| pubmed-article:7613089 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7613089 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:7613089 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7613089 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7613089 | lifeskim:mentions | umls-concept:C0754910 | lld:lifeskim |
| pubmed-article:7613089 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7613089 | pubmed:dateCreated | 1995-8-22 | lld:pubmed |
| pubmed-article:7613089 | pubmed:abstractText | Recent work has established that the Escherichia coli RNA polymerase alpha subunit consists of an amino-terminal domain containing determinants for interaction with the remainder of RNA polymerase, a carboxy-terminal domain containing determinants for interaction with DNA and interaction with transcriptional activator proteins, and a 13-36 amino acid unstructured and/or flexible linker. These findings suggest a simple, integrated model for the mechanism of involvement of alpha in promoter recognition and transcriptional activation. | lld:pubmed |
| pubmed-article:7613089 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7613089 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7613089 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7613089 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7613089 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7613089 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7613089 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7613089 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7613089 | pubmed:issn | 0959-437X | lld:pubmed |
| pubmed-article:7613089 | pubmed:author | pubmed-author:BusbySS | lld:pubmed |
| pubmed-article:7613089 | pubmed:author | pubmed-author:EbrightR HRH | lld:pubmed |
| pubmed-article:7613089 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7613089 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:7613089 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7613089 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7613089 | pubmed:pagination | 197-203 | lld:pubmed |
| pubmed-article:7613089 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7613089 | pubmed:meshHeading | pubmed-meshheading:7613089-... | lld:pubmed |
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| pubmed-article:7613089 | pubmed:meshHeading | pubmed-meshheading:7613089-... | lld:pubmed |
| pubmed-article:7613089 | pubmed:meshHeading | pubmed-meshheading:7613089-... | lld:pubmed |
| pubmed-article:7613089 | pubmed:meshHeading | pubmed-meshheading:7613089-... | lld:pubmed |
| pubmed-article:7613089 | pubmed:meshHeading | pubmed-meshheading:7613089-... | lld:pubmed |
| pubmed-article:7613089 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7613089 | pubmed:articleTitle | The Escherichia coli RNA polymerase alpha subunit: structure and function. | lld:pubmed |
| pubmed-article:7613089 | pubmed:affiliation | Department of Chemistry, Rutgers University, New Brunswick, New Jersey 08855, USA. | lld:pubmed |
| pubmed-article:7613089 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7613089 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7613089 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7613089 | pubmed:publicationType | Review | lld:pubmed |
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