Evidence map›Paper›PMID 24634666›Full record

ReviewFrontiers in endocrinology2014

Biophysical Detection of Diversity and Bias in GPCR Function.

Werner C Jaeger, Stephen P Armstrong, Stephen J Hill, Kevin D G Pfleger

Abstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. GPCR Heterodimers: Implications for Biased Signaling.Handbook of experimental pharmacology · 2026
    Review
  2. Review
  3. Orexin Signaling: A Complex, Multifaceted Process.Frontiers in cellular neuroscience · 2022
    Review
  4. Review
  5. Article
  6. Investigation of Receptor Heteromers Using NanoBRET Ligand Binding.International journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Complex Formation between VEGFR2 and the βCell chemical biology · 2019
    Article
  10. Article
  11. NanoBRET: The Bright Future of Proximity-Based Assays.Frontiers in bioengineering and biotechnology · 2019
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. G Protein-Coupled Receptor Heteromers.Annual review of pharmacology and toxicology · 2016
    Review
  18. Article
  19. 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.

Werner C JaegerMolecular Endocrinology and Pharmacology, Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia , Perth, WA , Australia.
Stephen P ArmstrongMolecular Endocrinology and Pharmacology, Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia , Perth, WA , Australia.
Stephen J HillCell Signalling Research Group, School of Life Sciences, Queen's Medical Centre, University of Nottingham Medical School , Nottingham , UK.
Kevin D G PflegerMolecular Endocrinology and Pharmacology, Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia , Perth, WA , Australia ; Dimerix Bioscience Pty Ltd , Perth, WA , Australia.

Funding

Medical Research Council G0800006
6 · The paper itself

Abstract

Guanine nucleotide binding protein (G protein)-coupled receptors (GPCRs) function in complexes with a range of molecules and proteins including ligands, G proteins, arrestins, ubiquitin, and other receptors. Elements of these complexes may interact constitutively or dynamically, dependent upon factors such as ligand binding, phosphorylation, and dephosphorylation. They may also be allosterically modulated by other proteins in a manner that changes temporally and spatially within the cell. Elucidating how these complexes function has been greatly enhanced by biophysical technologies that are able to monitor proximity and/or binding, often in real time and in live cells. These include resonance energy transfer approaches such as bioluminescence resonance energy transfer (BRET) and fluorescence resonance energy transfer (FRET). Furthermore, the use of fluorescent ligands has enabled novel insights into allosteric interactions between GPCRs. Consequently, biophysical approaches are helping to unlock the amazing diversity and bias in G protein-coupled receptor signaling.

Indexed as

bioluminescence resonance energy transferBRETfluorescence resonance energy transferFRETGPCRGPCR-HITheteromerReceptor-HIT

Identifiers

PMID24634666
PMCPMC3943086

What Socratic 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 Socratic graph.