Evidence map›Paper›PMID 26984408›Full record

ReviewThe Journal of biological chemistry2016

The β-Arrestins: Multifunctional Regulators of G Protein-coupled Receptors.

Jeffrey S Smith, Sudarshan Rajagopal

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed, 1 pooled it
23.3field-weighted citation impact, top 1% 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

154 citing papers in PubMed, 1 synthesis or guideline pooled it, 296 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Local GPCR density tips the balance of μ-opioid receptor trafficking.bioRxiv : the preprint server for biology · 2026
    Article
  8. Beta arrestin 1 is a key regulator of pulmonary vascular tone.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Article
  10. Mechanisms of Location Bias in G Protein-Coupled Receptors.Handbook of experimental pharmacology · 2026
    Review
  11. Review
  12. Article
  13. Review
  14. Biased signalingActa pharmaceutica Sinica. B · 2025
    Review
  15. Article
  16. Article
  17. G Protein-Coupled Receptor Signal Intersection at the Primary Cilium.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  18. Effects of positive mGlu5 modulation on DJournal of psychopharmacology (Oxford, England) · 2025
    Article
  19. Antagonists Enhance Cell-Surface Expression of Mammalian Odorant Receptors.International journal of molecular sciences · 2025
    Article
  20. Article

94 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Jeffrey S SmithFrom the Departments of Biochemistry and.
Sudarshan RajagopalFrom the Departments of Biochemistry and Medicine, Duke University Medical Center, Durham, North Carolina 27710 sudarshan.rajagopal@dm.duke.edu.
Duke Medical Center · USDuke University Hospital · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007171 · NIGMS · DUKE UNIVERSITY · PI KONTOS, CHRISTOPHER D · 1985 to 2021
$31.2M
Noncanonical Receptor Signaling in Pulmonary Arterial HypertensionK08HL114643 · NHLBI · DUKE UNIVERSITY · PI RAJAGOPAL, SUDARSHAN K · 2013 to 2017
$607k
NHLBI NIH HHS K08 HL114643NIGMS NIH HHS T32 GM007171
6 · The paper itself

Abstract

The β-arrestins (βarrs) are versatile, multifunctional adapter proteins that are best known for their ability to desensitize G protein-coupled receptors (GPCRs), but also regulate a diverse array of cellular functions. To signal in such a complex fashion, βarrs adopt multiple conformations and are regulated at multiple levels to differentially activate downstream pathways. Recent structural studies have demonstrated that βarrs have a conserved structure and activation mechanism, with plasticity of their structural fold, allowing them to adopt a wide array of conformations. Novel roles for βarrs continue to be identified, demonstrating the importance of these dynamic regulators of cellular signaling.

Indexed as

AnimalsArrestinHumansProtein ConformationReceptors, G-Protein-CoupledSignal TransductionArrestinReceptors, G-Protein-Coupled7-helix receptorarrestinG protein-coupled receptor (GPCR)receptor desensitizationreceptor endocytosissignaling

Identifiers

PMID26984408
PMCPMC4861465
OpenAlexW2300047490

What OpenQuestion holds

Textmetadata
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.