Evidence map›Paper›PMID 29330428›Full record

ArticleNature communications2018

Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168.

Tomio S Takahashi, Yoshihiro Hirade, Aya Toma, Yusuke Sato, Atsushi Yamagata, Sakurako Goto-Ito, Akiko Tomita, Shinichiro Nakada, Shuya Fukai

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

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  13. The role of ubiquitination in tumorigenesis and targeted drug discovery.Signal transduction and targeted therapy · 2020
    Review
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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

9 authors at 3 institutions in 1 country.

Tomio S TakahashiInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Yoshihiro HiradeDepartment of Bioregulation and Cellular Response, Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan.ORCID http://orcid.org/0000-0003-3270-7679
Aya TomaInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Yusuke SatoInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Atsushi YamagataInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Sakurako Goto-ItoInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Akiko TomitaDepartment of Bioregulation and Cellular Response, Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan.
Shinichiro NakadaDepartment of Bioregulation and Cellular Response, Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan. snakada@bcr.med.osaka-u.ac.jp.
Shuya FukaiInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan. fukai@iam.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-1241-1443
Japan Synchrotron Radiation Research Institute · JPThe University of Osaka · JPOsaka University of Pharmaceutical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The E3 ubiquitin (Ub) ligase RNF168 plays a critical role in the initiation of the DNA damage response to double-strand breaks (DSBs). The recruitment of RNF168 by ubiquitylated targets involves two distinct regions, Ub-dependent DSB recruitment module (UDM) 1 and UDM2. Here we report the crystal structures of the complex between UDM1 and Lys63-linked diUb (K63-Ub

Indexed as

Amino Acid MotifsCell Line, TumorDNA DamageHumansLysineModels, MolecularPolyubiquitinProtein BindingProtein FoldingUbiquitinationUbiquitin-Protein LigasesLysinePolyubiquitinRNF168 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID29330428
PMCPMC5766498
OpenAlexW2782639350

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.