pubmed-article:1690088 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0025966 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0950398 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0001186 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
pubmed-article:1690088 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
pubmed-article:1690088 | pubmed:issue | 2-3 | lld:pubmed |
pubmed-article:1690088 | pubmed:dateCreated | 1990-4-23 | lld:pubmed |
pubmed-article:1690088 | pubmed:abstractText | The effect of dimeric DNA intercalating compounds was assayed on a purified AP endonuclease from Microccoccus luteus using apurinic supercoiled PM2 DNA as a substrate. Binding on apurinic sites was estimated through the competition with the intercalating compound, 9-NH2-ellipticine, which displays great specificity for apurinic sites. An acridine dimer with a spermine linker is at 0.1 microM the best inhibitor of cleavage at the apurinic site induced either by the AP endonuclease or by 9-NH2-ellipticine. Bisintercalating agents are more effective inhibitors of AP endonuclease than monointercalating ones. Most effective inhibitors among dimers have acridine residues. | lld:pubmed |
pubmed-article:1690088 | pubmed:language | eng | lld:pubmed |
pubmed-article:1690088 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1690088 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1690088 | pubmed:issn | 0009-2797 | lld:pubmed |
pubmed-article:1690088 | pubmed:author | pubmed-author:PierreJJ | lld:pubmed |
pubmed-article:1690088 | pubmed:author | pubmed-author:RoquesBB | lld:pubmed |
pubmed-article:1690088 | pubmed:author | pubmed-author:GarbayCC | lld:pubmed |
pubmed-article:1690088 | pubmed:author | pubmed-author:MalvyCC | lld:pubmed |
pubmed-article:1690088 | pubmed:author | pubmed-author:MarkovitsJJ | lld:pubmed |
pubmed-article:1690088 | pubmed:author | pubmed-author:LefrançoisMM | lld:pubmed |
pubmed-article:1690088 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1690088 | pubmed:volume | 73 | lld:pubmed |
pubmed-article:1690088 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1690088 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1690088 | pubmed:pagination | 249-60 | lld:pubmed |
pubmed-article:1690088 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:1690088 | pubmed:meshHeading | pubmed-meshheading:1690088-... | lld:pubmed |
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pubmed-article:1690088 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:1690088 | pubmed:articleTitle | Low concentrations of acridine dimers inhibit micrococcus AP endonuclease through interaction with apurinic sites in DNA. | lld:pubmed |
pubmed-article:1690088 | pubmed:affiliation | URA 158 CNRS, U-140 INSERM, Institut G. Roussy, Villejuif, France. | lld:pubmed |
pubmed-article:1690088 | pubmed:publicationType | Journal Article | lld:pubmed |