Evidence map›Paper›PMID 30911173›Full record

ArticleNature protocols2019

Bioluminescence resonance energy transfer-based imaging of protein-protein interactions in living cells.

Hiroyuki Kobayashi, Louis-Philippe Picard, Anne-Marie Schönegge, Michel Bouvier

Abstract read
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In one paragraph

Article in Nature protocols, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
–field-weighted citation impact
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

55 citing papers in PubMed.

  1. Review
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  10. Precise andACS central science · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Genetically Encoded Metabolic Sensors to Study Retina Metabolism.Advances in experimental medicine and biology · 2025
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. OptimizediScience · 2024
    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

4 authors.

Hiroyuki KobayashiInstitute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montreal, QC, Canada.
Louis-Philippe PicardInstitute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montreal, QC, Canada.
Anne-Marie SchöneggeInstitute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montreal, QC, Canada.
Michel BouvierInstitute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montreal, QC, Canada. michel.bouvier@umontreal.ca.ORCID http://orcid.org/0000-0003-1128-0100

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bioluminescence resonance energy transfer (BRET) is a transfer of energy between a luminescence donor and a fluorescence acceptor. Because BRET occurs when the distance between the donor and acceptor is <10 nm, and its efficiency is inversely proportional to the sixth power of distance, it has gained popularity as a proximity-based assay to monitor protein-protein interactions and conformational rearrangements in live cells. In such assays, one protein of interest is fused to a bioluminescent energy donor (luciferases from Renilla reniformis or Oplophorus gracilirostris), and the other protein is fused to a fluorescent energy acceptor (such as GFP or YFP). Because the BRET donor does not require an external light source, it does not lead to phototoxicity or autofluorescence. It therefore represents an interesting alternative to fluorescence-based imaging such as FRET. However, the low signal output of BRET energy donors has limited the spatiotemporal resolution of BRET imaging. Here, we describe how recent improvements in detection devices and BRET probes can be used to markedly improve the resolution of BRET imaging, thus widening the field of BRET imaging applications. The protocol described herein involves three main stages. First, cell preparation and transfection require 3 d, including cell culture time. Second, image acquisition takes 10-120 min per sample, after an initial 60 min for microscope setup. Finally, image analysis typically takes 1-2 h. The choices of energy donor, acceptor, luminescent substrates, cameras and microscope setup, as well as acquisition modes to be used for different applications, are also discussed.

Indexed as

AnimalsBacterial ProteinsBenzeneacetamidesbeta-Arrestin 2Fluorescence Resonance Energy TransferGene ExpressionGreen Fluorescent ProteinsHEK293 CellsHumansImidazolesLuminescent MeasurementsLuminescent ProteinsMembrane ProteinsOptical ImagingPlasmidsProtein Interaction MappingBacterial ProteinsBenzeneacetamidesbeta-Arrestin 2coelenteramidecoelenterazineGreen Fluorescent ProteinsImidazolesLuminescent ProteinsMembrane ProteinsPyrazinesReceptors, VasopressinRecombinant Fusion ProteinsRTL8C protein, humanyellow fluorescent protein, Bacteria

Identifiers

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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.