Evidence map›Paper›PMID 22506000›Full record

ArticlePloS one2012

A multi-functional imaging approach to high-content protein interaction screening.

Daniel R Matthews, Gilbert O Fruhwirth, Gregory Weitsman, Leo M Carlin, Enyinnaya Ofo, Melanie Keppler, Paul R Barber, Iain D C Tullis, Borivoj Vojnovic, Tony Ng and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Fluorophore spectroscopy in aqueous glycerol solution: the interactions of glycerol with the fluorophore.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
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  10. Time-domain microfluidic fluorescence lifetime flow cytometry for high-throughput Förster resonance energy transfer screening.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2015
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  11. Review
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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

11 authors at 2 institutions in 1 country.

Daniel R MatthewsDivision of Cancer Studies, Randall Division of Cell and Molecular Biophysics, King's College London, London, United Kingdom.
Gilbert O Fruhwirth
Gregory Weitsman
Leo M Carlin
Enyinnaya Ofo
Melanie Keppler
Paul R Barber
Iain D C Tullis
Borivoj Vojnovic
Tony Ng
Simon M Ameer-Beg
King's College London · GBCRUK/MRC Oxford Institute for Radiation Oncology · GB

Funding

Cancer Research UK 15677Cancer Research UK C133/A/1812
6 · The paper itself

Abstract

Functional imaging can provide a level of quantification that is not possible in what might be termed traditional high-content screening. This is due to the fact that the current state-of-the-art high-content screening systems take the approach of scaling-up single cell assays, and are therefore based on essentially pictorial measures as assay indicators. Such phenotypic analyses have become extremely sophisticated, advancing screening enormously, but this approach can still be somewhat subjective. We describe the development, and validation, of a prototype high-content screening platform that combines steady-state fluorescence anisotropy imaging with fluorescence lifetime imaging (FLIM). This functional approach allows objective, quantitative screening of small molecule libraries in protein-protein interaction assays. We discuss the development of the instrumentation, the process by which information on fluorescence resonance energy transfer (FRET) can be extracted from wide-field, acceptor fluorescence anisotropy imaging and cross-checking of this modality using lifetime imaging by time-correlated single-photon counting. Imaging of cells expressing protein constructs where eGFP and mRFP1 are linked with amino-acid chains of various lengths (7, 19 and 32 amino acids) shows the two methodologies to be highly correlated. We validate our approach using a small-scale inhibitor screen of a Cdc42 FRET biosensor probe expressed in epidermoid cancer cells (A431) in a 96 microwell-plate format. We also show that acceptor fluorescence anisotropy can be used to measure variations in hetero-FRET in protein-protein interactions. We demonstrate this using a screen of inhibitors of internalization of the transmembrane receptor, CXCR4. These assays enable us to demonstrate all the capabilities of the instrument, image processing and analytical techniques that have been developed. Direct correlation between acceptor anisotropy and donor FLIM is observed for FRET assays, providing an opportunity to rapidly screen proteins, interacting on the nano-meter scale, using wide-field imaging.

Indexed as

Biosensing TechniquesCell Line, TumorFluorescence PolarizationFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHumansLuminescent ProteinsPhotonsProtein Interaction Domains and MotifsProteinsReceptors, CXCR4Red Fluorescent ProteinSensitivity and SpecificitySmall Molecule LibrariesCXCR4 protein, humanenhanced green fluorescent proteinGreen Fluorescent ProteinsLuminescent ProteinsProteinsReceptors, CXCR4Red Fluorescent ProteinSmall Molecule Libraries

Identifiers

PMID22506000
PMCPMC3323588
OpenAlexW2008351207

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.