BAB | lld:pubmed |
| pubmed-article:2408148 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2408148 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:2408148 | pubmed:volume | 247 | lld:pubmed |
| pubmed-article:2408148 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2408148 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2408148 | pubmed:pagination | 1077-9 | lld:pubmed |
| pubmed-article:2408148 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2408148 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2408148 | pubmed:articleTitle | Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. | lld:pubmed |
| pubmed-article:2408148 | pubmed:affiliation | Department of Biochemistry, Stanford Medical Center, CA 94305. | lld:pubmed |
| pubmed-article:2408148 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2408148 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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