Evidence map›Paper›PMID 26717941›Full record

ArticleThe EMBO journal2016

ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex.

Yaqi Liu, Sihyun Sung, Youngran Kim, Fuyang Li, Gwanghyun Gwon, Aera Jo, Ae-Kyoung Kim, Taeyoon Kim, Ok-Kyu Song, Sang Eun Lee and 1 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

82 citing papers in PubMed, 124 citations in OpenAlex.

  1. DNA Repair Mechanisms.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
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  17. Molecular basis of Gabija anti-phage supramolecular assemblies.Nature structural & molecular biology · 2024
    Article
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  20. Review

22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Yaqi LiuDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Sihyun SungDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Youngran KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Fuyang LiDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA Department of Radiation Oncology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.
Gwanghyun GwonDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Aera JoDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Ae-Kyoung KimPanbionet Corporation, Pohang, South Korea.
Taeyoon KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea.
Ok-Kyu SongPanbionet Corporation, Pohang, South Korea.
Sang Eun LeeDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA Department of Radiation Oncology, University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.
Yunje ChoDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, South Korea yunje@postech.ac.kr.
Pohang University of Science and Technology · KRPohang TechnoPark (South Korea) · KRThe University of Texas Health Science Center at San Antonio · US

Funding

Mechanisms of Error Prone Repair of DNA BreaksR01GM071011 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LEE, SANG EUN · 2004 to 2021
$4.5M
NIGMS NIH HHS R01 GM071011
6 · The paper itself

Abstract

ATP-dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here,Methanococcus jannaschii MR-ATPγS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPγS-bound Rad50 nucleotide-binding domains. Duplex DNA cannot access the Mre11 active site in the ATP-free full-length MR complex. ATP hydrolysis drives rotation of the nucleotide-binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis-driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity.

Indexed as

Adenosine TriphosphateAmino Acid SequenceArchaeal ProteinsDNAMethanococcusMolecular Sequence DataSequence Homology, Amino AcidAdenosine TriphosphateArchaeal ProteinsDNAcentral grooveDNA bindingDNA meltingMre11/Rad50nuclease

Identifiers

PMID26717941
PMCPMC4818763
OpenAlexW2197921315

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.