Evidence map›Paper›PMID 27917830›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution.

Damien Clavel, Guillaume Gotthard, David von Stetten, Daniele De Sanctis, Hélène Pasquier, Gerard G Lambert, Nathan C Shaner, Antoine Royant

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Absolute quantification of fluorescent protein fusions by mass spectrometry.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Review
  5. DNA Dendron Tagging as a Universal Way to Deliver Proteins to Cells.Journal of the American Chemical Society · 2025
    Article
  6. Shining a light on the impact of antifungals onAntimicrobial agents and chemotherapy · 2024
    Article
  7. Article
  8. A monomeric StayGold fluorescent protein.Nature biotechnology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Cyan fluorescent proteins derived from mNeonGreen.Protein engineering, design & selection : PEDS · 2022
    Article
  16. A genetically encoded BRET-based SARS-CoV-2 MCommunications chemistry · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. 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

8 authors at 4 institutions in 2 countries.

Damien ClavelUniversité Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38044 Grenoble, France.
Guillaume GotthardEuropean Synchrotron Radiation Facility, F-38043 Grenoble, France.
David von StettenEuropean Synchrotron Radiation Facility, F-38043 Grenoble, France.
Daniele De SanctisEuropean Synchrotron Radiation Facility, F-38043 Grenoble, France.
Hélène PasquierCNRS, Laboratoire de Chimie Physique, UMR 8000 and Université Paris-Sud, F-91405 Orsay, France.
Gerard G LambertDepartment of Photobiology and Bioimaging, The Scintillon Institute, San Diego, California, USA.
Nathan C ShanerDepartment of Photobiology and Bioimaging, The Scintillon Institute, San Diego, California, USA.
Antoine RoyantUniversité Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38044 Grenoble, France.
European Synchrotron Radiation Facility · FRScintillon Institute · USUniversité Paris-Sud · FRCentre National de la Recherche Scientifique · FR

Funding

Fluorescent proteins for superresolution imagingR01GM109984 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SHANER, NATHAN CHRISTOPHER · 2014 to 2018
$1.8M
NIGMS NIH HHS R01 GM109984
6 · The paper itself

Abstract

Until recently, genes coding for homologues of the autofluorescent protein GFP had only been identified in marine organisms from the phyla Cnidaria and Arthropoda. New fluorescent-protein genes have now been found in the phylum Chordata, coding for particularly bright oligomeric fluorescent proteins such as the tetrameric yellow fluorescent protein lanYFP from Branchiostoma lanceolatum. A successful monomerization attempt led to the development of the bright yellow-green fluorescent protein mNeonGreen. The structures of lanYFP and mNeonGreen have been determined and compared in order to rationalize the directed evolution process leading from a bright, tetrameric to a still bright, monomeric fluorescent protein. An unusual discolouration of crystals of mNeonGreen was observed after X-ray data collection, which was investigated using a combination of X-ray crystallography and UV-visible absorption and Raman spectroscopies, revealing the effects of specific radiation damage in the chromophore cavity. It is shown that X-rays rapidly lead to the protonation of the phenolate O atom of the chromophore and to the loss of its planarity at the methylene bridge.

Indexed as

AnimalsCloning, MolecularCrystallography, X-RayDirected Molecular EvolutionGreen Fluorescent ProteinsLanceletsLuminescent ProteinsModels, MolecularMutationProtein ConformationSpectrum Analysis, RamanGreen Fluorescent ProteinsLuminescent ProteinsBranchiostoma lanceolatumfluorescent proteinin crystallo optical spectroscopyonline Raman spectroscopyspecific radiation damage

Identifiers

PMID27917830
PMCPMC5137226
OpenAlexW2559382139

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.