| pubmed-article:10397352 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10397352 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:10397352 | lifeskim:mentions | umls-concept:C0040711 | lld:lifeskim |
| pubmed-article:10397352 | lifeskim:mentions | umls-concept:C0039593 | lld:lifeskim |
| pubmed-article:10397352 | lifeskim:mentions | umls-concept:C0022885 | lld:lifeskim |
| pubmed-article:10397352 | lifeskim:mentions | umls-concept:C0679199 | lld:lifeskim |
| pubmed-article:10397352 | lifeskim:mentions | umls-concept:C1705810 | lld:lifeskim |
| pubmed-article:10397352 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10397352 | pubmed:dateCreated | 1999-9-30 | lld:pubmed |
| pubmed-article:10397352 | pubmed:abstractText | There are regions in rRNA which are evolutionary conserved and exposed on ribosomal surface. We selected in plant material (Lupinus luteus) two of them: the alpha-sarcin domain of 26S rRNA (L-rRNA) and C loop of 5S rRNA, to be further investigated using antisense oligomers as research tools. We found inhibition of the model polypeptide biosynthesis (up to 80%) due to specific hybridization of oligomers addressed to alpha-sarcin domain and loop C. Based on our results we present the evidence for the key role played by these regions of rRNAs during protein biosynthesis in plant system. According to our hypothesis, conformational changes of these two regions are synchronised and cooperative during transition of pre- to post-translocation state of the ribosome. The correlation of structure and activity of rRNA domains in translation is shown. | lld:pubmed |
| pubmed-article:10397352 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10397352 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10397352 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10397352 | pubmed:issn | 0001-527X | lld:pubmed |
| pubmed-article:10397352 | pubmed:author | pubmed-author:PolakJJ | lld:pubmed |
| pubmed-article:10397352 | pubmed:author | pubmed-author:TwardowskiTT | lld:pubmed |
| pubmed-article:10397352 | pubmed:author | pubmed-author:NawrotMM | lld:pubmed |
| pubmed-article:10397352 | pubmed:author | pubmed-author:SobkiewiczAA | lld:pubmed |
| pubmed-article:10397352 | pubmed:author | pubmed-author:BohunEE | lld:pubmed |
| pubmed-article:10397352 | pubmed:author | pubmed-author:Ksiazczak-Kus... | lld:pubmed |
| pubmed-article:10397352 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10397352 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:10397352 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10397352 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10397352 | pubmed:pagination | 1053-66 | lld:pubmed |
| pubmed-article:10397352 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:meshHeading | pubmed-meshheading:10397352... | lld:pubmed |
| pubmed-article:10397352 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:10397352 | pubmed:articleTitle | Functional role of rRNAs in plant translation system tested with antisense strategy. | lld:pubmed |
| pubmed-article:10397352 | pubmed:affiliation | Institute of Bioorganic Chemistry, Polish Academy of Sciences, Pozna?. | lld:pubmed |
| pubmed-article:10397352 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10397352 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
