| pubmed-article:2662013 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C0035681 | lld:lifeskim |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C1332721 | lld:lifeskim |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:2662013 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:2662013 | pubmed:issue | 6227 | lld:pubmed |
| pubmed-article:2662013 | pubmed:dateCreated | 1989-8-2 | lld:pubmed |
| pubmed-article:2662013 | pubmed:abstractText | Actively transcribing eukaryotic RNA polymerase II is highly phosphorylated on its repetitive carboxyl-terminal domain. We have isolated a protein kinase that phosphorylates serine residues in this repetitive domain. A component of this kinase is cdc2, the product of a cell-cycle control gene previously shown to be a component of M-phase-promoting factor and M-phase-specific histone H1 kinase. This observation suggests a role for the cdc2 protein kinase in transcriptional regulation. | lld:pubmed |
| pubmed-article:2662013 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2662013 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2662013 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2662013 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2662013 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2662013 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:2662013 | pubmed:author | pubmed-author:CordenJ LJL | lld:pubmed |
| pubmed-article:2662013 | pubmed:author | pubmed-author:CisekL JLJ | lld:pubmed |
| pubmed-article:2662013 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2662013 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:2662013 | pubmed:volume | 339 | lld:pubmed |
| pubmed-article:2662013 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2662013 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2662013 | pubmed:pagination | 679-84 | lld:pubmed |
| pubmed-article:2662013 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2662013 | pubmed:meshHeading | pubmed-meshheading:2662013-... | lld:pubmed |
| pubmed-article:2662013 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2662013 | pubmed:articleTitle | Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2. | lld:pubmed |
| pubmed-article:2662013 | pubmed:affiliation | Howard Hughes Medical Institute, Johns Hopkins School of Medicine, Baltimore, Maryland 21205. | lld:pubmed |
| pubmed-article:2662013 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2662013 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2662013 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2662013 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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