Evidence map›Paper›PMID 12682355›Full record

ArticleNucleic acids research2003

A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily.

Ji Hyung Chung, Eun Kyoung Im, Hyun-Young Park, Jun Hye Kwon, Seahyoung Lee, Jaewon Oh, Ki-Chul Hwang, Jong Ho Lee, Yangsoo Jang

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Structural and Functional Insights into UDGs.Protein and peptide letters · 2025
    Review
  3. Article
  4. Article
  5. Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.Protein science : a publication of the Protein Society · 2016
    Review
  6. Review
  7. Review
  8. Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

9 authors at 1 institution in 1 country.

Ji Hyung ChungYonsei Research Institute of Aging Science, Yonsei University College of Medicine, Yonsei University, Seoul, 120-752, Korea.
Eun Kyoung Im
Hyun-Young Park
Jun Hye Kwon
Seahyoung Lee
Jaewon Oh
Ki-Chul Hwang
Jong Ho Lee
Yangsoo Jang
Yonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase (UDG), a ubiquitous uracil-excising enzyme found in bacteria and eukaryotes, is one of the enzymes that repair this kind of DNA damage. To date, no UDG-coding gene has been identified in Methanococcus jannaschii, although its entire genome was deciphered. Here, we have identified and characterized a novel UDG from M.jannaschii designated as MjUDG. It efficiently removed uracil from both single- and double-stranded DNA. MjUDG also catalyzes the excision of 8-oxoguanine from DNA. MjUDG has a helix-hairpin-helix motif and a [4Fe-4S]-binding cluster that is considered to be important for the DNA binding and catalytic activity. Although MjUDG shares these features with other structural families such as endonuclease III and mismatch-specific DNA glycosylase (MIG), unique conserved amino acids and substrate specificity distinguish MjUDG from other families. Also, a homologous member of MjUDG was identified in Aquifex aeolicus. We report that MjUDG belongs to a novel UDG family that has not been described to date.

Indexed as

DNA GlycosylasesAmino Acid SequenceArchaeal ProteinsDNA RepairEscherichia coliGuanosineMethanococcusMolecular Sequence DataN-Glycosyl HydrolasesOligonucleotidesPhylogenyRecombinant ProteinsSequence Homology, Amino AcidSubstrate SpecificityUracil-DNA Glycosidase8-hydroxyguanosineArchaeal ProteinsDNA-3-methyladenine glycosidase IIDNA GlycosylasesGuanosineN-Glycosyl HydrolasesOligonucleotidesRecombinant ProteinsUracil-DNA Glycosidase

Identifiers

PMID12682355
PMCPMC153747
OpenAlexW2129133561

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.