pubmed-article:2544029 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C0926407 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C0063690 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
pubmed-article:2544029 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:2544029 | pubmed:issue | 4911 | lld:pubmed |
pubmed-article:2544029 | pubmed:dateCreated | 1989-7-24 | lld:pubmed |
pubmed-article:2544029 | pubmed:abstractText | The multiprotein-DNA complexes that participate in bacteriophage lambda site-specific recombination were used to study the combined effect of protein-induced bending and protein-mediated looping of DNA. The protein integrase (Int) is a monomer with two autonomous DNA binding domains of different sequence specificity. Stimulation of Int binding and cleavage at the low affinity core-type DNA sites required interactions with the high affinity arm-type sites and depended on simultaneous binding of the sequence-specific DNA bending protein IHF (integration host factor). The bivalent DNA binding protein is positioned at high affinity sites and directed, by a DNA bending protein, to interactions with distant lower affinity sites. Assembly of this complex is independent of protein-protein interactions. | lld:pubmed |
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pubmed-article:2544029 | pubmed:language | eng | lld:pubmed |
pubmed-article:2544029 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2544029 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2544029 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2544029 | pubmed:month | Jun | lld:pubmed |
pubmed-article:2544029 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:2544029 | pubmed:author | pubmed-author:KimSS | lld:pubmed |
pubmed-article:2544029 | pubmed:author | pubmed-author:LandyAA | lld:pubmed |
pubmed-article:2544029 | pubmed:author | pubmed-author:Moitoso de... | lld:pubmed |
pubmed-article:2544029 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2544029 | pubmed:day | 23 | lld:pubmed |
pubmed-article:2544029 | pubmed:volume | 244 | lld:pubmed |
pubmed-article:2544029 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2544029 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2544029 | pubmed:pagination | 1457-61 | lld:pubmed |
pubmed-article:2544029 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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pubmed-article:2544029 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2544029 | pubmed:articleTitle | DNA looping generated by DNA bending protein IHF and the two domains of lambda integrase. | lld:pubmed |
pubmed-article:2544029 | pubmed:affiliation | Division of Biology and Medicine, Brown University, Providence, RI 02912. | lld:pubmed |
pubmed-article:2544029 | pubmed:publicationType | Journal Article | lld:pubmed |