Evidence map›Paper›PMID 28510206›Full record

ReviewBiophysical reviews2012

Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerisation.

Alan D Goddard, Anthony Watts

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Aptameric Probe Specifically Binding Protein Heterodimer Rather Than Monomers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
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.

Alan D GoddardBiomembrane Structure Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Anthony WattsBiomembrane Structure Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. anthony.watts@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G019738/1Medical Research Council G0900076
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are the largest class of eukaryotic cell-surface receptors and, over the last decade, it has become clear that they are capable of dimerisation. Whilst many biochemical and biophysical approaches have been used to study dimerisation, fluorescence techniques, including Förster resonance energy transfer and single molecule fluorescence, have been key players. Here we review recent contributions of fluorescence techniques to investigate GPCR dimers, including dimerisation in cell membranes and native tissues, the effect of ligand binding on dimerisation and the kinetics of dimer formation and dissociation. The challenges of studying multicomponent membrane protein systems have led to the development and refinement of many fluorescence assays, allowing the functional consequences of receptor dimerisation to be investigated and individual protein molecules to be imaged in the membranes of living cells. It is likely that the fluorescence techniques described here will be of use for investigating many other multicomponent membrane protein systems.

Indexed as

DimerFluorescenceFRETG protein-coupled receptorOligomerisationSingle molecule fluorescence

Identifiers

PMID28510206
PMCPMC5425692
OpenAlexW1990316802

What Socratic 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 Socratic graph.