Evidence map›Paper›PMID 26304551›Full record

ArticleNucleic acids research2015

A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily.

Pau Biak Sang, Thiruneelakantan Srinath, Aravind Goud Patil, Eui-Jeon Woo, Umesh Varshney

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Usnic Acid Derivatives as Inhibitors ofInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Structural and Functional Insights into UDGs.Protein and peptide letters · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Bacterial DNA excision repair pathways.Nature reviews. Microbiology · 2022
    Review
  11. Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Detection of Genomic Uracil Patterns.International journal of molecular sciences · 2021
    Review
  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

5 authors at 2 institutions in 2 countries.

Pau Biak SangDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560012, India.
Thiruneelakantan SrinathDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560012, India.
Aravind Goud PatilDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560012, India.
Eui-Jeon WooFunctional Genomic Research Center, Korea Research Institute of Bioscience and Biotechnology, 125 Gwahakro, Yuseongu, Daejeon, South Korea.
Umesh VarshneyDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560012, India Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, 560064, India varshney@mcbl.iisc.ernet.in.
Indian Institute of Science Bangalore · INKorea Research Institute of Bioscience and Biotechnology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uracil DNA glycosylases (UDGs) are an important group of DNA repair enzymes, which pioneer the base excision repair pathway by recognizing and excising uracil from DNA. Based on two short conserved sequences (motifs A and B), UDGs have been classified into six families. Here we report a novel UDG, UdgX, from Mycobacterium smegmatis and other organisms. UdgX specifically recognizes uracil in DNA, forms a tight complex stable to sodium dodecyl sulphate, 2-mercaptoethanol, urea and heat treatment, and shows no detectable uracil excision. UdgX shares highest homology to family 4 UDGs possessing Fe-S cluster. UdgX possesses a conserved sequence, KRRIH, which forms a flexible loop playing an important role in its activity. Mutations of H in the KRRIH sequence to S, G, A or Q lead to gain of uracil excision activity in MsmUdgX, establishing it as a novel member of the UDG superfamily. Our observations suggest that UdgX marks the uracil-DNA for its repair by a RecA dependent process. Finally, we observed that the tight binding activity of UdgX is useful in detecting uracils in the genomes.

Indexed as

Bacterial ProteinsDNADNA-Binding ProteinsDNA RepairMutationMycobacterium smegmatisRec A RecombinasesSequence Homology, Amino AcidStructural Homology, ProteinUracilUracil-DNA GlycosidaseViral ProteinsBacterial ProteinsDNADNA-Binding ProteinsRec A RecombinasesUracilUracil-DNA Glycosidaseuracil-DNA glycosylase inhibitor protein, B. subtilis bacteriophageViral Proteins

Identifiers

PMID26304551
PMCPMC4787834
OpenAlexW2126740644

What OpenQuestion holds

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LicenceCC BY-NC
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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.