Evidence map›Paper›PMID 33273123›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Directionality of light absorption and emission in representative fluorescent proteins.

Jitka Myšková, Olga Rybakova, Jiří Brynda, Petro Khoroshyy, Alexey Bondar, Josef Lazar

Erratum issuedAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. State-dependent motion of a genetically encoded fluorescent biosensor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
  5. Volumetric imaging of the 3D orientation of cellular structures with a polarized fluorescence light-sheet microscope.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Article
  8. Article
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  11. Review
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  14. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Jitka MyškováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 16610 Prague 6, Czech Republic.ORCID 0000-0003-1034-1792
Olga RybakovaInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 16610 Prague 6, Czech Republic.ORCID 0000-0001-9467-1208
Jiří BryndaInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 16610 Prague 6, Czech Republic.ORCID 0000-0003-3675-6769
Petro KhoroshyyInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 16610 Prague 6, Czech Republic.ORCID 0000-0001-5225-9805
Alexey BondarInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 16610 Prague 6, Czech Republic.ORCID 0000-0002-1980-2930
Josef LazarInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 16610 Prague 6, Czech Republic; lazar@uochb.cas.cz.ORCID 0000-0002-6285-3995

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent molecules are like antennas: The rate at which they absorb light depends on their orientation with respect to the incoming light wave, and the apparent intensity of their emission depends on their orientation with respect to the observer. However, the directions along which the most important fluorescent molecules in biology, fluorescent proteins (FPs), absorb and emit light are generally not known. Our optical and X-ray investigations of FP crystals have now allowed us to determine the molecular orientations of the excitation and emission transition dipole moments in the FPs mTurquoise2, eGFP, and mCherry, and the photoconvertible FP mEos4b. Our results will allow using FP directionality in studies of molecular and biological processes, but also in development of novel bioengineering and bioelectronics applications.

Indexed as

AnisotropyCrystallography, X-RayGreen Fluorescent ProteinsLightLuminescent ProteinsMicroscopy, PolarizationRed Fluorescent ProteinGreen Fluorescent ProteinsLuminescent ProteinsRed Fluorescent Proteinfluorescent proteinpolarization microscopytransition dipole moment

Identifiers

PMID33273123
PMCPMC7768707

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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.