Evidence map›Paper›PMID 30268365›Full record

ArticleDNA repair2018

Nucleosomes and the three glycosylases: High, medium, and low levels of excision by the uracil DNA glycosylase superfamily.

Mary E Tarantino, Blaine J Dow, Alexander C Drohat, Sarah Delaney

Abstract read
In one paragraph

Article in DNA repair, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. DNA Glycosylases Define the Outcome of Endogenous Base Modifications.International journal of molecular sciences · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Generation of Recombinant Nucleosomes Containing Site-Specific DNA Damage.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Article
  15. DNA Methyltransferases and DNA Damage.Advances in experimental medicine and biology · 2022
    Article
  16. Review
  17. Article
  18. The Multiple Cellular Roles of SMUG1 in Genome Maintenance and Cancer.International journal of molecular sciences · 2021
    Review
  19. Review
  20. Review
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

4 authors at 2 institutions in 1 country.

Mary E TarantinoDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI, 02912, United States.
Blaine J DowDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD, 21201, United States.
Alexander C DrohatDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD, 21201, United States; University of Maryland Marlene and Stewart Greenebaum Cancer Center, Baltimore, MD, 21201, United States.
Sarah DelaneyDepartment of Chemistry, Brown University, Providence, RI, 02912, United States. Electronic address: Sarah_Delaney@brown.edu.
Brown University · USUniversity of Maryland, Baltimore · US

Funding

Structure and Mechanism of CpG specific DNA glycosylasesR01GM072711 · NIGMS · WADSWORTH CENTER · PI DROHAT, ALEX C · 2005 to 2020
$5.0M
Predoctoral Training in the Molecular Biology of AgingT32AG041688 · NIA · BROWN UNIVERSITY · PI NICOLA NERETTI, John M Sedivy · 2012 to 2026
$3.5M
NIA NIH HHS T32 AG041688NIGMS NIH HHS R01 GM072711
6 · The paper itself

Abstract

Human cells express the UDG superfamily of glycosylases, which excise uracil (U) from the genome. The three members of this structural superfamily are uracil DNA glycosylase (UNG/UDG), single-strand selective monofunctional uracil DNA glycosylase (SMUG1), and thymine DNA glycosylase (TDG). We previously reported that UDG is efficient at removing U from DNA packaged into nucleosome core particles (NCP) and is minimally affected by the histone proteins when acting on an outward-facing U in the dyad region. In an effort to determine whether this high activity is a general property of the UDG superfamily of glycosylases, we compare the activity of UDG, SMUG1, and TDG on a U:G wobble base pair using NCP assembled from Xenopus laevis histones and the Widom 601 positioning sequence. We found that while UDG is highly active, SMUG1 is severely inhibited on NCP and this inhibition is independent of sequence context. Here we also provide the first report of TDG activity on an NCP, and found that TDG has an intermediate level of activity in excision of U and is severely inhibited in its excision of T. These results are discussed in the context of cellular roles for each of these enzymes.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsDNA RepairHumansKineticsModels, MolecularNucleosomesProtein ConformationThymine DNA GlycosylaseUracilUracil-DNA GlycosidaseXenopus laevisNucleosomesThymine DNA GlycosylaseUracilUracil-DNA GlycosidaseBase excision repairNucleosome core particleSingle-strand selective monofunctional uracil DNA glycosylaseThymine DNA glycosylaseUracil DNA glycosylase

Identifiers

PMID30268365
PMCPMC6420825
OpenAlexW2890191449

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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.