Evidence map›Paper›PMID 25981303›Full record

ReviewEuropean journal of pharmacology2015

Structural insights into ligand recognition and selectivity for classes A, B, and C GPCRs.

Sang-Min Lee, Jason M Booe, Augen A Pioszak

Abstract readReview
In one paragraph

Review in European journal of pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

30 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Dynamic mechanism for subtype selectivity of endocannabinoids.The Journal of biological chemistry · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Frontiers in endocrinology · 2023
    Article
  12. Activation and Speciation Mechanisms in Class A GPCRs.Journal of molecular biology · 2022
    Article
  13. Article
  14. Review
  15. Structure-based development of a subtype-selective orexin 1 receptor antagonist.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Structure and selectivity engineering of the MScience (New York, N.Y.) · 2020
    Article
  17. Review
  18. Article
  19. Review
  20. Structure-guided development of selective M3 muscarinic acetylcholine receptor antagonists.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

3 authors.

Sang-Min LeeDepartment of Biochemistry and Molecular Biology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Jason M BooeDepartment of Biochemistry and Molecular Biology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Augen A PioszakDepartment of Biochemistry and Molecular Biology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. Electronic address: augen-pioszak@ouhsc.edu.

Funding

RAMP-altered Class B GPCR Hormone RecognitionR01GM104251 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI PIOSZAK, AUGEN A · 2012 to 2024
$4.2M
NIGMS NIH HHS R01 GM104251NIGMS NIH HHS R01GM104251
6 · The paper itself

Abstract

The G protein-coupled receptor (GPCR) superfamily constitutes the largest collection of cell surface signaling proteins with approximately 800 members in the human genome. GPCRs regulate virtually all aspects of physiology and they are an important class of drug targets with ~30% of drugs on the market targeting a GPCR. Breakthroughs in GPCR structural biology in recent years have significantly expanded our understanding of GPCR structure and function and ushered in a new era of structure-based drug design for GPCRs. Crystal structures for nearly thirty distinct GPCRs are now available including receptors from each of the major classes, A, B, C, and F. These structures provide a foundation for understanding the molecular basis of GPCR pharmacology. Here, we review structural mechanisms of ligand recognition and selectivity of GPCRs with a focus on selected examples from classes A, B, and C, and we highlight major unresolved questions for future structural studies.

Indexed as

AnimalsHumansLigandsProtein BindingReceptors, G-Protein-CoupledSubstrate SpecificityLigandsReceptors, G-Protein-CoupledGPCR structureGPCR subtypeLigand recognitionSubtype selectivityX-ray crystallography

Identifiers

PMID25981303
PMCPMC4584177

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.