Evidence map›Paper›PMID 23952905›Full record

ArticleThe Biochemical journal2013

Histone deacetylase SIRT1 modulates and deacetylates DNA base excision repair enzyme thymine DNA glycosylase.

Amrita Madabushi, Bor-Jang Hwang, Jin Jin, A-Lien Lu

Abstract read
In one paragraph

Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Fueling genome maintenance: On the versatile roles of NADThe Journal of biological chemistry · 2022
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Nuclear DNA damage signalling to mitochondria in ageing.Nature reviews. Molecular cell biology · 2016
    Review
  17. Review
  18. Review
  19. Sirtuin regulation in aging and injury.Biochimica et biophysica acta · 2015
    Review
  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

4 authors at 1 institution in 1 country.

Amrita Madabushi*Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, U.S.A.
Bor-Jang Hwang
Jin Jin
A-Lien Lu
University of Maryland, Baltimore · US

Funding

REPAIR OF OXIDATIVELY DAMAGED GUANINES IN HUMANR01CA078391 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI LU-CHANG, A-LIEN L · 1998 to 2013
$3.4M
NCI NIH HHS R01 CA078391NCI NIH HHS R01-CA78391
6 · The paper itself

Abstract

TDG (thymine DNA glycosylase) is an essential multifunctional enzyme involved in DNA base excision repair, DNA demethylation and transcription regulation. TDG is the predominant enzyme that removes thymine from T/G mispair, which arises due to deamination of 5-methyl-cytosine at the CpG dinucleotide, thereby preventing C to T mutations. SIRT1 is a member of class III NAD+-dependent histone/protein deacetylases. In the present study, we demonstrate that SIRT1 interacts with residues 67-110 of hTDG (human TDG). In addition, SIRT1 enhances TDG glycosylase activity and deacetylates acetylated TDG. TDG acetylation weakens its interaction with SIRT1. Although acetylated TDG has reduced glycosylase activity towards T/G, 5-formylcytosine/G and 5-carboxylcytosine/G, it has a stronger activity towards a 5-fluorouracil/G substrate as compared with unmodified TDG. SIRT1 weakly stimulates acetylated hTDG activity towards T/G, 5-formylcytosine/G and 5-carboxylcytosine/G as compared with control hTDG. Sirt1-knockout mouse embryonic fibroblast cells have higher levels of TDG expression and acetylation. The physical and functional interactions between SIRT1 and TDG may mediate DNA repair, gene expression and FU (5-fluorouracil)-mediated cytotoxicity.

Indexed as

AcetylationAnimalsAntineoplastic AgentsDNA RepairFibroblastsFluorouracilHEK293 CellsHumansMiceMice, KnockoutSirtuin 1Substrate SpecificityThymine DNA GlycosylaseAntineoplastic AgentsFluorouracilSIRT1 protein, humanSirt1 protein, mouseSirtuin 1Thymine DNA Glycosylase

Identifiers

PMID23952905
PMCPMC4465237
OpenAlexW2328229027

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.