Evidence map›Paper›PMID 33557162›Full record

ReviewBiomolecules2021

Receptor-Arrestin Interactions: The GPCR Perspective.

Mohammad Seyedabadi, Mehdi Gharghabi, Eugenia V Gurevich, Vsevolod V Gurevich

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. From empirical screening to lipid trolling: the evolution of extrahelical allosteric modulators of AMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Review
  3. Article
  4. Canonical Cannabinoid Receptors.Current topics in behavioral neurosciences · 2026
    Review
  5. Review
  6. Biased signalingActa pharmaceutica Sinica. B · 2025
    Review
  7. Review
  8. Review
  9. An atomic look at the interface of GHSR and its partners.Computational and structural biotechnology journal · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. First Potent Macrocyclic AACS pharmacology & translational science · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

4 authors at 3 institutions in 2 countries.

Mohammad SeyedabadiDepartment of Toxicology & Pharmacology, Faculty of Pharmacy, Mazandaran University of Medical Sciences, Sari 48471-93698, Iran.ORCID 0000-0003-0044-8270
Mehdi GharghabiDepartment of Cancer Biology and Genetics, The Ohio State University Wexner Medical Center, Columbus, OH 43210, USA.
Eugenia V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.ORCID 0000-0002-3950-5351
Vanderbilt University · USMazandaran University of Medical Sciences · IRThe Ohio State University Wexner Medical Center · US

Funding

STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
Targeted Engineering of Designer Arrestins to Regulate Cell SignalingR35GM122491 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2017 to 2021
$2.6M
Signaling regulation in the striatum in Parkinson's diseaseR01NS065868 · NINDS · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2009 to 2013
$1.7M
The role of receptor desensitization machinery in psychostimulant addictionR21DA030103 · NIDA · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2011 to 2012
$390k
NEI NIH HHS EY011500NIDA NIH HHS R21 DA030103NIGMS NIH HHS GM122491NINDS NIH HHS R01 NS065868
6 · The paper itself

Abstract

Arrestins are a small family of four proteins in most vertebrates that bind hundreds of different G protein-coupled receptors (GPCRs). Arrestin binding to a GPCR has at least three functions: precluding further receptor coupling to G proteins, facilitating receptor internalization, and initiating distinct arrestin-mediated signaling. The molecular mechanism of arrestin-GPCR interactions has been extensively studied and discussed from the "arrestin perspective", focusing on the roles of arrestin elements in receptor binding. Here, we discuss this phenomenon from the "receptor perspective", focusing on the receptor elements involved in arrestin binding and emphasizing existing gaps in our knowledge that need to be filled. It is vitally important to understand the role of receptor elements in arrestin activation and how the interaction of each of these elements with arrestin contributes to the latter's transition to the high-affinity binding state. A more precise knowledge of the molecular mechanisms of arrestin activation is needed to enable the construction of arrestin mutants with desired functional characteristics.

Indexed as

AnimalsArrestinArrestinsBinding SitesCattleCrystallography, X-RayFishesHumansHydrophobic and Hydrophilic InteractionsMiceModels, MolecularMutationPhosphorylationProtein BindingProtein ConformationProtein DomainsArrestinArrestinsProtein IsoformsReceptors, G-Protein-Coupledarrestinconformational changeGPCRprotein–protein interactionssignaling

Identifiers

PMID33557162
PMCPMC7913897
OpenAlexW3126619508

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.