Evidence map›Paper›PMID 24893771›Full record

ArticleJournal of visualized experiments : JoVE2014

Investigating protein-protein interactions in live cells using bioluminescence resonance energy transfer.

Pelagia Deriziotis, Sarah A Graham, Sara B Estruch, Simon E Fisher

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2014. 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
1.3field-weighted citation impact, top 21% 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, 25 citations in OpenAlex.

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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 1 institution in 1 country.

Pelagia DeriziotisLanguage and Genetics Department, Max Planck Institute for Psycholinguistics.
Sarah A GrahamLanguage and Genetics Department, Max Planck Institute for Psycholinguistics.
Sara B EstruchLanguage and Genetics Department, Max Planck Institute for Psycholinguistics.
Simon E FisherLanguage and Genetics Department, Max Planck Institute for Psycholinguistics; Donders Institute for Brain, Cognition and Behaviour; simon.fisher@mpi.nl.
Max Planck Institute for Psycholinguistics · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assays based on Bioluminescence Resonance Energy Transfer (BRET) provide a sensitive and reliable means to monitor protein-protein interactions in live cells. BRET is the non-radiative transfer of energy from a 'donor' luciferase enzyme to an 'acceptor' fluorescent protein. In the most common configuration of this assay, the donor is Renilla reniformis luciferase and the acceptor is Yellow Fluorescent Protein (YFP). Because the efficiency of energy transfer is strongly distance-dependent, observation of the BRET phenomenon requires that the donor and acceptor be in close proximity. To test for an interaction between two proteins of interest in cultured mammalian cells, one protein is expressed as a fusion with luciferase and the second as a fusion with YFP. An interaction between the two proteins of interest may bring the donor and acceptor sufficiently close for energy transfer to occur. Compared to other techniques for investigating protein-protein interactions, the BRET assay is sensitive, requires little hands-on time and few reagents, and is able to detect interactions which are weak, transient, or dependent on the biochemical environment found within a live cell. It is therefore an ideal approach for confirming putative interactions suggested by yeast two-hybrid or mass spectrometry proteomics studies, and in addition it is well-suited for mapping interacting regions, assessing the effect of post-translational modifications on protein-protein interactions, and evaluating the impact of mutations identified in patient DNA.

Indexed as

Protein Interaction MapsAnimalsBacterial ProteinsEnergy TransferFluorescence Resonance Energy TransferHEK293 CellsHumansLuciferasesLuminescent MeasurementsLuminescent ProteinsRecombinant Fusion ProteinsRenillaBacterial ProteinsLuciferasesLuminescent ProteinsRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID24893771
PMCPMC4207229
OpenAlexW1973799342

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.