Evidence map›Paper›PMID 32093126›Full record

ArticleMolecules (Basel, Switzerland)2020

Large-Scale Virtual Screening Against the MET Kinase Domain Identifies a New Putative Inhibitor Type.

Emmanuel Bresso, Alessandro Furlan, Philippe Noel, Vincent Leroux, Flavio Maina, Rosanna Dono, Bernard Maigret

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Ensemble Docking as a Tool for the Rational Design of PeptidomimeticInternational journal of molecular sciences · 2024
    Article
  2. Cimicifugin, a broad-spectrum inhibitor ofAntimicrobial agents and chemotherapy · 2024
    Article
  3. 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

7 authors at 1 institution in 1 country.

Emmanuel BressoUniversité de Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France.ORCID 0000-0002-5650-3155
Alessandro FurlanAix Marseille Univ, CNRS, Developmental Biology Institute of Marseille (IBDM), UMR7288, Parc Scientifique de Luminy, 13009 Marseille, France.
Philippe NoelUniversité de Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France.
Vincent LerouxUniversité de Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France.
Flavio MainaAix Marseille Univ, CNRS, Developmental Biology Institute of Marseille (IBDM), UMR7288, Parc Scientifique de Luminy, 13009 Marseille, France.ORCID 0000-0001-6100-4695
Rosanna DonoAix Marseille Univ, CNRS, Developmental Biology Institute of Marseille (IBDM), UMR7288, Parc Scientifique de Luminy, 13009 Marseille, France.
Bernard MaigretUniversité de Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France.ORCID 0000-0002-1983-1950
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By using an ensemble-docking strategy, we undertook a large-scale virtual screening campaign in order to identify new putative hits against the MET kinase target. Following a large molecular dynamics sampling of its conformational space, a set of 45 conformers of the kinase was retained as docking targets to take into account the flexibility of the binding site moieties. Our screening funnel started from about 80,000 chemical compounds to be tested in silico for their potential affinities towards the kinase binding site. The top 100 molecules selected-thanks to the molecular docking results-were further analyzed for their interactions, and 25 of the most promising ligands were tested for their ability to inhibit MET activity in cells. F0514-4011 compound was the most efficient and impaired this scattering response to HGF (Hepatocyte Growth Factor) with an IC 50 of 7.2 μ M. Interestingly, careful docking analysis of this molecule with MET suggests a possible conformation halfway between classical type-I and type-II MET inhibitors, with an additional region of interaction. This compound could therefore be an innovative seed to be repositioned from its initial antiviral purpose towards the field of MET inhibitors. Altogether, these results validate our ensemble docking strategy as a cost-effective functional method for drug development.

Indexed as

Molecular Docking SimulationMolecular Dynamics SimulationHumansProtein Kinase InhibitorsProto-Oncogene Proteins c-metMET protein, humanProtein Kinase InhibitorsProto-Oncogene Proteins c-metconformational selectioncross-docking validationensemble-dockinginduced fitMET kinasestructure-based drug designvirtual screening

Identifiers

PMID32093126
PMCPMC7070486
OpenAlexW3007932287

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.