Evidence map›Paper›PMID 14657033›Full record

ArticleThe EMBO journal2003

Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis.

Caixia Guo, Paula L Fischhaber, Margaret J Luk-Paszyc, Yuji Masuda, Jing Zhou, Kenji Kamiya, Caroline Kisker, Errol C Friedberg

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 194 papers.

0numbers the graph read from it
0cells of the map it votes in
194citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

194 citing papers in PubMed, 358 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. eLife · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. The Catalytic Activity of Human REV1 on Undamaged and Damaged DNA.International journal of molecular sciences · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Mammalian life depends on two distinct pathways of DNA damage tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

134 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Caixia GuoLaboratory of Molecular Pathology, Department of Pathology, University of Texas Southwestern Medical Center, Dallas,TX 75390-9072, USA.
Paula L Fischhaber
Margaret J Luk-Paszyc
Yuji Masuda
Jing Zhou
Kenji Kamiya
Caroline Kisker
Errol C Friedberg
The University of Texas Southwestern Medical Center · US

Funding

MOUSE MODELS OF DNA REPAIR - DEFECTIVE HUMAN DISEASESR01ES011344 · NIEHS · UT SOUTHWESTERN MEDICAL CENTER · PI FRIEDBERG, ERROL · 2001 to 2011
$3.3M
NIEHS NIH HHS ES11344NIEHS NIH HHS R01 ES011344
6 · The paper itself

Abstract

Pol kappa and Rev1 are members of the Y family of DNA polymerases involved in tolerance to DNA damage by replicative bypass [translesion DNA synthesis (TLS)]. We demonstrate that mouse Rev1 protein physically associates with Pol kappa. We show too that Rev1 interacts independently with Rev7 (a subunit of a TLS polymerase, Pol zeta) and with two other Y-family polymerases, Pol iota and Pol eta. Mouse Pol kappa, Rev7, Pol iota and Pol eta each bind to the same approximately 100 amino acid C-terminal region of Rev1. Furthermore, Rev7 competes directly with Pol kappa for binding to the Rev1 C-terminus. Notwithstanding the physical interaction between Rev1 and Pol kappa, the DNA polymerase activity of each measured by primer extension in vitro is unaffected by the complex, either when extending normal primer-termini, when bypassing a single thymine glycol lesion, or when extending certain mismatched primer termini. Our observations suggest that Rev1 plays a role(s) in mediating protein-protein interactions among DNA polymerases required for TLS. The precise function(s) of these interactions during TLS remains to be determined.

Indexed as

DNA DamageDNA RepairAnimalsBase SequenceBinding SitesCloning, MolecularDNA-Directed DNA PolymeraseDNA PrimersKineticsMiceNucleotidyltransferasesPlasmidsRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsY-Family DNA PolymerasesDNA-Directed DNA PolymeraseDNA PrimersNucleotidyltransferasesPolk protein, mouseRecombinant ProteinsREV1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsY-Family DNA Polymerases

Identifiers

PMID14657033
PMCPMC291821
OpenAlexW2024703739

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.