Evidence map›Paper›PMID 23195996›Full record

ReviewMutation research

MBD4 and TDG: multifaceted DNA glycosylases with ever expanding biological roles.

Ashley B Sjolund, Alireza G Senejani, Joann B Sweasy

Abstract readReview
In one paragraph

Review in Mutation research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

66 citing papers in PubMed, 109 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Base Excision DNA Repair in Plants:International journal of molecular sciences · 2023
    Review
  14. Article
  15. Levels of base excision repair proteins in CD4Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2022
    Article
  16. Article
  17. DNA Methyltransferases and DNA Damage.Advances in experimental medicine and biology · 2022
    Article
  18. Article
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Ashley B SjolundDepartment of Human Genetics, Yale University School of Medicine, New Haven, CT 06520, USA.
Alireza G SenejaniDepartment of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06520, USA.
Joann B SweasyDepartment of Human Genetics, Yale University School of Medicine, New Haven, CT 06520, USA; Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06520, USA. Electronic address: joann.sweasy@yale.edu.
Yale University · US

Funding

TUMOR SELECTIVE INACTIVATION OF THE REPAIR PROTEIN AGTP01CA129186 · NCI · YALE UNIVERSITY · PI SARTORELLI, ALAN CLAYTON · 2007 to 2012
$8.5M
NCI NIH HHS P01 CA129186
6 · The paper itself

Abstract

The base excision repair system is vital to the repair of endogenous and exogenous DNA damage. This pathway is initiated by one of several DNA glycosylases that recognizes and excises specific DNA lesions in a coordinated fashion. Methyl-CpG Domain Protein 4 (MBD4) and Thymine DNA Glycosylase (TDG) are the two major G:T glycosylases that remove thymine generated by the deamination of 5-methylcytosine. Both of these glycosylases also remove a variety of other base lesions, including G:U and preferentially act at CpG sites throughout the genome. Many have questioned the purpose of seemingly redundant glycosylases, but new information has emerged to suggest MBD4 and TDG have diverse biological functions. MBD4 has been closely linked to apoptosis, while TDG has been clearly implicated in transcriptional regulation. This article reviews all of these developments, and discusses the consequences of germline and somatic mutations that lead to non-synonymous amino acid substitutions on MBD4 and TDG protein function. In addition, we report the finding of alternatively spliced variants of MBD4 and TDG and the results of functional studies of a tumor-associated variant of MBD4.

Indexed as

DNA DamageDNA RepairAnimalsEndodeoxyribonucleasesHumansMutationThymineThymine DNA GlycosylaseEndodeoxyribonucleasesThymineThymine DNA Glycosylase

Identifiers

PMID23195996
PMCPMC3661743
OpenAlexW2027875128

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.