Evidence map›Paper›PMID 41870364›Full record

ArticleJournal of medicinal chemistry2026

Discovery, Structure-Activity Relationship, and Functional Characterization of a Chromenopyrrole Series as Orthosteric Antagonists of GPR84.

Michael A Malone, Ruijing Yin, Yueming Li, Laura Jenkins, Abdul-Akim Guseinov, Sara Marsango, Mark Huggett, Margaret Huggett, Anna Boyle, Angus Morrison and 3 more

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2026. 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
–field-weighted citation impact
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.

  1. 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

13 authors.

Michael A MaloneSchool of Chemistry, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.ORCID 0009-0007-1476-0659
Ruijing YinCentre for Translational Pharmacology, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.
Yueming LiCentre for Translational Pharmacology, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.
Laura JenkinsCentre for Translational Pharmacology, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.
Abdul-Akim GuseinovCentre for Translational Pharmacology, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.ORCID 0000-0002-2796-4323
Sara MarsangoCentre for Translational Pharmacology, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.
Mark HuggettBioAscent Discovery Ltd, Bo'Ness Road, Newhouse, Lanarkshire ML1 5UH, U.K.
Margaret HuggettBioAscent Discovery Ltd, Bo'Ness Road, Newhouse, Lanarkshire ML1 5UH, U.K.
Anna BoyleBioAscent Discovery Ltd, Bo'Ness Road, Newhouse, Lanarkshire ML1 5UH, U.K.
Angus MorrisonBioAscent Discovery Ltd, Bo'Ness Road, Newhouse, Lanarkshire ML1 5UH, U.K.
Irina G TikhonovaSchool of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, U.K.ORCID 0000-0002-6228-9431
Graeme MilliganCentre for Translational Pharmacology, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.ORCID 0000-0002-6946-3519
Andrew G JamiesonSchool of Chemistry, The Advanced Research Centre, University of Glasgow, 11 Chapel Lane, Glasgow G11 6EW, U.K.ORCID 0000-0003-1726-7353

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GPR84 is a proinflammatory G-protein-coupled receptor implicated in autoimmune and fibrotic disorders. Although orthosteric antagonists have been reported, their physicochemical limitations have hindered development. Here, we describe the discovery and optimization of a chromenopyrrole scaffold as a new class of orthosteric GPR84 antagonists. Guided by molecular modeling and iterative SAR, we identified ligands that competitively inhibit agonist binding, confirmed by Schild analysis and radioligand displacement. Structural refinement defined key steric and hydrophobic features required for high-affinity binding, culminating in the isolation of a single active enantiomer,

Indexed as

Drug DiscoveryPyrrolesReceptors, G-Protein-CoupledAnimalsHumansModels, MolecularStructure-Activity RelationshipGPR84 protein, humanPyrrolesReceptors, G-Protein-Coupled

Identifiers

PMID41870364
PMCPMC13071874

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.