Evidence map›Paper›PMID 8807283›Full record

ArticleGenetics1996

Bacteriophage T4 mutants hypersensitive to an antitumor agent that induces topoisomerase-DNA cleavage complexes.

D L Woodworth, K N Kreuzer

Abstract read
In one paragraph

Article in Genetics, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. DNA- and DNA-Protein-Crosslink Repair in Plants.International journal of molecular sciences · 2019
    Review
  6. Mechanisms of DNA-protein crosslink repair.Nature reviews. Molecular cell biology · 2017
    Review
  7. Article
  8. Review
  9. Regression supports two mechanisms of fork processing in phage T4.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  10. Article
  11. Bacteriophage T4 genome.Microbiology and molecular biology reviews : MMBR · 2003
    Review
  12. The tight linkage between DNA replication and double-strand break repair in bacteriophage T4.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. The SbcCD nuclease of Escherichia coli is a structural maintenance of chromosomes (SMC) family protein that cleaves hairpin DNA.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  18. Article
  19. Article
  20. 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.

D L WoodworthDepartment of Microbiology, Duke University Medical Center, Durham, North Carolina 27710, USA.
K N Kreuzer
Duke Medical Center · USDuke University · US

Funding

ORGANIZATION AND FUNCTIONS OF CELLULAR STRUCTUREST32GM007184 · NIGMS · DUKE UNIVERSITY · PI JINKS-ROBERTSON, SUE · 1985 to 2019
$18.2M
ANTITUMOR AGENTS AND THE BACTERIOPHAGE T4 TOPOISOMERASER01CA060836 · NCI · DUKE UNIVERSITY · PI KREUZER, KENNETH N · 1993 to 2001
$505k
NCI NIH HHS CA-60836NIGMS NIH HHS 5T32 GM07184
6 · The paper itself

Abstract

Many antitumor agents and antibiotics affect cells by interacting with type II topoisomerases, stabilizing a covalent enzyme-DNA complex. A pathway of recombination can apparently repair this DNA damage. In this study, transposon mutagenesis was used to identify possible components of the repair pathway in bacteriophage T4. Substantial increases in sensitivity to the antitumor agent m-AMSA [4'-(9-acridinylamino)methanesulfon-m-anisidide] were found with transposon insertion mutations that inactivate any of six T4-encoded proteins: UvsY (DNA synaptase accessory protein), UvsW (unknown function), Rnh (RNase H and 5' to 3' DNA exonuclease), alpha-gt (alpha-glucosyl transferase), gp47.1 (uncharacterized), and NrdB (beta subunit of ribonucleotide reductase). The role of the rnh gene in drug sensitivity was further characterized. First, an in-frame rnh deletion mutation was constructed and analyzed, providing evidence that the absence of Rnh protein causes hypersensitivity to m-AMSA. Second, the m-AMSA sensitivity of the rnh-deletion mutant was shown to require a drug-sensitive T4 topoisomerase. Third, analysis of double mutants suggested that uvsW and rnh mutations impair a common step in the recombinational repair pathway for m-AMSA-induced damage. Finally, the rnh-deletion mutant was found to be hypersensitive to UV, implicating Rnh in recombinational repair of UV-induced damage.

Indexed as

Amino Acid SequenceAmsacrineAntineoplastic AgentsBacteriophage T4Base SequenceDNA-Binding ProteinsDNA Topoisomerases, Type IIDNA Transposable ElementsDNA, ViralExodeoxyribonucleasesExodeoxyribonuclease VMembrane ProteinsMolecular Sequence DataMutagenesis, InsertionalRibonuclease HUltraviolet RaysAmsacrineAntineoplastic AgentsDNA-Binding ProteinsDNA Topoisomerases, Type IIDNA Transposable ElementsDNA, ViralExodeoxyribonucleasesExodeoxyribonuclease VMembrane ProteinsRibonuclease HUvsX protein, Enterobacteria phage T4Viral Proteins

Identifiers

PMID8807283
PMCPMC1207380
OpenAlexW2152920971

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.