Evidence map›Paper›PMID 23898172›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Insight into mechanisms of 3'-5' exonuclease activity and removal of bulky 8,5'-cyclopurine adducts by apurinic/apyrimidinic endonucleases.

Abdelghani Mazouzi, Armelle Vigouroux, Bulat Aikeshev, Philip J Brooks, Murat K Saparbaev, Solange Morera, Alexander A Ishchenko

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

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  6. Recent Advances in Phenolic Metabolites and Skin Cancer.International journal of molecular sciences · 2021
    Review
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  9. (5'International journal of molecular sciences · 2021
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  17. Base excision repair of oxidative DNA damage: from mechanism to disease.Frontiers in bioscience (Landmark edition) · 2017
    Review
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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

7 authors at 4 institutions in 3 countries.

Abdelghani MazouziUniversité Paris-Sud, Laboratoire Stabilité Génétique et Oncogenèse, Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche 8200, Institut de Cancérologie Gustave-Roussy, F-94805 Villejuif Cedex, France.
Armelle Vigouroux
Bulat Aikeshev
Philip J Brooks
Murat K Saparbaev
Solange Morera
Alexander A Ishchenko
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FRLaboratoire d'Enzymologie et Biochimie Structurales · FRNational Center for Advancing Translational Sciences · US

Funding

Integrative genetics of behavior with high throughput technologiesZIAAA000301 · NIAAA · NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM · PI GOLDMAN, DAVID · 2009 to 2025
$68.6M
6 · The paper itself

Abstract

8,5'-cyclo-2'-deoxyadenosine (cdA) and 8,5'-cyclo-2'-deoxyguanosine generated in DNA by both endogenous oxidative stress and ionizing radiation are helix-distorting lesions and strong blocks for DNA replication and transcription. In duplex DNA, these lesions are repaired in the nucleotide excision repair (NER) pathway. However, lesions at DNA strand breaks are most likely poor substrates for NER. Here we report that the apurinic/apyrimidinic (AP) endonucleases--Escherichia coli Xth and human APE1--can remove 5'S cdA (S-cdA) at 3' termini of duplex DNA. In contrast, E. coli Nfo and yeast Apn1 are unable to carry out this reaction. None of these enzymes can remove S-cdA adduct located at 1 or more nt away from the 3' end. To understand the structural basis of 3' repair activity, we determined a high-resolution crystal structure of E. coli Nfo-H69A mutant bound to a duplex DNA containing an α-anomeric 2'-deoxyadenosine:T base pair. Surprisingly, the structure reveals a bound nucleotide incision repair (NIR) product with an abortive 3'-terminal dC close to the scissile position in the enzyme active site, providing insight into the mechanism for Nfo-catalyzed 3'→5' exonuclease function and its inhibition by 3'-terminal S-cdA residue. This structure was used as a template to model 3'-terminal residues in the APE1 active site and to explain biochemical data on APE1-catalyzed 3' repair activities. We propose that Xth and APE1 may act as a complementary repair pathway to NER to remove S-cdA adducts from 3' DNA termini in E. coli and human cells, respectively.

Indexed as

Models, MolecularProtein ConformationDenaturing Gradient Gel ElectrophoresisDeoxyadenosinesDeoxyguanosineDeoxyribonuclease IV (Phage T4-Induced)DNA AdductsDNA-(Apurinic or Apyrimidinic Site) LyaseDNA RepairEscherichia coliEscherichia coli ProteinsExonucleasesHumansMolecular StructureOligonucleotidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization8,5'-cyclo-2'-deoxyadenosine8,5'-cyclo-2'-deoxyguanosineAPEX1 protein, humanDeoxyadenosinesDeoxyguanosineDeoxyribonuclease IV (Phage T4-Induced)DNA AdductsDNA-(Apurinic or Apyrimidinic Site) Lyaseendonuclease IV, E coliEscherichia coli ProteinsExonucleasesOligonucleotidesbase excision repairdamage specific endonucleaseDNA glycosylaseendonuclease IVoxidative DNA damage

Identifiers

PMID23898172
PMCPMC3746914
OpenAlexW2037431380

What OpenQuestion holds

Textmetadata
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.