Evidence map›Paper›PMID 27826255›Full record

ReviewFrontiers in physiology2016

Membrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR Function.

Stefan Gahbauer, Rainer A Böckmann

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Stabilized DNature communications · 2025
    Article
  10. Review
  11. Early Events in βThe Journal of membrane biology · 2024
    Article
  12. DNA-modulated dimerization and oligomerization of cell membrane receptors.Chemical communications (Cambridge, England) · 2024
    Review
  13. Article
  14. Serotonin Signaling through Lipid Membranes.ACS chemical neuroscience · 2024
    Review
  15. G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024
    Review
  16. Modeling membrane geometries implicitly in Rosetta.Protein science : a publication of the Protein Society · 2024
    Article
  17. Article
  18. Review
  19. Review
  20. Article

6 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 1 institution in 1 country.

Stefan GahbauerComputational Biology, Department of Biology, Friedrich-Alexander University of Erlangen-Nürnberg Erlangen, Germany.
Rainer A BöckmannComputational Biology, Department of Biology, Friedrich-Alexander University of Erlangen-Nürnberg Erlangen, Germany.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dimerization or even oligomerization of G protein coupled receptors (GPCRs) causes ongoing, controversial debates about its functional role and the coupled biophysical, biochemical or biomedical implications. A continously growing number of studies hints to a relation between oligomerization and function of GPCRs and strengthens the assumption that receptor assembly plays a key role in the regulation of protein function. Additionally, progress in the structural analysis of GPCR-G protein and GPCR-ligand interactions allows to distinguish between actively functional and non-signaling complexes. Recent findings further suggest that the surrounding membrane, i.e., its lipid composition may modulate the preferred dimerization interface and as a result the abundance of distinct dimeric conformations. In this review, the association of GPCRs and the role of the membrane in oligomerization will be discussed. An overview of the different reported oligomeric interfaces is provided and their capability for signaling discussed. The currently available data is summarized with regard to the formation of GPCR oligomers, their structures and dependency on the membrane microenvironment as well as the coupling of oligomerization to receptor function.

Indexed as

cholesteroldimerizationFRETGPCRmembranemolecular dynamics simulationoligomerizationpalmitoylation

Identifiers

PMID27826255
PMCPMC5078798
OpenAlexW2537341571

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.