Evidence map›Paper›PMID 31101917›Full record

ArticleNature chemical biology2019

Covalent binding of uracil DNA glycosylase UdgX to abasic DNA upon uracil excision.

Woo-Chan Ahn, Shashanka Aroli, Jin-Hahn Kim, Jeong Hee Moon, Ga Seal Lee, Min-Ho Lee, Pau Biak Sang, Byung-Ha Oh, Umesh Varshney, Eui-Jeon Woo

Abstract read
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In one paragraph

Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Structural and Functional Insights into UDGs.Protein and peptide letters · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Bacterial DNA excision repair pathways.Nature reviews. Microbiology · 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
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

10 authors at 4 institutions in 2 countries.

Woo-Chan AhnDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
Shashanka AroliDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.
Jin-Hahn KimCreative Research Initiative Center for Chemical Dynamics in Living Cells, Department of Chemistry, Chung-Ang University, Seoul, Korea.
Jeong Hee MoonDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
Ga Seal LeeDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
Min-Ho LeeDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
Pau Biak SangDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.
Byung-Ha OhDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Korea.ORCID http://orcid.org/0000-0002-6437-8470
Umesh VarshneyDepartment of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India. varshney@iisc.ac.in.
Eui-Jeon WooDisease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea. ejwoo@kribb.re.kr.ORCID http://orcid.org/0000-0001-6983-0270
Korea Research Institute of Bioscience and Biotechnology · KRIndian Institute of Science Bangalore · INKorea Advanced Institute of Science and Technology · KRChung-Ang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uracil DNA glycosylases (UDGs) are important DNA repair enzymes that excise uracil from DNA, yielding an abasic site. Recently, UdgX, an unconventional UDG with extremely tight binding to DNA containing uracil, was discovered. The structure of UdgX from Mycobacterium smegmatis in complex with DNA shows an overall similarity to that of family 4 UDGs except for a protruding loop at the entrance of the uracil-binding pocket. Surprisingly, H109 in the loop was found to make a covalent bond to the abasic site to form a stable intermediate, while the excised uracil remained in the pocket of the active site. H109 functions as a nucleophile to attack the oxocarbenium ion, substituting for the catalytic water molecule found in other UDGs. To our knowledge, this change from a catalytic water attack to a direct nucleophilic attack by the histidine residue is unprecedented. UdgX utilizes a unique mechanism of protecting cytotoxic abasic sites from exposure to the cellular environment.

Indexed as

DNA DamageBinding SitesBiocatalysisDNA, BacterialModels, MolecularMycobacterium smegmatisProtein ConformationUracilUracil-DNA GlycosidaseDNA, BacterialUracilUracil-DNA Glycosidase

Identifiers

PMID31101917
OpenAlexW2945194478

What OpenQuestion holds

Textmetadata
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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.