pubmed-article:12764140 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12764140 | lifeskim:mentions | umls-concept:C0035679 | lld:lifeskim |
pubmed-article:12764140 | lifeskim:mentions | umls-concept:C1519591 | lld:lifeskim |
pubmed-article:12764140 | lifeskim:mentions | umls-concept:C1156205 | lld:lifeskim |
pubmed-article:12764140 | pubmed:issue | 29 | lld:pubmed |
pubmed-article:12764140 | pubmed:dateCreated | 2003-7-14 | lld:pubmed |
pubmed-article:12764140 | pubmed:abstractText | mRNA synthesis in eukaryotic organisms is a key biological process that is regulated at multiple levels. From the covalent modifications of chromatin by a number of chromatin remodeling complexes during the initiation and activation steps of transcription to the processing of mRNA transcripts, a very large consortium of proteins and multiprotein complexes is critical for gene expression by RNA polymerase II. The list of proteins essential for the successful synthesis of mRNA continues to grow at a rapid pace. Recent advances in this area of research have been focused on transcription through chromatin. In this article, we will review the recent literature linking the key biochemical process of transcriptional elongation by RNA polymerase II to histone methylation by COMPASS, Dot1p, and Set2 methyltransferases. | lld:pubmed |
pubmed-article:12764140 | pubmed:language | eng | lld:pubmed |
pubmed-article:12764140 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12764140 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12764140 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12764140 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12764140 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12764140 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12764140 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12764140 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12764140 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12764140 | pubmed:author | pubmed-author:ShilatifardAl... | lld:pubmed |
pubmed-article:12764140 | pubmed:author | pubmed-author:GerberMarkM | lld:pubmed |
pubmed-article:12764140 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12764140 | pubmed:day | 18 | lld:pubmed |
pubmed-article:12764140 | pubmed:volume | 278 | lld:pubmed |
pubmed-article:12764140 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12764140 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12764140 | pubmed:pagination | 26303-6 | lld:pubmed |
pubmed-article:12764140 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:12764140 | pubmed:meshHeading | pubmed-meshheading:12764140... | lld:pubmed |
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pubmed-article:12764140 | pubmed:meshHeading | pubmed-meshheading:12764140... | lld:pubmed |
pubmed-article:12764140 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12764140 | pubmed:articleTitle | Transcriptional elongation by RNA polymerase II and histone methylation. | lld:pubmed |
pubmed-article:12764140 | pubmed:affiliation | Department of Biochemistry and the St. Louis University Cancer Center, St. Louis University School of Medicine, St. Louis, Missouri 63104, USA. | lld:pubmed |
pubmed-article:12764140 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12764140 | pubmed:publicationType | Review | lld:pubmed |
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