Evidence map›Paper›PMID 7603986›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

SCT1 mutants suppress the camptothecin sensitivity of yeast cells expressing wild-type DNA topoisomerase I.

E A Kauh, M A Bjornsti

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 68 citations in OpenAlex.

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  17. Locking the DNA topoisomerase I protein clamp inhibits DNA rotation and induces cell lethality.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  18. CDC45 and DPB11 are required for processive DNA replication and resistance to DNA topoisomerase I-mediated DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  19. A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

E A KauhDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
M A Bjornsti
Harvard University Press · USThomas Jefferson University · US

Funding

DNA TOPOISOMERASE-CAMPTOTHECIN INTERACTIONSR01CA058755 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BJORNSTI, MARY-ANN · 1993 to 2011
$3.2M
NCI NIH HHS CA58755
6 · The paper itself

Abstract

Camptothecin is a potent antineoplastic agent that interferes with the action of eukaryotic DNA topoisomerase I; the covalent enzyme-DNA intermediate is reversibly stabilized, leading to G2 arrest and cell death. We used a genetic screen to identify cellular factors, other than DNA topoisomerase I, that participate in the process of camptothecin-induced cell death. Following ethyl methanesulfonate mutagenesis of top1 delta yeast cells expressing plasmid-borne wild-type DNA topoisomerase I, six dominant suppressors of camptothecin toxicity were isolated that define a single genetic locus, sct1. Mutant SCT1 cells expressed DNA topoisomerase I protein of similar specific activity and camptothecin sensitivity to that of congenic, drug-sensitive sct1 cells, yet were resistant to camptothecin-mediated lethality. Moreover, camptothecin-treated SCT1 cells did not exhibit the G2-arrested, terminal phenotype characteristic of drug-treated wild-type cells. SCT1 cell sensitivity to other DNA-damaging agents suggests that alterations in SCT1 function suppress camptothecin-induced DNA damage produced in the presence of yeast DNA topoisomerase I.

Indexed as

CamptothecinCell CycleDNA-Binding ProteinsDNA Topoisomerases, Type IEthyl MethanesulfonateFungal ProteinsGene ExpressionKineticsMutagenesisSaccharomyces cerevisiaeSpecies SpecificityTranscription FactorsCamptothecinDNA-Binding ProteinsDNA Topoisomerases, Type IEthyl MethanesulfonateFungal ProteinsTranscription Factors

Identifiers

PMID7603986
PMCPMC41505
OpenAlexW1977295594

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.