Evidence map›Paper›PMID 28776949›Full record

ArticleChemMedChem2017

Structure-Guided Design of Peptides as Tools to Probe the Protein-Protein Interaction between Cullin-2 and Elongin BC Substrate Adaptor in Cullin RING E3 Ubiquitin Ligases.

Teresa A F Cardote, Alessio Ciulli

Open access · hybridAbstract read
In one paragraph

Article in ChemMedChem, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Spy vs. spy: selecting the best reporter forChemical communications (Cambridge, England) · 2019
    Article
  6. Article
  7. 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

2 authors at 1 institution in 1 country.

Teresa A F CardoteBiological Chemistry and Drug Discovery Division, School of Life Sciences, University of Dundee, Dow Street, DD1 5EH, Dundee, UK.
Alessio CiulliBiological Chemistry and Drug Discovery Division, School of Life Sciences, University of Dundee, Dow Street, DD1 5EH, Dundee, UK.ORCID 0000-0002-8654-1670
University of Dundee · GB

Funding

European Research Council 311460Wellcome Trust
6 · The paper itself

Abstract

Cullin RING E3 ubiquitin ligases (CRLs) are large dynamic multi-subunit complexes that control the fate of many proteins in cells. CRLs are attractive drug targets for the development of small-molecule inhibitors and chemical inducers of protein degradation. Herein we describe a structure-guided biophysical approach to probe the protein-protein interaction (PPI) between the Cullin-2 scaffold protein and the adaptor subunits Elongin BC within the context of the von Hippel-Lindau complex (CRL2

Indexed as

Amino Acid SequenceBinding SitesCalorimetryCullin ProteinsDrug DesignElonginHumansInterferometryKineticsMagnetic Resonance SpectroscopyPeptidesProtein Interaction Domains and MotifsRecombinant ProteinsTranscription FactorsUbiquitin-Protein LigasesCUL2 protein, humanCullin ProteinsELOC protein, humanElonginPeptidesRecombinant ProteinsTranscription FactorsUbiquitin-Protein Ligaseschemical probesCullin RING E3 ligasespeptidesprotein-protein interactionsstructure-guided design

Identifiers

PMID28776949
PMCPMC5639367
OpenAlexW2742937176

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.