Evidence map›Paper›PMID 28345889›Full record

ArticleBiochemistry2017

AP-Endonuclease 1 Accelerates Turnover of Human 8-Oxoguanine DNA Glycosylase by Preventing Retrograde Binding to the Abasic-Site Product.

Alexandre Esadze, Gaddiel Rodriguez, Shannen L Cravens, James T Stivers

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-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

28 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. 8-Oxoguanine: A Lesion, an Epigenetic Mark, or a Molecular Signal?International journal of molecular sciences · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. The Role of Natural Polymorphic Variants of DNA Polymerase β in DNA Repair.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. DNA Oxidation and Excision Repair Pathways.International journal of molecular sciences · 2019
    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 1 institution in 1 country.

Alexandre EsadzeDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States.
Gaddiel RodriguezDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States.
Shannen L CravensDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States.
James T StiversDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States.ORCID 0000-0003-2572-7807
Johns Hopkins University · US

Funding

University of Pennsylvania Postdoctoral Opportunities in Research and TeachingK12GM081259 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Janis K. Burkhardt · 2007 to 2026
$20.1M
PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Uracil Damage Recognition by Uracil DNA GlyocosylaseR01GM056834 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI STIVERS, JAMES T. · 1998 to 2021
$8.3M
Comprehensive Mechanism for DNA Damage Search and Repair in Human CellsF31GM114994 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CRAVENS, SHANNEN · 2015 to 2015
$43k
NIGMS NIH HHS F31 GM114994NIGMS NIH HHS K12 GM081259NIGMS NIH HHS R01 GM056834NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

A major product of oxidative DNA damage is 8-oxoguanine. In humans, 8-oxoguanine DNA glycosylase (hOGG1) facilitates removal of these lesions, producing an abasic (AP) site in the DNA that is subsequently incised by AP-endonuclease 1 (APE1). APE1 stimulates turnover of several glycosylases by accelerating rate-limiting product release. However, there have been conflicting accounts of whether hOGG1 follows a similar mechanism. In pre-steady-state kinetic measurements, we found that addition of APE1 had no effect on the rapid burst phase of 8-oxoguanine excision by hOGG1 but accelerated steady-state turnover (k

Indexed as

Adenosine TriphosphateCross-Linking ReagentsDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageDNA GlycosylasesGene ExpressionGlutaralGuaninePhosphorus RadioisotopesProtein BindingProtein TransportRecombinant ProteinsStaining and Labeling8-hydroxyguanineAdenosine TriphosphateAPEX1 protein, humanCross-Linking ReagentsDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesGlutaralGuanineoxoguanine glycosylase 1, humanPhosphorus RadioisotopesRecombinant Proteins

Identifiers

PMID28345889
PMCPMC5526596
OpenAlexW2601458043

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.