pubmed-article:2717405 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C1335858 | lld:lifeskim |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C0179400 | lld:lifeskim |
pubmed-article:2717405 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:2717405 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:2717405 | pubmed:dateCreated | 1989-6-14 | lld:pubmed |
pubmed-article:2717405 | pubmed:abstractText | The equilibrium constant was determined for the binding of the transcription factor Sp1 to a single consensus GC box DNA recognition site, (5'-GGGGCGGGGC-3'). For these experiments, single copies of the recognition site were synthesized and cloned in a standard plasmid background. Binding was measured either by a footprinting assay modified so that the binding reaction was at equilibrium, or by a gel mobility shift assay. The concentration of active Sp1 in the reactions and the dissociation constant were determined by computer-assisted fitting to theoretical curves. Values for the dissociation constant obtained in different experiments ranged from 4.1 X 10(-10) M to 5.3 X 10(-10) M. Several variants of the consensus recognition site were also tested. An A-substituted variant (5'-GGGGAGGGGC-3') and a T-substituted variant (5'-GGGGTGGGGC-3') were bound 3-fold and 6-fold more weakly than the consensus site, respectively. A G-substituted variant (5'-GGGGGGGGGC-3') was bound at least 30-fold more weakly than the consensus site. These findings help distinguish between alternative models for Sp1-DNA recognition. They are consistent with the presence of specific hydrogen-bond contacts between Sp1 and the central C-G base pair, but provide no particular evidence to support a model where local DNA structure is the dominant factor in the interaction. | lld:pubmed |
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pubmed-article:2717405 | pubmed:language | eng | lld:pubmed |
pubmed-article:2717405 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2717405 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2717405 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2717405 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2717405 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:2717405 | pubmed:author | pubmed-author:DynanW SWS | lld:pubmed |
pubmed-article:2717405 | pubmed:author | pubmed-author:LetovskyJJ | lld:pubmed |
pubmed-article:2717405 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2717405 | pubmed:day | 11 | lld:pubmed |
pubmed-article:2717405 | pubmed:volume | 17 | lld:pubmed |
pubmed-article:2717405 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2717405 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2717405 | pubmed:pagination | 2639-53 | lld:pubmed |
pubmed-article:2717405 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2717405 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2717405 | pubmed:articleTitle | Measurement of the binding of transcription factor Sp1 to a single GC box recognition sequence. | lld:pubmed |
pubmed-article:2717405 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309. | lld:pubmed |
pubmed-article:2717405 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2717405 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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