Evidence map›Paper›PMID 19136958›Full record

ArticleNature structural & molecular biology2009

Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair.

Bjørn Dalhus, Andrew S Arvai, Ida Rosnes, Øyvind E Olsen, Paul H Backe, Ingrun Alseth, Honghai Gao, Weiguo Cao, John A Tainer, Magnar Bjørås

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

60 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Structural and Functional Insights into UDGs.Protein and peptide letters · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Structural basis for recognition of distinct deaminated DNA lesions by endonuclease Q.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Bjørn DalhusCentre for Molecular Biology and Neuroscience, Rikshospitalet University Hospital, Sognsvannsveien 20, N-0027 Oslo, Norway.
Andrew S Arvai
Ida Rosnes
Øyvind E Olsen
Paul H Backe
Ingrun Alseth
Honghai Gao
Weiguo Cao
John A Tainer
Magnar Bjørås
Oslo University Hospital · NOUniversity of Oslo · NOClemson University · USScripps Research Institute · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
STRUCTURE AND FUNCTION OF METALLOENZYMES FOR DNA REPAIRR01GM046312 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1991 to 2012
$5.9M
NCI NIH HHS P01 CA092584NIGMS NIH HHS R01 GM046312
6 · The paper itself

Abstract

Endonuclease V (EndoV) initiates a major base-repair pathway for nitrosative deamination resulting from endogenous processes and increased by oxidative stress from mitochondrial dysfunction or inflammatory responses. We solved the crystal structures of Thermotoga maritima EndoV in complex with a hypoxanthine lesion substrate and with product DNA. The PYIP wedge motif acts as a minor groove-damage sensor for helical distortions and base mismatches and separates DNA strands at the lesion. EndoV incises DNA with an unusual offset nick 1 nucleotide 3' of the lesion, as the deaminated adenine is rotated approximately 90 degrees into a recognition pocket approximately 8 A from the catalytic site. Tight binding by the lesion-recognition pocket in addition to Mg(2+) and hydrogen-bonding interactions to the DNA ends stabilize the product complex, suggesting an orderly recruitment of downstream proteins in this base-repair pathway.

Indexed as

DNA RepairBacterial ProteinsCrystallography, X-RayDeoxyribonuclease (Pyrimidine Dimer)DNADNA DamageHypoxanthineModels, MolecularThermotoga maritimaBacterial ProteinsDeoxyribonuclease (Pyrimidine Dimer)DNAHypoxanthine

Identifiers

PMID19136958
PMCPMC3560532
OpenAlexW2030887477

What OpenQuestion holds

Textmetadata
LicenceTDM
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.