Evidence map›Paper›PMID 12821945›Full record

ArticleOncogene2003

p53 mutated in the transactivation domain retains regulatory functions in homology-directed double-strand break repair.

Gisa S Boehden, Nuray Akyüz, Klaus Roemer, Lisa Wiesmüller

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2003. 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
1.7field-weighted citation impact, top 17% 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, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. p53 and its isoforms in DNA double-stranded break repair.Journal of Zhejiang University. Science. B · 2019
    Review
  8. p53 in the DNA-Damage-Repair Process.Cold Spring Harbor perspectives in medicine · 2016
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

4 authors at 3 institutions in 1 country.

Gisa S BoehdenGynaecological Oncology, Universitätsfrauenklinik, D-89075 Ulm, Germany.
Nuray Akyüz
Klaus Roemer
Lisa Wiesmüller
Universitäts Frauenklinik · DELeibniz Institute of Virology (LIV) · DESaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumor suppressor p53 transcriptionally transactivates cellular target genes that are implicated in growth control, apoptosis, and DNA repair. However, several studies involving p53 core domain mutants suggested that regulatory functions in recombinative repair do not require transcriptional transactivation and are separable from growth-regulation and apoptosis. Leu22 and Trp23 within the transactivation domain of human p53 play a critical role in binding basal components of the transcription machinery and, therefore, in the transactivation activity of p53. To further delineate whether p53 target genes are involved in recombination regulation, we ectopically expressed p53(22Q,23S) in p53-negative cell lines, which carry reporter systems for different homology-directed double-strand break (DSB) repair events. Like wild-type p53, p53(22Q,23S) efficiently downregulated homologous recombination on two chromosomally integrated substrates without affecting exchange on a substrate for the compound pathway of gene conversion and nonhomologous end joining. Only upon lowering the p53 protein to DNA substrate ratio by several orders of magnitude, we noticed a weak defect of a p53 transactivation domain mutant in DSB repair assays. In conclusion, molecular interactions of p53 within the N-terminal domain are not required to restrain DNA recombination, but might contribute to this genome stabilizing function.

Indexed as

DNA DamageDNA RepairGenes, p53MutationTranscriptional ActivationApoptosisDown-RegulationGreen Fluorescent ProteinsHumansK562 CellsLeucineLuminescent ProteinsModels, BiologicalProtein Structure, TertiaryRecombination, GeneticTryptophanGreen Fluorescent ProteinsLeucineLuminescent ProteinsTryptophan

Identifiers

PMID12821945
OpenAlexW1970542601

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.