Evidence map›Paper›PMID 33345902›Full record

ArticleBiophysical journal2021

Time-Resolved Fluorescence Anisotropy and Molecular Dynamics Analysis of a Novel GFP Homo-FRET Dimer.

Yurema Teijeiro-Gonzalez, Alessandro Crnjar, Andrew J Beavil, Rebecca L Beavil, Jakub Nedbal, Alix Le Marois, Carla Molteni, Klaus Suhling

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2021. 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
1.5field-weighted citation impact, top 18% 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, 34 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

8 authors at 2 institutions in 1 country.

Yurema Teijeiro-GonzalezDepartment of Physics, King's College London, London, United Kingdom. Electronic address: yurema.teijeiro_gonzalez@kcl.ac.uk.
Alessandro CrnjarDepartment of Physics, King's College London, London, United Kingdom.
Andrew J BeavilRandall Centre for Cell and Molecular Biophysics, King's College London, London, United Kingdom.
Rebecca L BeavilRandall Centre for Cell and Molecular Biophysics, King's College London, London, United Kingdom.
Jakub NedbalDepartment of Physics, King's College London, London, United Kingdom.
Alix Le MaroisDepartment of Cell Biology, The Francis Crick Institute, London, United Kingdom.
Carla MolteniDepartment of Physics, King's College London, London, United Kingdom.
Klaus SuhlingDepartment of Physics, King's College London, London, United Kingdom.
King's College London · GBThe Francis Crick Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R004803/1
6 · The paper itself

Abstract

Förster resonance energy transfer (FRET) is a powerful tool to investigate the interaction between proteins in living cells. Fluorescence proteins, such as the green fluorescent protein (GFP) and its derivatives, are coexpressed in cells linked to proteins of interest. Time-resolved fluorescence anisotropy is a popular tool to study homo-FRET of fluorescent proteins as an indicator of dimerization, in which its signature consists of a very short component at the beginning of the anisotropy decay. In this work, we present an approach to study GFP homo-FRET via a combination of time-resolved fluorescence anisotropy, the stretched exponential decay model, and molecular dynamics simulations. We characterize a new, to our knowledge, FRET standard formed by two enhanced GFPs (eGFPs) and a flexible linker of 15 aminoacids (eGFP15eGFP) with this protocol, which is validated by using an eGFP monomer as a reference. An excellent agreement is found between the FRET efficiency calculated from the fit of the eGFP15eGFP fluorescence anisotropy decays with a stretched exponential decay model (〈E

Indexed as

Fluorescence Resonance Energy TransferMolecular Dynamics SimulationFluorescence PolarizationGreen Fluorescent ProteinsMicroscopy, FluorescenceGreen Fluorescent Proteins

Identifiers

PMID33345902
PMCPMC7840444
OpenAlexW3108185277

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.