Evidence map›Paper›PMID 24013086›Full record

ReviewGene2013

Structure and function of the DNA ligases encoded by the mammalian LIG3 gene.

Alan E Tomkinson, Annahita Sallmyr

Open access · greenAbstract readReview
In one paragraph

Review in Gene, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.6field-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

42 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Novel Biallelic LIG3 Mutations Causing Lethal Phenotype With Immunodeficiency.American journal of medical genetics. Part A · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025
    Review
  11. Article
  12. DNA Damage Induced by T-2 Mycotoxin in Human Skin Fibroblast Cell Line-Hs68.International journal of molecular sciences · 2023
    Article
  13. Article
  14. Review
  15. Characterization of the interactome profiling ofFrontiers in microbiology · 2022
    Article
  16. Article
  17. DNA glycosylase NEIL2 functions in multiple cellular processes.Progress in biophysics and molecular biology · 2021
    Review
  18. Article
  19. Article
  20. 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

2 authors at 2 institutions in 1 country.

Alan E TomkinsonDepartment of Internal Medicine and University of New Mexico Cancer Center, University of New Mexico, Albuquerque, NM 87131, USA. Electronic address: atomkinson@salud.unm.edu.
Annahita Sallmyr
New Mexico Cancer Center · USUniversity of New Mexico · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Roles of LIG3 and XRCC1 genes in genome stability.R01ES012512 · NIEHS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Alan E Tomkinson · 2004 to 2026
$6.3M
NCI NIH HHS P01 CA092584NCI NIH HHS P01 CA92584NIEHS NIH HHS ES12512NIEHS NIH HHS R01 ES012512
6 · The paper itself

Abstract

Among the mammalian genes encoding DNA ligases (LIG), the LIG3 gene is unique in that it encodes multiple DNA ligase polypeptides with different cellular functions. Notably, this nuclear gene encodes the only mitochondrial DNA ligase and so is essential for this organelle. In the nucleus, there is significant functional redundancy between DNA ligase IIIα and DNA ligase I in excision repair. In addition, DNA ligase IIIα is essential for DNA replication in the absence of the replicative DNA ligase, DNA ligase I. DNA ligase IIIα is a component of an alternative non-homologous end joining (NHEJ) pathway for DNA double-strand break (DSB) repair that is more active when the major DNA ligase IV-dependent pathway is defective. Unlike its other nuclear functions, the role of DNA ligase IIIα in alternative NHEJ is independent of its nuclear partner protein, X-ray repair cross-complementing protein 1 (XRCC1). DNA ligase IIIα is frequently overexpressed in cancer cells, acting as a biomarker for increased dependence upon alternative NHEJ for DSB repair and it is a promising novel therapeutic target.

Indexed as

AnimalsDNA Ligase ATPDNA LigasesDNA RepairGene Expression Regulation, EnzymologicHumansModels, BiologicalModels, MolecularNeuronsPoly-ADP-Ribose Binding ProteinsProtein ConformationXenopus ProteinsDNA Ligase ATPDNA ligase III alpha protein, XenopusDNA LigasesLIG3 protein, humanPoly-ADP-Ribose Binding ProteinsXenopus ProteinsBRCTbreast cancer susceptibility protein 1-related C-terminalCancerDBDDNA binding domainDNA-dependent protein kinaseDNA double-strand breakDNA ligase encoding geneDNA ligasesDNA PKDNA single-strand breakDSBLIGLIG3Mitochondriamitochondrial leader sequenceMLSNei endonoclease VIII-like proteinNEILNeurodegenerationNHEJNLSnon-homologous end joiningNTaseNuclear DNA repairnuclear localization signalnucleotidyl transferase domainOBDoligonucleotide/oligosaccharide-fold binding domainPARP1PNKPpoly(ADP-ribose) polymerase 1polynucleotide kinase phosphataseSSBTdp1tyrosyl phosphodiesterase 1X-ray cross-complementing protein 1XRCC1zinc fingerZnF

Identifiers

PMID24013086
PMCPMC3881560
OpenAlexW2009855165

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.