Evidence map›Paper›PMID 20015298›Full record

ReviewBritish journal of pharmacology2010

Bimolecular fluorescence complementation: lighting up seven transmembrane domain receptor signalling networks.

Rachel H Rose, Stephen J Briddon, Nicholas D Holliday

Open access · bronzeAbstract readReview
In one paragraph

Review in British journal of pharmacology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Efficient G protein coupling is not required for agonist-mediated internalization and membrane reorganization of the adenosine AFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  4. A localized adaptor protein performs distinct functions at theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Molybdenum Cofactor Biosynthesis Network:Frontiers in plant science · 2017
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Allosteric interactions across native adenosine-A3 receptor homodimers: quantification using single-cell ligand-binding kinetics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    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 at 1 institution in 1 country.

Rachel H RoseInstitute of Cell Signalling, School of Biomedical Sciences, University of Nottingham, Queen's Medical Centre, Nottingham, UK.
Stephen J Briddon
Nicholas D Holliday
University of Nottingham · GB

Funding

Medical Research Council G0700049Medical Research Council G0800006
6 · The paper itself

Abstract

There is increasing complexity in the organization of seven transmembrane domain (7TM) receptor signalling pathways, and in the ability of their ligands to modulate and direct this signalling. Underlying these events is a network of protein interactions between the 7TM receptors themselves and associated effectors, such as G proteins and beta-arrestins. Bimolecular fluorescence complementation, or BiFC, is a technique capable of detecting these protein-protein events essential for 7TM receptor function. Fluorescent proteins, such as those from Aequorea victoria, are split into two non-fluorescent halves, which then tag the proteins under study. On association, these fragments refold and regenerate a mature fluorescent protein, producing a BiFC signal indicative of complex formation. Here, we review the experimental criteria for successful application of BiFC, considered in the context of 7TM receptor signalling events such as receptor dimerization, G protein and beta-arrestin signalling. The advantages and limitations of BiFC imaging are compared with alternative resonance energy transfer techniques. We show that the essential simplicity of the fluorescent BiFC measurement allows high-content and advanced imaging applications, and that it can probe more complex multi-protein interactions alone or in combination with resonance energy transfer. These capabilities suggest that BiFC techniques will become ever more useful in the analysis of ligand and 7TM receptor pharmacology at the molecular level of protein-protein interactions.

Indexed as

Biosensing TechniquesMicroscopy, FluorescenceMolecular ImagingMolecular Probe TechniquesSignal TransductionAnimalsArrestinsbeta-ArrestinsDose-Response Relationship, DrugFluorescence Recovery After PhotobleachingFluorescence Resonance Energy TransferHumansLigandsLuminescent ProteinsMultiprotein ComplexesProtein BindingArrestinsbeta-ArrestinsLigandsLuminescent ProteinsMultiprotein ComplexesReceptors, G-Protein-Coupledseven-transmembrane G-protein-coupled receptor

Identifiers

PMID20015298
PMCPMC2829200
OpenAlexW1528269861

What OpenQuestion holds

Textmetadata
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.