Evidence map›Paper›PMID 35417013›Full record

ArticleProtein engineering, design & selection : PEDS2022

Cyan fluorescent proteins derived from mNeonGreen.

Landon Zarowny, Damien Clavel, Ryan Johannson, Kévin Duarte, Hadrien Depernet, Jérôme Dupuy, Heather Baker, Alex Brown, Antoine Royant, Robert E Campbell

Open access · hybridAbstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 6 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

10 authors at 3 institutions in 3 countries.

Landon ZarownyDepartment of Chemistry, University of Alberta, Edmonton T6G 2G2, Canada.
Damien ClavelUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France.
Ryan JohannsonDepartment of Chemistry, University of Alberta, Edmonton T6G 2G2, Canada.ORCID 0000-0003-4650-1620
Kévin DuarteUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France.
Hadrien DepernetStructural Biology Group, European Synchrotron Radiation Facility, 38043 Grenoble, France.
Jérôme DupuyUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France.
Heather BakerDepartment of Chemistry, University of Alberta, Edmonton T6G 2G2, Canada.
Alex BrownDepartment of Chemistry, University of Alberta, Edmonton T6G 2G2, Canada.ORCID 0000-0002-5384-9222
Antoine RoyantUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 38000 Grenoble, France.
Robert E CampbellDepartment of Chemistry, University of Alberta, Edmonton T6G 2G2, Canada.ORCID 0000-0003-0604-092X
University of Alberta · CACentre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · 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

mNeonGreen, an engineered green fluorescent protein (GFP) derived from lancelet, is one of the most brightly fluorescent homologs of Aequorea victoria jellyfish GFP (avGFP) yet reported. In this work, we investigated whether this bright fluorescence might be retained in homologs of mNeonGreen with modified chromophore structures and altered fluorescent hues. We found mNeonGreen to be generally less tolerant than avGFP to chromophore modification by substitution of the key chromophore-forming tyrosine residue with other aromatic amino acids. However, we were ultimately successful in creating a variant, designated as NeonCyan1, with a tryptophan-derived cyan fluorescent protein (CFP)-type chromophore, and two additional mutants with distinct spectral hues. Structural, computational, and photophysical characterization of NeonCyan1 and its variants provided insight into the factors that control the fluorescence emission color. Though not recommended as replacements for contemporary CFP variants, we demonstrate that NeonCyan1 variants are potentially suitable for live cell imaging applications.

Indexed as

Green Fluorescent ProteinsLuminescent ProteinsSpectrometry, FluorescenceCyan Fluorescent ProteinGreen Fluorescent ProteinsLuminescent Proteinscrystal structurefluorescence microscopyfluorescent proteinprotein engineeringtryptophan-derived chromophore

Identifiers

PMID35417013
PMCPMC9083105
OpenAlexW4223596430

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.