Evidence map›Paper›PMID 25541108›Full record

ReviewTrends in pharmacological sciences2015

Generic GPCR residue numbers - aligning topology maps while minding the gaps.

Vignir Isberg, Chris de Graaf, Andrea Bortolato, Vadim Cherezov, Vsevolod Katritch, Fiona H Marshall, Stefan Mordalski, Jean-Philippe Pin, Raymond C Stevens, Gerrit Vriend and 1 more

Abstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 295 papers.

0numbers the graph read from it
0cells of the map it votes in
295citing papers in PubMed
–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

295 citing papers in PubMed.

  1. Trial
  2. Review
  3. Article
  4. 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
  5. Article
  6. GnRH Promotes Gonadotropin Synthesis and Secretion in the Bovine Anterior Pituitary by Inhibiting METTL1-Mediated m7G Modification of FOXO1 mRNA.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  7. The structure of the dopamine DScience advances · 2026
    Article
  8. Article
  9. Article
  10. The Origins of GPCRs.International journal of molecular sciences · 2026
    Review
  11. Article
  12. Molecular mechanism of allosteric modulation of opioid receptors.Signal transduction and targeted therapy · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  19. Article
  20. Article

235 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

11 authors.

Vignir IsbergDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Chris de GraafDivision of Medicinal Chemistry, Faculty of Sciences, Amsterdam Institute for Molecules, Medicines and Systems, VU University Amsterdam, The Netherlands.
Andrea BortolatoHeptares Therapeutics Ltd, Welwyn Garden City, UK.
Vadim CherezovThe Bridge@USC, Department of Chemistry, University of Southern California, Los Angeles, CA 90089 USA.
Vsevolod KatritchThe Bridge@USC, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089 USA.
Fiona H MarshallHeptares Therapeutics Ltd, Welwyn Garden City, UK.
Stefan MordalskiDepartment of Medicinal Chemistry, Institute of Pharmacology, Polish Academy of Sciences, Krakow, Poland; Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland.
Jean-Philippe PinInstitute of Functional Genomics, Centre National de la Recherche Scientifique (CNRS) Unité Mixte de Recherche 5203, Universities Montpellier, Montpellier, France; Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 661, Montpellier, France.
Raymond C StevensThe Bridge@USC, Department of Chemistry, University of Southern California, Los Angeles, CA 90089 USA; The Bridge@USC, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089 USA.
Gerrit VriendCentre for Molecular and Biomolecular Informatics (CMBI), Radboudumc, Nijmegen, The Netherlands.
David E GloriamDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. Electronic address: david.gloriam@sund.ku.dk.

Funding

Project 3U54GM094618 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STEVENS, RAYMOND C · 2010 to 2014
$17.1M
Structure-Function of Opioid ReceptorsP01DA035764 · NIDA · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEREZOV, VADIM, ROTH, BRYAN L. · 2014 to 2018
$7.1M
European Research Council 639125NIDA NIH HHS P01 DA035764NIGMS NIH HHS U54 GM094618
6 · The paper itself

Abstract

Generic residue numbers facilitate comparisons of, for example, mutational effects, ligand interactions, and structural motifs. The numbering scheme by Ballesteros and Weinstein for residues within the class A GPCRs (G protein-coupled receptors) has more than 1100 citations, and the recent crystal structures for classes B, C, and F now call for a community consensus in residue numbering within and across these classes. Furthermore, the structural era has uncovered helix bulges and constrictions that offset the generic residue numbers. The use of generic residue numbers depends on convenient access by pharmacologists, chemists, and structural biologists. We review the generic residue numbering schemes for each GPCR class, as well as a complementary structure-based scheme, and provide illustrative examples and GPCR database (GPCRDB) web tools to number any receptor sequence or structure.

Indexed as

HumansProtein ConformationReceptors, G-Protein-CoupledSequence AlignmentSequence Analysis, ProteinReceptors, G-Protein-CoupledG protein-coupled receptorligand bindingmutational effectssequence alignmentsstructural motifs

Identifiers

PMID25541108
PMCPMC4408928

What OpenQuestion holds

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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.