| pubmed-article:2571937 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C0206558 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C1442824 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C0040627 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:2571937 | lifeskim:mentions | umls-concept:C0733688 | lld:lifeskim |
| pubmed-article:2571937 | pubmed:issue | 6243 | lld:pubmed |
| pubmed-article:2571937 | pubmed:dateCreated | 1989-11-16 | lld:pubmed |
| pubmed-article:2571937 | pubmed:abstractText | The herpes simplex virus transactivator VP16 participates in the formation of a multiprotein-DNA complex with the ubiquitous octamer-motif-binding factor Oct-1. Complex formation is dependent on specific amino acids in the Oct-1 homoeodomain which are in positions analogous to positive control mutations in helix 2 of the lambda phage repressor helix-turn-helix motif, indicating that this structure is an ancient target for protein-protein interactions mediating transcriptional control. | lld:pubmed |
| pubmed-article:2571937 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2571937 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2571937 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2571937 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2571937 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2571937 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:2571937 | pubmed:author | pubmed-author:TanakaMM | lld:pubmed |
| pubmed-article:2571937 | pubmed:author | pubmed-author:SternSS | lld:pubmed |
| pubmed-article:2571937 | pubmed:author | pubmed-author:HerrWW | lld:pubmed |
| pubmed-article:2571937 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2571937 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:2571937 | pubmed:volume | 341 | lld:pubmed |
| pubmed-article:2571937 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2571937 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2571937 | pubmed:pagination | 624-30 | lld:pubmed |
| pubmed-article:2571937 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2571937 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2571937 | pubmed:articleTitle | The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16. | lld:pubmed |
| pubmed-article:2571937 | pubmed:affiliation | Cold Spring Harbor Laboratory, New York 11724. | lld:pubmed |
| pubmed-article:2571937 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2571937 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2571937 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2571937 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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