Evidence map›Paper›PMID 30177755›Full record

ArticleNature structural & molecular biology2018

A single XLF dimer bridges DNA ends during nonhomologous end joining.

Thomas G W Graham, Sean M Carney, Johannes C Walter, Joseph J Loparo

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Core NHEJ Factors Maintain Synapsis Across Diverse DNA End Structures.bioRxiv : the preprint server for biology · 2026
    Article
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  5. Article
  6. Article
  7. Article
  8. Review
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  12. Phosphorylation of DNA-PKcs at the S2056 cluster ensures efficient and productive lymphocyte development in XLF-deficient mice.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. The mechanisms of human lymphoid chromosomal translocations and their medical relevance.Critical reviews in biochemistry and molecular biology · 2022
    Article
  16. Article
  17. Review
  18. Article
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  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

4 authors.

Thomas G W GrahamDepartment of Systems Biology, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0001-5189-4313
Sean M CarneyDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Johannes C WalterDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Joseph J LoparoDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA. joseph_loparo@hms.harvard.edu.ORCID http://orcid.org/0000-0003-4941-4696

Funding

The mechanism of vertebrate DNA replication terminationR01GM080676 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALTER, JOHANNES · 2007 to 2019
$3.7M
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
NIGMS NIH HHS R01 GM080676NIGMS NIH HHS R01 GM115487
6 · The paper itself

Abstract

Nonhomologous end joining (NHEJ) is the primary pathway of DNA double-strand-break repair in vertebrate cells, yet how NHEJ factors assemble a synaptic complex that bridges DNA ends remains unclear. To address the role of XRCC4-like factor (XLF) in synaptic-complex assembly, we used single-molecule fluorescence imaging in Xenopus laevis egg extract, a system that efficiently joins DNA ends. We found that a single XLF dimer binds DNA substrates just before the formation of a ligation-competent synaptic complex between DNA ends. The interaction of both globular head domains of the XLF dimer with XRCC4 is required for efficient formation of this synaptic complex. Our results indicate that, in contrast to a model in which filaments of XLF and XRCC4 bridge DNA ends, binding of a single XLF dimer facilitates the assembly of a stoichiometrically well-defined synaptic complex.

Indexed as

DNA End-Joining RepairAnimalsDimerizationDNA-Binding ProteinsHumansOptical ImagingXenopus laevisDNA-Binding Proteins

Identifiers

PMID30177755
PMCPMC6128732

What OpenQuestion holds

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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.