Evidence map›Paper›PMID 34201418›Full record

ArticleBiomolecules2021

Discovery of Novel Allosteric Modulators Targeting an Extra-Helical Binding Site of GLP-1R Using Structure- and Ligand-Based Virtual Screening.

Qingtong Zhou, Wanjing Guo, Antao Dai, Xiaoqing Cai, Márton Vass, Chris de Graaf, Wenqing Shui, Suwen Zhao, Dehua Yang, Ming-Wei Wang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2021. 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 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Novel anti-Frontiers in cellular and infection microbiology · 2024
    Article
  3. Review
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

10 authors at 5 institutions in 2 countries.

Qingtong ZhouSchool of Basic Medical Sciences, Fudan University, Shanghai 200032, China.ORCID 0000-0001-8124-3079
Wanjing GuoThe National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Antao DaiThe National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Xiaoqing CaiThe National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Márton VassAmsterdam Institute for Molecules, Medicines and Systems, Division of Medicinal Chemistry, Faculty of Sciences, Vrije Universiteit Amsterdam, 1081 Amsterdam, The Netherlands.
Chris de GraafAmsterdam Institute for Molecules, Medicines and Systems, Division of Medicinal Chemistry, Faculty of Sciences, Vrije Universiteit Amsterdam, 1081 Amsterdam, The Netherlands.ORCID 0000-0002-1226-2150
Wenqing ShuiiHuman Institute, ShanghaiTech University, Shanghai 201210, China.
Suwen ZhaoiHuman Institute, ShanghaiTech University, Shanghai 201210, China.
Dehua YangThe National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Ming-Wei WangSchool of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Chinese Academy of Sciences · CNShanghai Medical College of Fudan University · CNShanghaiTech University · CNVrije Universiteit Amsterdam · NLShanghai Institute of Materia Medica · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allosteric modulators have emerged with many potential pharmacological advantages as they do not compete the binding of agonist or antagonist to the orthosteric sites but ultimately affect downstream signaling. To identify allosteric modulators targeting an extra-helical binding site of the glucagon-like peptide-1 receptor (GLP-1R) within the membrane environment, the following two computational approaches were applied: structure-based virtual screening with consideration of lipid contacts and ligand-based virtual screening with the maintenance of specific allosteric pocket residue interactions. Verified by radiolabeled ligand binding and cAMP accumulation experiments, two negative allosteric modulators and seven positive allosteric modulators were discovered using structure-based and ligand-based virtual screening methods, respectively. The computational approach presented here could possibly be used to discover allosteric modulators of other G protein-coupled receptors.

Indexed as

Allosteric SiteAnimalsBinding SitesCHO CellsCricetinaeCricetulusDrug Delivery SystemsDrug DiscoveryGlucagonGlucagon-Like Peptide-1 ReceptorHumansLigandsMolecular Docking SimulationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryGLP1R protein, humanGlucagonGlucagon-Like Peptide-1 ReceptorLigandsallosteric modulatordrug discoveryGLP-1Rmolecular dockingvirtual screening

Identifiers

PMID34201418
PMCPMC8301998
OpenAlexW3173312470

What OpenQuestion holds

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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.