| pubmed-article:8380128 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0002699 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0012863 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0015133 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C1519554 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0013203 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0039476 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0314603 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0002085 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:8380128 | lifeskim:mentions | umls-concept:C0332324 | lld:lifeskim |
| pubmed-article:8380128 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8380128 | pubmed:dateCreated | 1993-1-25 | lld:pubmed |
| pubmed-article:8380128 | pubmed:abstractText | We have developed a simple system for determining the specific contribution of topoisomerase II targeting to the cytotoxic activity of a drug. We have constructed yeast strains that are permeable to anti-topoisomerase II drugs, carry a DNA repair mutation, rad52, and also have a temperature sensitive topoisomerase II mutation, top2-1. Strains carrying the top2-1 mutation have nearly normal topoisomerase II activity at 25 degrees C but less than 10% of wild type activity at 36 degrees C. We find that at a semi-permissive temperature (30 degrees C), there is sufficient topoisomerase II activity for viability; but since the topoisomerase II activity is greatly reduced, the cells are very resistant to anti-topoisomerase II drugs. Conversely, such cells are hypersensitive to the topoisomerase I inhibitor camptothecin. These results provide strong support for the model that drug stabilized DNA cleavage, rather than a lack of enzyme activity, is responsible for cell killing by eukaryotic anti-topoisomerase II agents. They also show that there is a minimum level of topoisomerase II activity in yeast that is consistent with viability but also allows a high degree of resistance to anti-topoisomerase II agents. | lld:pubmed |
| pubmed-article:8380128 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8380128 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8380128 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8380128 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8380128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8380128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8380128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8380128 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8380128 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8380128 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:8380128 | pubmed:author | pubmed-author:LieY HYH | lld:pubmed |
| pubmed-article:8380128 | pubmed:author | pubmed-author:NitissJ LJL | lld:pubmed |
| pubmed-article:8380128 | pubmed:author | pubmed-author:HsiungYY | lld:pubmed |
| pubmed-article:8380128 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8380128 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8380128 | pubmed:volume | 53 | lld:pubmed |
| pubmed-article:8380128 | pubmed:geneSymbol | top2-1 | lld:pubmed |
| pubmed-article:8380128 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8380128 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8380128 | pubmed:pagination | 89-93 | lld:pubmed |
| pubmed-article:8380128 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8380128 | pubmed:meshHeading | pubmed-meshheading:8380128-... | lld:pubmed |
| pubmed-article:8380128 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8380128 | pubmed:articleTitle | A temperature sensitive topoisomerase II allele confers temperature dependent drug resistance on amsacrine and etoposide: a genetic system for determining the targets of topoisomerase II inhibitors. | lld:pubmed |
| pubmed-article:8380128 | pubmed:affiliation | Division of Hematology/Oncology, Children's Hospital of Los Angeles, California 90027. | lld:pubmed |
| pubmed-article:8380128 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8380128 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8380128 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8380128 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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