Evidence map›Paper›PMID 28466855›Full record

ArticleNature communications2017

A domain in human EXOG converts apoptotic endonuclease to DNA-repair exonuclease.

Michal R Szymanski, Wangsheng Yu, Aleksandra M Gmyrek, Mark A White, Ian J Molineux, J Ching Lee, Y Whitney Yin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Mitochondria-Nuclear Crosstalk: Orchestrating mtDNA Maintenance.Environmental and molecular mutagenesis · 2025
    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 2 institutions in 1 country.

Michal R SzymanskiDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Wangsheng YuDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Aleksandra M GmyrekDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Mark A WhiteSealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA.ORCID 0000-0003-1057-4203
Ian J MolineuxDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712, USA.
J Ching LeeSealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Y Whitney YinDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
The University of Texas Medical Branch at Galveston · USThe University of Texas at Austin · US

Funding

Dissecting Dual Function of Pol gamma in mtDNA Replication and Oxidative Damage RepairR01GM110591 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI YIN, YUHUI · 2014 to 2018
$1.3M
Studies of toxicities of HIV RT inhibitors to human mitochondrial DNA polymeraseR01GM083703 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI YIN, YUHUI · 2008 to 2012
$1.3M
NIGMS NIH HHS R01 GM083703NIGMS NIH HHS R01 GM110591
6 · The paper itself

Abstract

Human EXOG (hEXOG) is a 5'-exonuclease that is crucial for mitochondrial DNA repair; the enzyme belongs to a nonspecific nuclease family that includes the apoptotic endonuclease EndoG. Here we report biochemical and structural studies of hEXOG, including structures in its apo form and in a complex with DNA at 1.81 and 1.85 Å resolution, respectively. A Wing domain, absent in other ββα-Me members, suppresses endonuclease activity, but confers on hEXOG a strong 5'-dsDNA exonuclease activity that precisely excises a dinucleotide using an intrinsic 'tape-measure'. The symmetrical apo hEXOG homodimer becomes asymmetrical upon binding to DNA, providing a structural basis for how substrate DNA bound to one active site allosterically regulates the activity of the other. These properties of hEXOG suggest a pathway for mitochondrial BER that provides an optimal substrate for subsequent gap-filling synthesis by DNA polymerase γ.

Indexed as

DNA RepairProtein DomainsAmino Acid SequenceCatalytic DomainCrystallography, X-RayDNAEndodeoxyribonucleasesEndonucleasesHumansKineticsMitochondriaModels, MolecularNucleic Acid ConformationSequence Homology, Amino AcidSubstrate SpecificityDNAEndodeoxyribonucleasesendonuclease GEndonucleasesEXOG protein, human

Identifiers

PMID28466855
PMCPMC5418593
OpenAlexW2611006674

What OpenQuestion holds

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Registered trials

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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.