Evidence map›Paper›PMID 25349191›Full record

ArticleThe EMBO journal2014

Structure of the Rad50 DNA double-strand break repair protein in complex with DNA.

Anna Rojowska, Katja Lammens, Florian U Seifert, Carolin Direnberger, Heidi Feldmann, Karl-Peter Hopfner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

41 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Importance of Germline and Somatic Alterations in HumanInternational journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. The dynamic nature of the Mre11-Rad50 DNA break repair complex.Progress in biophysics and molecular biology · 2021
    Review
  15. Article
  16. Article
  17. MRN complex is an essential effector of DNA damage repair.Journal of Zhejiang University. Science. B · 2021
    Review
  18. Article
  19. Review
  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

6 authors at 1 institution in 1 country.

Anna RojowskaDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany.
Katja LammensDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany.
Florian U SeifertDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany.
Carolin DirenbergerDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany.
Heidi FeldmannDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany.
Karl-Peter HopfnerDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Munich, Germany Center for Integrated Protein Sciences, Munich, Germany hopfner@genzentrum.lmu.de.
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Mre11-Rad50 nuclease-ATPase is an evolutionarily conserved multifunctional DNA double-strand break (DSB) repair factor. Mre11-Rad50's mechanism in the processing, tethering, and signaling of DSBs is unclear, in part because we lack a structural framework for its interaction with DNA in different functional states. We determined the crystal structure of Thermotoga maritima Rad50(NBD) (nucleotide-binding domain) in complex with Mre11(HLH) (helix-loop-helix domain), AMPPNP, and double-stranded DNA. DNA binds between both coiled-coil domains of the Rad50 dimer with main interactions to a strand-loop-helix motif on the NBD. Our analysis suggests that this motif on Rad50 does not directly recognize DNA ends and binds internal sites on DNA. Functional studies reveal that DNA binding to Rad50 is not critical for DNA double-strand break repair but is important for telomere maintenance. In summary, we provide a structural framework for DNA binding to Rad50 in the ATP-bound state.

Indexed as

Models, MolecularAmino Acid SequenceBacterial ProteinsBase SequenceBinding SitesCrystallographyDNADNA-Binding ProteinsDNA Repair EnzymesMolecular Sequence DataMultiprotein ComplexesProtein ConformationProtein Structure, TertiarySaccharomyces cerevisiaeSequence AlignmentSequence Analysis, DNABacterial ProteinsDNADNA-Binding ProteinsDNA Repair EnzymesMultiprotein Complexescrystal structureDNA double‐strand break repairhomologous recombinationMre11–Rad50protein:DNA complex

Identifiers

PMID25349191
PMCPMC4282560
OpenAlexW2059287705

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.