Evidence map›Paper›PMID 28591624›Full record

ArticleStructure (London, England : 1993)2017

Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex.

Teresa A F Cardote, Morgan S Gadd, Alessio Ciulli

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
4.4field-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

95 citing papers in PubMed, 150 citations in OpenAlex.

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35 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

3 authors at 1 institution in 1 country.

Teresa A F CardoteDivision of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Morgan S GaddDivision of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Alessio CiulliDivision of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK. Electronic address: a.ciulli@dundee.ac.uk.
University of Dundee · GB

Funding

European Research Council 311460Wellcome TrustWellcome Trust 094090/Z/10/ZWellcome Trust 100476/Z/12/Z
6 · The paper itself

Abstract

Cullin RING E3 ubiquitin ligases (CRLs) function in the ubiquitin proteasome system to catalyze the transfer of ubiquitin from E2 conjugating enzymes to specific substrate proteins. CRLs are large dynamic complexes and attractive drug targets for the development of small-molecule inhibitors and chemical inducers of protein degradation. The atomic details of whole CRL assembly and interactions that dictate subunit specificity remain elusive. Here we present the crystal structure of a pentameric CRL2

Indexed as

Carrier ProteinsCrystallography, X-RayCullin ProteinsElonginHumansHydrophobic and Hydrophilic InteractionsModels, MolecularMultiprotein ComplexesMutationProtein ConformationThermodynamicsVon Hippel-Lindau Tumor Suppressor ProteinCarrier ProteinsCUL2 protein, humanCUL5 protein, humanCullin ProteinsELOB protein, humanELOC protein, humanElonginMultiprotein ComplexesRBX1 protein, humanVHL protein, humanVon Hippel-Lindau Tumor Suppressor ProteinCullin-2cullin-RING E3 ubiquitin ligasesprotein-protein interactionsRING domain proteinsVHL

Identifiers

PMID28591624
PMCPMC5462531
OpenAlexW2624244777

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.