pubmed-article:3697083 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0080125 | lld:lifeskim |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0205332 | lld:lifeskim |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0039679 | lld:lifeskim |
pubmed-article:3697083 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:3697083 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:3697083 | pubmed:dateCreated | 1988-2-23 | lld:pubmed |
pubmed-article:3697083 | pubmed:abstractText | The precursor rRNA of Tetrahymena thermophila contains a group I intervening sequence (IVS) that catalyzes its own excision to yield mature rRNA. The excised IVS catalyzes a number of cleavage/ligation reactions that are analogous to the transesterification reactions of splicing. We examined the behavior of a variety of 3'-truncated forms of the IVS and found several abbreviated molecules that retained catalytic activity. The reactivity of these molecules indicates that the site at which cleavage/ligation occurs lies in close proximity to all of the conserved sequence elements within the catalytic core of the IVS. | lld:pubmed |
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pubmed-article:3697083 | pubmed:language | eng | lld:pubmed |
pubmed-article:3697083 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3697083 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3697083 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3697083 | pubmed:month | Dec | lld:pubmed |
pubmed-article:3697083 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:3697083 | pubmed:author | pubmed-author:InoueTT | lld:pubmed |
pubmed-article:3697083 | pubmed:author | pubmed-author:JoyceG FGF | lld:pubmed |
pubmed-article:3697083 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3697083 | pubmed:day | 10 | lld:pubmed |
pubmed-article:3697083 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:3697083 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3697083 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3697083 | pubmed:pagination | 9825-40 | lld:pubmed |
pubmed-article:3697083 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:3697083 | pubmed:meshHeading | pubmed-meshheading:3697083-... | lld:pubmed |
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pubmed-article:3697083 | pubmed:meshHeading | pubmed-meshheading:3697083-... | lld:pubmed |
pubmed-article:3697083 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3697083 | pubmed:articleTitle | Structure of the catalytic core of the Tetrahymena ribozyme as indicated by reactive abbreviated forms of the molecule. | lld:pubmed |
pubmed-article:3697083 | pubmed:affiliation | Salk Institute for Biological Studies, San Diego, CA 92138. | lld:pubmed |
pubmed-article:3697083 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3697083 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3697083 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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