pubmed-article:2685606 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2685606 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:2685606 | lifeskim:mentions | umls-concept:C0080125 | lld:lifeskim |
pubmed-article:2685606 | lifeskim:mentions | umls-concept:C0018330 | lld:lifeskim |
pubmed-article:2685606 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:2685606 | lifeskim:mentions | umls-concept:C0039679 | lld:lifeskim |
pubmed-article:2685606 | pubmed:issue | 6248 | lld:pubmed |
pubmed-article:2685606 | pubmed:dateCreated | 1990-1-4 | lld:pubmed |
pubmed-article:2685606 | pubmed:abstractText | The self-splicing Group I introns have a highly specific binding site for the substrate guanosine. Mutant versions of the Tetrahymena ribozyme have been used in combination with guanosine analogues to identify the nucleotide in the ribozyme that is primarily responsible for recognition of the guanine base. | lld:pubmed |
pubmed-article:2685606 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:language | eng | lld:pubmed |
pubmed-article:2685606 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2685606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2685606 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2685606 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2685606 | pubmed:issn | 0028-0836 | lld:pubmed |
pubmed-article:2685606 | pubmed:author | pubmed-author:GreenRR | lld:pubmed |
pubmed-article:2685606 | pubmed:author | pubmed-author:MichelFF | lld:pubmed |
pubmed-article:2685606 | pubmed:author | pubmed-author:HannaMM | lld:pubmed |
pubmed-article:2685606 | pubmed:author | pubmed-author:SzostakJ WJW | lld:pubmed |
pubmed-article:2685606 | pubmed:author | pubmed-author:BartelD PDP | lld:pubmed |
pubmed-article:2685606 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2685606 | pubmed:day | 23 | lld:pubmed |
pubmed-article:2685606 | pubmed:volume | 342 | lld:pubmed |
pubmed-article:2685606 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2685606 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2685606 | pubmed:pagination | 391-5 | lld:pubmed |
pubmed-article:2685606 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
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pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:meshHeading | pubmed-meshheading:2685606-... | lld:pubmed |
pubmed-article:2685606 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2685606 | pubmed:articleTitle | The guanosine binding site of the Tetrahymena ribozyme. | lld:pubmed |
pubmed-article:2685606 | pubmed:affiliation | Department of Molecular Biology, Massachusetts General Hospital, Boston 02114. | lld:pubmed |
pubmed-article:2685606 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2685606 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2685606 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:2685606 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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