| pubmed-article:3233212 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3233212 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:3233212 | lifeskim:mentions | umls-concept:C0002503 | lld:lifeskim |
| pubmed-article:3233212 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:3233212 | lifeskim:mentions | umls-concept:C1521990 | lld:lifeskim |
| pubmed-article:3233212 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:3233212 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:3233212 | pubmed:dateCreated | 1989-5-1 | lld:pubmed |
| pubmed-article:3233212 | pubmed:abstractText | Complexes of 9-aminoacridine and two derivatives with oligomers based on the sequence of a hot spot for frame-shift mutations, 5'dGATGGGGCAG, are investigated by proton NMR and equilibrium dialysis. Competition dialysis experiments show that the drug binds bulge-containing oligomers more strongly than regular duplexes of similar sequence and length, with one apparent strong site. A duplex containing an extra cytidine in a run of C's has the highest affinity for 9-aminoacridine among the sequences tested. An oligomer containing five consecutive G.C pairs shows cooperative drug binding, indicating that G tracts of this length may have an altered helical structure. Complexes of a regular 8-mer and a 9-mer containing a bulged guanosine are examined in detail by two-dimensional NMR techniques. 9-Aminoacridine preferentially binds at TpG sites in the 8-mer but binds primarily at the bulged guanosine in the G-bulge 9-mer. Drug-DNA NOE's in the 8-mer complex are compared with the crystal structure of 9-aminoacridine and 5-iodo-CpG [Sakore et al. (1979) J. Mol. Biol. 135, 763-785]. The NMR data suggest that the drug intercalates across the base pairs of both strands with the amino group projecting into the minor groove. | lld:pubmed |
| pubmed-article:3233212 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3233212 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3233212 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3233212 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3233212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3233212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3233212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3233212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3233212 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3233212 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3233212 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:3233212 | pubmed:author | pubmed-author:CrothersD MDM | lld:pubmed |
| pubmed-article:3233212 | pubmed:author | pubmed-author:WoodsonS ASA | lld:pubmed |
| pubmed-article:3233212 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3233212 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:3233212 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:3233212 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3233212 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3233212 | pubmed:pagination | 8904-14 | lld:pubmed |
| pubmed-article:3233212 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:meshHeading | pubmed-meshheading:3233212-... | lld:pubmed |
| pubmed-article:3233212 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3233212 | pubmed:articleTitle | Binding of 9-aminoacridine to bulged-base DNA oligomers from a frame-shift hot spot. | lld:pubmed |
| pubmed-article:3233212 | pubmed:affiliation | Department of Chemistry, Yale University, New Haven, Connecticut 06511. | lld:pubmed |
| pubmed-article:3233212 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3233212 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3233212 | lld:pubmed |
