Evidence map›Paper›PMID 17124166›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4.

Pierre-Olivier Mari, Bogdan I Florea, Stephan P Persengiev, Nicole S Verkaik, Hennie T Brüggenwirth, Mauro Modesti, Giuseppina Giglia-Mari, Karel Bezstarosti, Jeroen A A Demmers, Theo M Luider and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 206 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
206citing papers in PubMed, 1 pooled it
9.4field-weighted citation impact, top 1% 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

206 citing papers in PubMed, 1 synthesis or guideline pooled it, 397 citations in OpenAlex.

  1. Pooled it
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  17. Chemical Insights into Oxidative and Nitrative Modifications of DNA.International journal of molecular sciences · 2023
    Review
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146 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

12 authors at 3 institutions in 2 countries.

Pierre-Olivier MariDepartment of Biochemistry, Center for Biomics, Erasmus MC, University Medical Center, 3000 CA Rotterdam, The Netherlands.
Bogdan I Florea
Stephan P Persengiev
Nicole S Verkaik
Hennie T Brüggenwirth
Mauro Modesti
Giuseppina Giglia-Mari
Karel Bezstarosti
Jeroen A A Demmers
Theo M Luider
Adriaan B Houtsmuller
Dik C van Gent
Erasmus MC · NLPediatrics and Genetics · USNeurology, Inc · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA double-strand break (DSB) repair by nonhomologous end joining (NHEJ) requires the assembly of several proteins on DNA ends. Although biochemical studies have elucidated several aspects of the NHEJ reaction mechanism, much less is known about NHEJ in living cells, mainly because of the inability to visualize NHEJ repair proteins at DNA damage. Here we provide evidence that a pulsed near IR laser can produce DSBs without any visible alterations in the nucleus, and we show that NHEJ proteins accumulate in the irradiated areas. The levels of DSBs and Ku accumulation diminished in time, showing that this approach allows us to study DNA repair kinetics in vivo. Remarkably, the Ku heterodimers on DNA ends were in dynamic equilibrium with Ku70/80 in solution, showing that NHEJ complex assembly is reversible. Accumulation of XRCC4/ligase IV on DSBs depended on the presence of Ku70/80, but not DNA-PK(CS). We detected a direct interaction between Ku70 and XRCC4 that could explain these requirements. Our results suggest that this assembly constitutes the core of the NHEJ reaction and that XRCC4 may serve as a flexible tether between Ku70/80 and ligase IV.

Indexed as

Antigens, NuclearDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA Ligase ATPDNA LigasesDNA RepairGreen Fluorescent ProteinsHeLa CellsHumansKu AutoantigenAntigens, NuclearDNA-Binding ProteinsDNA Ligase ATPDNA Ligasesenhanced green fluorescent proteinGreen Fluorescent ProteinsKu AutoantigenXRCC4 protein, humanXrcc6 protein, human

Identifiers

PMID17124166
PMCPMC1693708
OpenAlexW2137239016

What OpenQuestion holds

Textmetadata
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.