| pubmed-article:11017191 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11017191 | lifeskim:mentions | umls-concept:C0162771 | lld:lifeskim |
| pubmed-article:11017191 | lifeskim:mentions | umls-concept:C0080125 | lld:lifeskim |
| pubmed-article:11017191 | lifeskim:mentions | umls-concept:C1522634 | lld:lifeskim |
| pubmed-article:11017191 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:11017191 | pubmed:dateCreated | 2000-11-7 | lld:pubmed |
| pubmed-article:11017191 | pubmed:abstractText | The two phosphoryl transfer steps of pre-mRNA splicing are catalyzed within the large ribonuclear protein machine called the spliceosome. The highly dynamic nature of the spliceosome has presented many challenges to a structural and mechanistic understanding of its catalytic core. While much evidence supports the popular hypothesis that the catalytic steps of pre-mRNA splicing are mediated by spliceosomal RNA, a role for protein in catalysis cannot yet be ruled out. A highly conserved protein, Prp8, is a component of the catalytic core. We review data consistent with the hypothesis that Prp8 functions as a cofactor to an RNA enzyme. | lld:pubmed |
| pubmed-article:11017191 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11017191 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11017191 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11017191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11017191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11017191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11017191 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11017191 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11017191 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:11017191 | pubmed:author | pubmed-author:GuthrieCC | lld:pubmed |
| pubmed-article:11017191 | pubmed:author | pubmed-author:CollinsC ACA | lld:pubmed |
| pubmed-article:11017191 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11017191 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:11017191 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11017191 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11017191 | pubmed:pagination | 850-4 | lld:pubmed |
| pubmed-article:11017191 | pubmed:dateRevised | 2005-11-16 | lld:pubmed |
| pubmed-article:11017191 | pubmed:meshHeading | pubmed-meshheading:11017191... | lld:pubmed |
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| pubmed-article:11017191 | pubmed:meshHeading | pubmed-meshheading:11017191... | lld:pubmed |
| pubmed-article:11017191 | pubmed:meshHeading | pubmed-meshheading:11017191... | lld:pubmed |
| pubmed-article:11017191 | pubmed:meshHeading | pubmed-meshheading:11017191... | lld:pubmed |
| pubmed-article:11017191 | pubmed:meshHeading | pubmed-meshheading:11017191... | lld:pubmed |
| pubmed-article:11017191 | pubmed:meshHeading | pubmed-meshheading:11017191... | lld:pubmed |
| pubmed-article:11017191 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11017191 | pubmed:articleTitle | The question remains: is the spliceosome a ribozyme? | lld:pubmed |
| pubmed-article:11017191 | pubmed:affiliation | Graduate Group in Biophysics, University of California, San Francisco, San Francisco, California 94143-0448, USA. | lld:pubmed |
| pubmed-article:11017191 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11017191 | pubmed:publicationType | Review | lld:pubmed |
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