Evidence map›Paper›PMID 21486746›Full record

ArticleNucleic acids research2011

5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA glycosylases.

Yann-Vaï Le Bihan, Maria Angeles Izquierdo, Franck Coste, Pierre Aller, Françoise Culard, Tim H Gehrke, Kadija Essalhi, Thomas Carell, Bertrand Castaing

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Trial
  2. Article
  3. Inhibitors of DNA Glycosylases as Prospective Drugs.International journal of molecular sciences · 2020
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013
    Review
  11. Article
  12. The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage.Progress in molecular biology and translational science · 2012
    Review
  13. 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

9 authors at 2 institutions in 2 countries.

Yann-Vaï Le BihanCentre de Biophysique Moléculaire, UPR4301, CNRS, rue Charles Sadron, 45071 Orléans cedex 02, France.
Maria Angeles Izquierdo
Franck Coste
Pierre Aller
Françoise Culard
Tim H Gehrke
Kadija Essalhi
Thomas Carell
Bertrand Castaing
University of Vermont · USCentre de Biophysique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA base-damage recognition in the base excision repair (BER) is a process operating on a wide variety of alkylated, oxidized and degraded bases. DNA glycosylases are the key enzymes which initiate the BER pathway by recognizing and excising the base damages guiding the damaged DNA through repair synthesis. We report here biochemical and structural evidence for the irreversible entrapment of DNA glycosylases by 5-hydroxy-5-methylhydantoin, an oxidized thymine lesion. The first crystal structure of a suicide complex between DNA glycosylase and unrepaired DNA has been solved. In this structure, the formamidopyrimidine-(Fapy) DNA glycosylase from Lactococcus lactis (LlFpg/LlMutM) is covalently bound to the hydantoin carbanucleoside-containing DNA. Coupling a structural approach by solving also the crystal structure of the non-covalent complex with site directed mutagenesis, this atypical suicide reaction mechanism was elucidated. It results from the nucleophilic attack of the catalytic N-terminal proline of LlFpg on the C5-carbon of the base moiety of the hydantoin lesion. The biological significance of this finding is discussed.

Indexed as

Catalytic DomainDNADNA DamageDNA-Formamidopyrimidine GlycosylaseHydantoinsModels, MolecularProtein Binding5-hydroxy-5-methylhydantoinDNADNA-Formamidopyrimidine GlycosylaseHydantoins

Identifiers

PMID21486746
PMCPMC3152353
OpenAlexW2004313947

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.