Evidence map›Paper›PMID 35427647›Full record

ArticleThe Journal of biological chemistry2022

Selective phosphorylation of threonine residues defines GPR84-arrestin interactions of biased ligands.

Sara Marsango, Richard J Ward, Laura Jenkins, Adrian J Butcher, Zobaer Al Mahmud, Louis Dwomoh, Falko Nagel, Stefan Schulz, Irina G Tikhonova, Andrew B Tobin and 1 more

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. 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

11 authors at 4 institutions in 2 countries.

Sara MarsangoThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Richard J WardThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Laura JenkinsThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Adrian J ButcherDepartment of Clinical Neurosciences, University of Cambridge, Cambridge, United Kingdom.
Zobaer Al MahmudThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Louis DwomohThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Falko Nagel7TM Antibodies GmbH, Jena, Germany.
Stefan Schulz7TM Antibodies GmbH, Jena, Germany; Institute of Pharmacology and Toxicology, University Hospital Jena, Jena, Germany.
Irina G TikhonovaSchool of Pharmacy, Medical Biology Centre, Queen's University Belfast, Belfast, United Kingdom.
Andrew B TobinThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Graeme MilliganThe Centre for Translational Pharmacology, Institute of Molecular, Cellular and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom. Electronic address: Graeme.Milligan@glasgow.ac.uk.
University of Glasgow · GBJena University Hospital · DEQueen's University Belfast · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R007101/1Biotechnology and Biological Sciences Research Council BB/T000562/1Medical Research Council MC_PC_17160
6 · The paper itself

Abstract

GPR84 is an immune cell-expressed, proinflammatory receptor currently being assessed as a therapeutic target in conditions including fibrosis and inflammatory bowel disease. Although it was previously shown that the orthosteric GPR84 activators 2-HTP and 6-OAU promoted its interactions with arrestin-3, a G protein-biased agonist DL-175 did not. Here, we show that replacement of all 21 serine and threonine residues within i-loop 3 of GPR84, but not the two serines in the C-terminal tail, eliminated the incorporation of [

Indexed as

ArrestinsThreoninebeta-Arrestin 2HumansLigandsMutationPhosphorylationReceptors, G-Protein-CoupledSerineArrestinsbeta-Arrestin 2GPR84 protein, humanLigandsReceptors, G-Protein-CoupledSerineThreoninearrestin recruitmentGPR84G protein–coupled receptor phosphorylationGRK2/3phospho-site specific antisera

Identifiers

PMID35427647
PMCPMC9118924
OpenAlexW4223575014

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.