Evidence map›Paper›PMID 35396120›Full record

ReviewTrends in biochemical sciences2022

Structural basis of GPCR coupling to distinct signal transducers: implications for biased signaling.

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

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.7field-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

23 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Beyond G protein and arrestin: GRK2-biased β₂AR signaling.Trends in pharmacological sciences · 2025
    Article
  4. GPCR signaling via cAMP nanodomains.The Biochemical journal · 2025
    Review
  5. Review
  6. Review
  7. Molecular Determinant Underlying Selective Coupling of Primary G-Protein by Class A GPCRs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Pharmacological reviews · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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 and Pharmacology, Faculty of Pharmacy, Mazandaran University of Medical Sciences, Sari, Iran; Pharmaceutical Sciences Research Center, Faculty of Pharmacy, Mazandaran University of Medical Sciences, Sari, Iran.
Mehdi GharghabiDepartment of Cancer Biology and Genetics, The Ohio State University Wexner Medical Center, Columbus, OH, USA.
Eugenia V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA.
Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA. Electronic address: vsevolod.gurevich@vanderbilt.edu.
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
NEI NIH HHS R01 EY011500NIGMS NIH HHS R35 GM122491
6 · The paper itself

Abstract

Three classes of G-protein-coupled receptor (GPCR) partners - G proteins, GPCR kinases, and arrestins - preferentially bind active GPCRs. Our analysis suggests that the structures of GPCRs bound to these interaction partners available today do not reveal a clear conformational basis for signaling bias, which would have enabled the rational design of biased GRCR ligands. In view of this, three possibilities are conceivable: (i) there are no generalizable GPCR conformations conducive to binding a particular type of partner; (ii) subtle differences in the orientation of individual residues and/or their interactions not easily detectable in the receptor-transducer structures determine partner preference; or (iii) the dynamics of GPCR binding to different types of partners rather than the structures of the final complexes might underlie transducer bias.

Indexed as

ArrestinsReceptors, G-Protein-CoupledLigandsProtein BindingSignal TransductionArrestinsLigandsReceptors, G-Protein-Coupledarrestinbiased signalingGPCRGPCR kinaseG protein

Identifiers

PMID35396120
PMCPMC9189013
OpenAlexW4223570521

What OpenQuestion holds

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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.