Evidence map›Paper›PMID 24860101›Full record

ArticleThe Journal of biological chemistry2014

The molecular basis of ligand interaction at free fatty acid receptor 4 (FFA4/GPR120).

Brian D Hudson, Bharat Shimpukade, Graeme Milligan, Trond Ulven

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
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  9. Review
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  11. Pharmacology of Free Fatty Acid Receptors and Their Allosteric Modulators.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Review
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  19. Review
  20. A novel anti-inflammatory role of GPR120 in intestinal epithelial cells.American journal of physiology. Cell physiology · 2016
    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

4 authors.

Brian D HudsonFrom the Molecular Pharmacology Group, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom and.
Bharat Shimpukadethe Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
Graeme MilliganFrom the Molecular Pharmacology Group, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom and Graeme.Milligan@glasgow.ac.uk.
Trond Ulventhe Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark ulven@sdu.dk.

Funding

Biotechnology and Biological Sciences Research Council BB/K019864/1Canadian Institutes of Health Research
6 · The paper itself

Abstract

The long-chain fatty acid receptor FFA4 (previously GPR120) is receiving substantial interest as a novel target for the treatment of metabolic and inflammatory disease. This study examines for the first time the detailed mode of binding of both long-chain fatty acid and synthetic agonist ligands at FFA4 by integrating molecular modeling, receptor mutagenesis, and ligand structure-activity relationship approaches in an iterative format. In doing so, residues required for binding of fatty acid and synthetic agonists to FFA4 have been identified. This has allowed for the refinement of a well validated model of the mode of ligand-FFA4 interaction that will be invaluable in the identification of novel ligands and the future development of this receptor as a therapeutic target. The model reliably predicted the effects of substituent variations on agonist potency, and it was also able to predict the qualitative effect of binding site mutations in the majority of cases.

Indexed as

alpha-Linolenic AcidAmino Acid SubstitutionArrestinsbeta-ArrestinsBinding SitesFatty Acids, NonesterifiedHEK293 CellsHumansHydrogen BondingLigandsMethylaminesModels, MolecularMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPropionatesProtein Conformationalpha-Linolenic AcidArrestinsbeta-ArrestinsFatty Acids, NonesterifiedFFAR4 protein, humanGW9508LigandsMethylaminesPropionatesReceptors, G-Protein-CoupledRecombinant Proteins7-Helix ReceptorBioluminescence Resonance Energy Transfer (BRET)DiabetesFatty AcidG Protein-coupled Receptor (GPCR)Homology Modeling

Identifiers

PMID24860101
PMCPMC4106347

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.