Evidence map›Paper›PMID 28134932›Full record

ArticleNature structural & molecular biology2017

Eukaryotic Rad50 functions as a rod-shaped dimer.

Young Bong Park, Marcel Hohl, Michał Padjasek, Eunyoung Jeong, Kyeong Sik Jin, Artur Krężel, John H J Petrini, Yunje Cho

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Review
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  6. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  7. Article
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  9. Article
  10. Article
  11. Review
  12. Dynamic Properties of the DNA Damage Response Mre11/Rad50 Complex.International journal of molecular sciences · 2023
    Review
  13. Importance of Germline and Somatic Alterations in HumanInternational journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. An Extremely Stable Interprotein Tetrahedral Hg(Cys)Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

8 authors at 3 institutions in 3 countries.

Young Bong ParkDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Marcel HohlMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Michał PadjasekLaboratory of Chemical Biology, University of Wrocław, Wrocław, Poland.
Eunyoung JeongDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Kyeong Sik JinPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, South Korea.
Artur KrężelLaboratory of Chemical Biology, University of Wrocław, Wrocław, Poland.
John H J PetriniMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Yunje ChoDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Pohang University of Science and Technology · KRMemorial Sloan Kettering Cancer Center · USUniversity of Wrocław · PL

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
ROLES OF MRELL AND RAD50 IN THE DNA DAMAGE RESPONSER01GM056888 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI PETRINI, JOHN HJ · 1998 to 2019
$8.6M
The Proneural Perivascular Niche and Therapeutic ResponseU54CA163167 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI HOLLAND, ERIC C. · 2011 to 2015
$4.6M
FASEB SRC on Genetic Recombination and Genome RearrangementsR13CA162528 · NCI · FEDERATION OF AMER SOC FOR EXPER BIOLOGY · PI PETRINI, JOHN HJ · 2011 to 2011
$5k
NCI NIH HHS P30 CA008748NCI NIH HHS R13 CA162528NCI NIH HHS U54 CA163167NIGMS NIH HHS R01 GM056888
6 · The paper itself

Abstract

The Rad50 hook interface is crucial for assembly and various functions of the Mre11 complex. Previous analyses suggested that Rad50 molecules interact within (intracomplex) or between (intercomplex) dimeric complexes. In this study, we determined the structure of the human Rad50 hook and coiled-coil domains. The data suggest that the predominant structure is the intracomplex, in which the two parallel coiled coils proximal to the hook form a rod shape, and that a novel interface within the coiled-coil domains of Rad50 stabilizes the interaction of Rad50 protomers in the dimeric assembly. In yeast, removal of the coiled-coil interface compromised Tel1 activation without affecting DNA repair, while simultaneous disruption of that interface and the hook phenocopied a null mutation. The results demonstrate that the hook and coiled-coil interfaces coordinately promote intracomplex assembly and define the intracomplex as the functional form of the Mre11 complex.

Indexed as

Protein MultimerizationAcid Anhydride HydrolasesAmino Acid SequenceCell Cycle CheckpointsCrystallography, X-RayDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA RepairDNA Repair EnzymesEukaryotic CellsFluorescence Resonance Energy TransferHumansMeiosisModels, BiologicalMutant ProteinsProtein DomainsAcid Anhydride HydrolasesDNA-Binding ProteinsDNA Repair EnzymesMutant ProteinsRAD50 protein, humanSolutionsZinc

Identifiers

PMID28134932
PMCPMC5625350
OpenAlexW2583003623

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.