| pubmed-article:1390733 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1390733 | lifeskim:mentions | umls-concept:C0242958 | lld:lifeskim |
| pubmed-article:1390733 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:1390733 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:1390733 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:1390733 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:1390733 | lifeskim:mentions | umls-concept:C0046798 | lld:lifeskim |
| pubmed-article:1390733 | pubmed:issue | 40 | lld:pubmed |
| pubmed-article:1390733 | pubmed:dateCreated | 1992-11-18 | lld:pubmed |
| pubmed-article:1390733 | pubmed:abstractText | The reaction of cyanomorpholinoadriamycin (CMA) with DNA results in the formation of sequence-specific complexes with DNA. These complexes were revealed as blocked transcripts in an in vitro transcription assay--of 14 high-intensity blockages detected in the 120 bp probed in this assay, 12 were prior to GpG or CpC sequences. Slow read-through past the first few sites exhibited first-order kinetics, with half-lives of 25-200 min. Bidirectional transcription footprinting revealed nine high-intensity sites, eight of which were defined by a GpG element (nontemplate strand). Reaction of CMA with single-strand DNA, followed by a primer-extension assay, revealed four major blockages all of which were at GpG sites on the initial single-strand DNA. From a combination of these three experimental approaches, it appears that CMA yields dominantly intrastrand cross-links between adjacent guanine residues. Since CMA is also known to form interstrand cross-links, these appear to occur at GpC sequences but are minor in comparison to the extent of formation of intrastrand cross-links. | lld:pubmed |
| pubmed-article:1390733 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1390733 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1390733 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1390733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1390733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1390733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1390733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1390733 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1390733 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1390733 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1390733 | pubmed:author | pubmed-author:PhillipsD RDR | lld:pubmed |
| pubmed-article:1390733 | pubmed:author | pubmed-author:CullinaneCC | lld:pubmed |
| pubmed-article:1390733 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1390733 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:1390733 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:1390733 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1390733 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1390733 | pubmed:pagination | 9513-9 | lld:pubmed |
| pubmed-article:1390733 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1390733 | pubmed:meshHeading | pubmed-meshheading:1390733-... | lld:pubmed |
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| pubmed-article:1390733 | pubmed:meshHeading | pubmed-meshheading:1390733-... | lld:pubmed |
| pubmed-article:1390733 | pubmed:meshHeading | pubmed-meshheading:1390733-... | lld:pubmed |
| pubmed-article:1390733 | pubmed:meshHeading | pubmed-meshheading:1390733-... | lld:pubmed |
| pubmed-article:1390733 | pubmed:meshHeading | pubmed-meshheading:1390733-... | lld:pubmed |
| pubmed-article:1390733 | pubmed:meshHeading | pubmed-meshheading:1390733-... | lld:pubmed |
| pubmed-article:1390733 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1390733 | pubmed:articleTitle | In vitro transcription analysis of DNA adducts induced by cyanomorpholinoadriamycin. | lld:pubmed |
| pubmed-article:1390733 | pubmed:affiliation | Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia. | lld:pubmed |
| pubmed-article:1390733 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1390733 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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