| pubmed-article:12176389 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0035679 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0086860 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12176389 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:12176389 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:12176389 | pubmed:dateCreated | 2002-8-14 | lld:pubmed |
| pubmed-article:12176389 | pubmed:abstractText | An 18 A resolution structure of the 12-subunit yeast RNA polymerase II (RNAPII) calculated from electron microscope images of single particles preserved in amorphous ice reveals the conformation of the enzyme in solution. The Rpb4/Rpb7 polymerase subunit complex was localized and found to be ideally positioned to determine the path of the nascent RNA transcript. The RNAPII structure suggests a revised mode of interaction with promoter DNA and demonstrates that regulation of RNAPII must involve structural changes that render the enzyme competent for initiation. | lld:pubmed |
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| pubmed-article:12176389 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12176389 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12176389 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12176389 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12176389 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12176389 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12176389 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12176389 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:12176389 | pubmed:author | pubmed-author:CraigheadJohn... | lld:pubmed |
| pubmed-article:12176389 | pubmed:author | pubmed-author:ChangWei-hauW... | lld:pubmed |
| pubmed-article:12176389 | pubmed:author | pubmed-author:AsturiasFranc... | lld:pubmed |
| pubmed-article:12176389 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12176389 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:12176389 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12176389 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12176389 | pubmed:pagination | 1117-25 | lld:pubmed |
| pubmed-article:12176389 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:12176389 | pubmed:meshHeading | pubmed-meshheading:12176389... | lld:pubmed |
| pubmed-article:12176389 | pubmed:meshHeading | pubmed-meshheading:12176389... | lld:pubmed |
| pubmed-article:12176389 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12176389 | pubmed:articleTitle | Structure of yeast RNA polymerase II in solution: implications for enzyme regulation and interaction with promoter DNA. | lld:pubmed |
| pubmed-article:12176389 | pubmed:affiliation | Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:12176389 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12176389 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12176389 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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