Evidence map›Paper›PMID 33128009›Full record

ArticleCommunications biology2020

Absolute quantum yield measurements of fluorescent proteins using a plasmonic nanocavity.

Daja Ruhlandt, Martin Andresen, Nickels Jensen, Ingo Gregor, Stefan Jakobs, Jörg Enderlein, Alexey I Chizhik

Abstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Bright monomeric fluorescent protein elite-niRFP704 for two-channel near-infrared STED nanoscopy.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Engineered fluorogenic HaloTag ligands for turn-on labelling in live cells.Chemical communications (Cambridge, England) · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  10. 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

7 authors.

Daja RuhlandtGeorg-August-University Göttingen, Third Institute of Physics - Biophysics, Göttingen, Germany.
Martin AndresenDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Nickels JensenDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Ingo GregorGeorg-August-University Göttingen, Third Institute of Physics - Biophysics, Göttingen, Germany.ORCID 0000-0002-1775-2159
Stefan JakobsDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.ORCID 0000-0002-8028-3121
Jörg EnderleinGeorg-August-University Göttingen, Third Institute of Physics - Biophysics, Göttingen, Germany. jenderl@gwdg.de.ORCID 0000-0001-5091-7157
Alexey I ChizhikGeorg-August-University Göttingen, Third Institute of Physics - Biophysics, Göttingen, Germany. alexey.chizhik@phys.uni-goettingen.de.ORCID 0000-0003-0454-5924

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the key photophysical properties of fluorescent proteins that is most difficult to measure is the quantum yield. It describes how efficiently a fluorophore converts absorbed light into fluorescence. Its measurement using conventional methods become particularly problematic when it is unknown how many of the proposedly fluorescent molecules of a sample are indeed fluorescent (for example due to incomplete maturation, or the presence of photophysical dark states). Here, we use a plasmonic nanocavity-based method to measure absolute quantum yield values of commonly used fluorescent proteins. The method is calibration-free, does not require knowledge about maturation or potential dark states, and works on minute amounts of sample. The insensitivity of the nanocavity-based method to the presence of non-luminescent species allowed us to measure precisely the quantum yield of photo-switchable proteins in their on-state and to analyze the origin of the residual fluorescence of protein ensembles switched to the dark state.

Indexed as

CalibrationEquipment DesignFluorescenceFluorescent DyesGreen Fluorescent ProteinsLuminescent ProteinsMicroscopy, ConfocalPhotochemistryQuantum Theoryenhanced green fluorescent proteinFluorescent DyesGreen Fluorescent ProteinsLuminescent Proteins

Identifiers

PMID33128009
PMCPMC7599333

What OpenQuestion holds

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Registered trials

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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.