Evidence map›Paper›PMID 30232697›Full record

ArticleThe protein journal2018

Exploring the Structural Mechanism of Covalently Bound E3 Ubiquitin Ligase: Catalytic or Allosteric Inhibition?

Imane Bjij, Shama Khan, Robin Betz, Driss Cherqaoui, Mahmoud E S Soliman

Abstract read
PubMed Publisher
In one paragraph

Article in The protein journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. 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

5 authors at 3 institutions in 3 countries.

Imane BjijMolecular Bio-Computation & Drug Design Lab, School of Health Sciences, University of KwaZulu-Natal, Westville, Durban, 4000, South Africa.
Shama KhanMolecular Bio-Computation & Drug Design Lab, School of Health Sciences, University of KwaZulu-Natal, Westville, Durban, 4000, South Africa.
Robin BetzBiophysics Program, Stanford University, Stanford, CA, 94305, USA.
Driss CherqaouiDépartement de Chimie, Faculté des Sciences Semlalia, Université Cadi Ayyad, Av. My Abdellah, BP2390, Marrakech, Morocco.
Mahmoud E S SolimanMolecular Bio-Computation & Drug Design Lab, School of Health Sciences, University of KwaZulu-Natal, Westville, Durban, 4000, South Africa. soliman@ukzn.ac.za.
University of KwaZulu-Natal · ZACadi Ayyad University · MAStanford University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Covalent inhibition has recently gained a resurgence of interest in several drug discovery areas. The expansion of this approach is based on evidence elucidating the selectivity and potency of covalent inhibitors when bound to particular amino acids of a biological target. The Nedd4-1, an E3 ubiquitin ligase, is characterized by two covalent binding sites, of which catalytic Cys

Indexed as

Molecular Dynamics SimulationAllosteric RegulationCatalysisHumansNedd4 Ubiquitin Protein LigasesProtein DomainsStructure-Activity RelationshipNedd4 protein, humanNedd4 Ubiquitin Protein LigasesAllosteric-targeted enzymeCatalytic-targeted enzymeCovalent inhibitionMolecular dynamic simulations

Identifiers

PMID30232697
OpenAlexW2890317478

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.