Evidence map›Paper›PMID 24945870›Full record

ArticlePloS one2014

Analyzing receptor assemblies in the cell membrane using fluorescence anisotropy imaging with TIRF microscopy.

Miklos Erdelyi, Joseph Simon, Eric A Barnard, Clemens F Kaminski

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2019
    Article
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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 at 2 institutions in 2 countries.

Miklos ErdelyiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, United Kingdom; Analytical Science Division, National Physical Laboratory, Teddington, Middlesex, United Kingdom; Department of Optics and Quantum Electronics, University of Szeged, Szeged, Hungary.
Joseph SimonDepartment of Pharmacology, University of Cambridge, Cambridge, United Kingdom.
Eric A BarnardDepartment of Pharmacology, University of Cambridge, Cambridge, United Kingdom.
Clemens F KaminskiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, United Kingdom.
University of Cambridge · GBUniversity of Szeged · HU

Funding

Medical Research Council MR/K015850/1Medical Research Council MR/K02292X/1Wellcome TrustWellcome Trust 089703/Z/09/Z
6 · The paper itself

Abstract

Signaling within and between animal cells is controlled by the many receptor proteins in their membrane. They variously operate as trans-membrane monomers and homo- or hetero-dimers, and may assemble with ion-channels: analyses thereof are needed in studies of receptor actions in tissue physiology and pathology. Interactions between membrane proteins are detectable when pre-labeled with fluorophores, but a much fuller analysis is achievable via advanced optical techniques on living cells. In this context, the measurement of polarization anisotropy in the emitted fluorescence has been the least exploited. Here we demonstrate its methodology and particular advantages in the study of receptor protein assembly. Through excitation in both TIRF and EPI fluorescence illumination modes we are able to quantify and suppress contributions to the signal from extraneous intra-cellular fluorescence, and we show that the loss of fluorescence-polarization measured in membrane proteins reports on receptor protein assembly in real time. Receptor monomers and homo-dimers in the cell membrane can be analyzed quantitatively and for homo-dimers only a single fluorescent marker is needed, thus suppressing ambiguities that arise in alternative assays, which require multiple label moieties and which are thus subject to stoichiometric uncertainty.

Indexed as

Signal TransductionAdenosine TriphosphateAmino Acid SequenceDeoxyadenine NucleotidesFluorescence PolarizationGene ExpressionGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHumansMicroscopy, FluorescenceMolecular Sequence DataPlasmidsProtein MultimerizationPurinergic P2Y Receptor AgonistsPurinergic P2Y Receptor Antagonists2-iodo-N(6)-methyl-(N)-methanocarba-2'-deoxyadenosine-3',5'-bisphosphate2-methylthio-ATPAdenosine TriphosphateCyan Fluorescent ProteinDeoxyadenine NucleotidesGreen Fluorescent ProteinsPurinergic P2Y Receptor AgonistsPurinergic P2Y Receptor AntagonistsReceptors, Purinergic P2Y1Thionucleotides

Identifiers

PMID24945870
PMCPMC4063901
OpenAlexW2093532742

What OpenQuestion holds

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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.