Evidence map›Paper›PMID 31862156›Full record

ArticleMolecular cell2020

A Mechanism to Minimize Errors during Non-homologous End Joining.

Benjamin M Stinson, Andrew T Moreno, Johannes C Walter, Joseph J Loparo

Abstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
–field-weighted citation impact
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

66 citing papers in PubMed.

  1. Core NHEJ Factors Maintain Synapsis Across Diverse DNA End Structures.bioRxiv : the preprint server for biology · 2026
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  8. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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6 more citing papers are in PubMed but not listed here.

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.

Benjamin M StinsonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Andrew T MorenoDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Johannes C WalterDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Howard Hughes Medical Institute, Boston, MA 02115, USA. Electronic address: johannes_walter@hms.harvard.edu.
Joseph J LoparoDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: joseph_loparo@hms.harvard.edu.

Funding

Visualizing DNA break repair: single-molecule studies of non-homologous end joiningR01GM115487 · NIGMS · HARVARD MEDICAL SCHOOL · PI LOPARO, JOSEPH J. · 2015 to 2024
$3.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM115487
6 · The paper itself

Abstract

Enzymatic processing of DNA underlies all DNA repair, yet inappropriate DNA processing must be avoided. In vertebrates, double-strand breaks are repaired predominantly by non-homologous end joining (NHEJ), which directly ligates DNA ends. NHEJ has the potential to be highly mutagenic because it uses DNA polymerases, nucleases, and other enzymes that modify incompatible DNA ends to allow their ligation. Using frog egg extracts that recapitulate NHEJ, we show that end processing requires the formation of a "short-range synaptic complex" in which DNA ends are closely aligned in a ligation-competent state. Furthermore, single-molecule imaging directly demonstrates that processing occurs within the short-range complex. This confinement of end processing to a ligation-competent complex ensures that DNA ends undergo ligation as soon as they become compatible, thereby minimizing mutagenesis. Our results illustrate how the coordination of enzymatic catalysis with higher-order structural organization of substrate maximizes the fidelity of DNA repair.

Indexed as

DNA Breaks, Double-StrandedDNA End-Joining RepairGenomic InstabilityAnimalsDNA-Activated Protein KinaseDNA-Binding ProteinsDNA LigasesDNA Repair EnzymesFemaleKu AutoantigenModels, GeneticMultiprotein ComplexesPhosphoric Diester HydrolasesSingle Molecule ImagingTime FactorsXenopus laevisDNA-Activated Protein KinaseDNA-Binding ProteinsDNA LigasesDNA Repair EnzymesKu AutoantigenMultiprotein ComplexesPhosphoric Diester HydrolasesXenopus Proteinsend processingNHEJnon-homologous end joiningsingle-moleculesmFRET

Identifiers

PMID31862156
PMCPMC7060804

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.