Evidence map›Paper›PMID 33437587›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2020

Association of Fluorescent Protein Pairs and Its Significant Impact on Fluorescence and Energy Transfer.

Jacob R Pope, Rachel L Johnson, W David Jamieson, Harley L Worthy, Senthilkumar Kailasam, Rochelle D Ahmed, Ismail Taban, Husam Sabah Auhim, Daniel W Watkins, Pierre J Rizkallah and 2 more

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2020. 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
2.5field-weighted citation impact, top 10% 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.

  1. Article
  2. Article
  3. Absolute quantification of fluorescent protein fusions by mass spectrometry.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review of FRET biosensing and its application in biomolecular detection.American journal of translational research · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

12 authors at 3 institutions in 3 countries.

Jacob R PopeMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.
Rachel L JohnsonMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.
W David JamiesonSchool of Pharmacy Cardiff University Cardiff CF10 3NB UK.ORCID https://orcid.org/0000-0001-8260-5211
Harley L WorthyMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.ORCID https://orcid.org/0000-0001-8497-0773
Senthilkumar KailasamMcGill University and Genome Quebec Innovation Centre Montreal Quebec H3A 0G1 Canada.ORCID https://orcid.org/0000-0002-2816-8222
Rochelle D AhmedMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.
Ismail TabanMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.ORCID https://orcid.org/0000-0003-0387-155X
Husam Sabah AuhimMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.
Daniel W WatkinsMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.ORCID https://orcid.org/0000-0003-3825-5036
Pierre J RizkallahSchool of Medicine Cardiff University Cardiff CF14 4XN UK.ORCID https://orcid.org/0000-0002-9290-0369
Oliver K CastellSchool of Pharmacy Cardiff University Cardiff CF10 3NB UK.ORCID https://orcid.org/0000-0002-6059-8062
D Dafydd JonesMolecular Biosciences School of Biosciences Cardiff University Cardiff CF10 3AX UK.ORCID https://orcid.org/0000-0001-7709-3995
Cardiff University · GBMcGill University and Génome Québec Innovation Centre · CAUniversity of Baghdad · IQ

Funding

Biotechnology and Biological Sciences Research Council BB/H003746/1Wellcome Trust
6 · The paper itself

Abstract

Fluorescent proteins (FPs) are commonly used in pairs to monitor dynamic biomolecular events through changes in proximity via distance dependent processes such as Förster resonance energy transfer (FRET). The impact of FP association is assessed by predicting dimerization sites in silico and stabilizing the dimers by bio-orthogonal covalent linkages. In each tested case dimerization changes inherent fluorescence, including FRET. GFP homodimers demonstrate synergistic behavior with the dimer being brighter than the sum of the monomers. The homodimer structure reveals the chromophores are close with favorable transition dipole alignments and a highly solvated interface. Heterodimerization (GFP with Venus) results in a complex with ≈87% FRET efficiency, significantly below the 99.7% efficiency predicted. A similar efficiency is observed when the wild-type FPs are fused to a naturally occurring protein-protein interface system. GFP complexation with mCherry results in loss of mCherry fluorescence. Thus, simple assumptions used when monitoring interactions between proteins via FP FRET may not always hold true, especially under conditions whereby the protein-protein interactions promote FP interaction.

Indexed as

fluorescencefluorescent proteinsFörster resonance energy transfer (FRET)oligomerizationprotein design

Identifiers

PMID33437587
PMCPMC7788595
OpenAlexW3104795035

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.