Evidence map›Paper›PMID 17426133›Full record

ArticleNucleic acids research2007

The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase beta in long patch base excision repair.

Agnieszka Gembka, Magali Toueille, Ekaterina Smirnova, Rainer Poltz, Elena Ferrari, Giuseppe Villani, Ulrich Hübscher

Abstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
–field-weighted citation impact
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

46 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. The Role of Protein Arginine Methyltransferases in DNA Damage Response.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Damage sensor role of UV-DDB during base excision repair.Nature structural & molecular biology · 2019
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

7 authors.

Agnieszka GembkaInstitute of Veterinary Biochemistry and Molecular Biology, University of Zürich-Irchel, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland.
Magali Toueille
Ekaterina Smirnova
Rainer Poltz
Elena Ferrari
Giuseppe Villani
Ulrich Hübscher

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Growing evidence suggests that the Rad9-Rad1-Hus1 complex (the 9-1-1 complex), besides its functions in DNA damage sensing and signaling pathways, plays also a direct role in various DNA repair processes. Recent studies have demonstrated that the 9-1-1 complex physically and functionally interacts with several components of the base excision repair (BER) machinery namely DNA polymerase beta (Pol beta), flap endonuclease 1 (Fen 1), DNA ligase I (Lig I) and the MutY homologue of Schizosaccharomyces pombe. In this work, we found for the first time that the 9-1-1 complex interacts in vitro and in vivo with the apurinic/apyrimidinic endonuclease 1 (APE 1), an early component of BER, and can stimulate its AP-endonuclease activity. Moreover, we show that the 9-1-1 complex possesses a stimulatory effect on long patch base excision repair (LP-BER) reconstituted in vitro. The enhancement of LP-BER activity is due to the specific stimulation of the two early components of the repair machinery, namely APE 1 and Pol beta, suggesting a hierarchy of interactions between the 9-1-1 complex and the BER proteins acting in the repairosome. Overall, our results indicate that the 9-1-1 complex is directly involved in LP-BER, thus providing a possible link between DNA damage checkpoints and BER.

Indexed as

DNA RepairCell Cycle ProteinsCell LineDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA Ligase ATPDNA LigasesDNA Polymerase betaEnzyme ActivationExonucleasesFlap EndonucleasesHumansAPEX1 protein, humanCell Cycle ProteinsDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA Ligase ATPDNA LigasesDNA Polymerase betaExonucleasesFEN1 protein, humanFlap EndonucleasesHUS1B protein, humanHUS1 protein, humanLIG1 protein, humanRad1 protein, humanrad9 protein

Identifiers

PMID17426133
PMCPMC1885638

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Registered trials

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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.