Evidence map›Paper›PMID 26408825›Full record

ArticleDNA repair2015

The interaction between ALKBH2 DNA repair enzyme and PCNA is direct, mediated by the hydrophobic pocket of PCNA and perturbed in naturally-occurring ALKBH2 variants.

Dragony Fu, Leona D Samson, Ullrich Hübscher, Barbara van Loon

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Predictive Analysis and Validation of Critical Missense SNPs of theInternational journal of molecular sciences · 2025
    Review
  2. Article
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  5. Article
  6. Article
  7. DNA Alkylation Damage by Nitrosamines and Relevant DNA Repair Pathways.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
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  14. The PCNA interaction motifs revisited: thinking outside the PIP-box.Cellular and molecular life sciences : CMLS · 2019
    Article
  15. Review
  16. Article
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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

4 authors at 2 institutions in 2 countries.

Dragony FuInstitute of Veterinary Biochemistry and Molecular Biology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland. Electronic address: dragonyfu@rochester.edu.
Leona D SamsonDepartment of Biological Engineering and Biology, Center for Environmental Health Sciences, David H. Koch Center for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Ullrich HübscherInstitute of Veterinary Biochemistry and Molecular Biology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Barbara van LoonInstitute of Veterinary Biochemistry and Molecular Biology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland. Electronic address: bvanloon@vetbio.uzh.ch.
Massachusetts Institute of Technology · USUniversity of Zurich · CH

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LEVINE, STUART S · 1985 to 2020
$25.6M
EUKARYTIC DNA ALKYLATION REPAIRR01CA055042 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAMSON, LEONA D. · 1991 to 2010
$4.8M
Eukaryotic DNA Alkylation RepairR01ES022872 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAMSON, LEONA D. · 2013 to 2017
$1.7M
NCI NIH HHS CA055042NCI NIH HHS R01 CA055042NIEHS NIH HHS ES002109NIEHS NIH HHS P30 ES002109NIEHS NIH HHS R01 ES022872
6 · The paper itself

Abstract

Human AlkB homolog 2 (ALKBH2) is a DNA repair enzyme that catalyzes the direct reversal of DNA methylation damage through oxidative demethylation. While ALKBH2 colocalizes with proliferating cell nuclear antigen (PCNA) in DNA replication foci, it remains unknown whether these two proteins alone form a complex or require additional components for interaction. Here, we demonstrate that ALKBH2 can directly interact with PCNA independent from other cellular factors, and we identify the hydrophobic pocket of PCNA as the key domain mediating this interaction. Moreover, we find that PCNA association with ALKBH2 increases significantly during DNA replication, suggesting that ALKBH2 forms a cell-cycle dependent complex with PCNA. Intriguingly, we show that an ALKBH2 germline variant, as well as a variant found in cancer, display altered interaction with PCNA. Our studies reveal the ALKBH2 binding interface of PCNA and indicate that both germline and somatic ALKBH2 variants could have cellular effects on ALKBH2 function in DNA repair.

Indexed as

DNA RepairAlkB Homolog 2, Alpha-Ketoglutarate-Dependent DioxygenaseAmino Acid SubstitutionDioxygenasesDNA Repair EnzymesDNA ReplicationGerm-Line MutationHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsNeoplasmsProliferating Cell Nuclear AntigenProtein IsoformsProtein Structure, TertiaryS PhaseALKBH2 protein, humanAlkB Homolog 2, Alpha-Ketoglutarate-Dependent DioxygenaseDioxygenasesDNA Repair EnzymesProliferating Cell Nuclear AntigenProtein IsoformsAlkBALKBH2APIMDNA repairPCNA

Identifiers

PMID26408825
PMCPMC5206904
OpenAlexW1883201575

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.