Evidence map›Paper›PMID 28169830›Full record

ArticleeLife2017

Phosphorylation of β-arrestin2 at Thr

Elisabeth Cassier, Nathalie Gallay, Thomas Bourquard, Sylvie Claeysen, Joël Bockaert, Pascale Crépieux, Anne Poupon, Eric Reiter, Philippe Marin, Franck Vandermoere

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

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Independent Skeletal Actions of Pituitary Hormones.Endocrinology and metabolism (Seoul, Korea) · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. The Two Non-Visual Arrestins Engage ERK2 Differently.Journal of molecular biology · 2022
    Article
  14. Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins.International journal of molecular sciences · 2022
    Review
  15. Review
  16. Biochemical and physiological insights into TRH receptor-mediated signaling.Frontiers in cell and developmental biology · 2022
    Review
  17. Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. The LPAInternational journal of molecular sciences · 2021
    Review
  19. Review
  20. 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

10 authors at 2 institutions in 1 country.

Elisabeth CassierCNRS, UMR-5203, Institut de Génomique Fonctionnelle, Montpellier, France.
Nathalie GallayINRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, Nouzilly, France.
Thomas BourquardINRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, Nouzilly, France.
Sylvie ClaeysenCNRS, UMR-5203, Institut de Génomique Fonctionnelle, Montpellier, France.
Joël BockaertCNRS, UMR-5203, Institut de Génomique Fonctionnelle, Montpellier, France.
Pascale CrépieuxINRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, Nouzilly, France.
Anne PouponINRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, Nouzilly, France.
Eric ReiterINRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, Nouzilly, France.
Philippe MarinCNRS, UMR-5203, Institut de Génomique Fonctionnelle, Montpellier, France.ORCID 0000-0002-5977-7274
Franck VandermoereCNRS, UMR-5203, Institut de Génomique Fonctionnelle, Montpellier, France.
Centre National de la Recherche Scientifique · FRUniversité de Tours · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to their role in desensitization and internalization of G protein-coupled receptors (GPCRs), β-arrestins are essential scaffolds linking GPCRs to Erk1/2 signaling. However, their role in GPCR-operated Erk1/2 activation differs between GPCRs and the underlying mechanism remains poorly characterized. Here, we show that activation of serotonin 5-HT

Indexed as

Protein Processing, Post-Translationalbeta-Arrestin 2HEK293 CellsHumansMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase KinasesPhosphorylationReceptors, G-Protein-CoupledReceptors, Serotoninbeta-Arrestin 2MAPK1 protein, humanMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase KinasesReceptors, G-Protein-CoupledReceptors, Serotonincell biologyExtracellular signal-regulated kinaseG protein-coupled receptorhumanmass spectrometryphosphorylationratβ-arrestin

Identifiers

PMID28169830
PMCPMC5325621
OpenAlexW2587396276

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.