Evidence map›Paper›PMID 40671276›Full record

ArticleProtein science : a publication of the Protein Society2025

Decoding mEos4b day-long maturation and engineering fast-maturing variants.

Arijit Maity, Oleksandr Glushonkov, Isabel Ayala, Pascale Tacnet, Jip Wulffelé, Philippe Frachet, Bernhard Brutscher, Dominique Bourgeois, Virgile Adam

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Decoding mEos4b day-long maturation and engineering fast-maturing variants.Protein science : a publication of the Protein Society · 2025
    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

9 authors.

Arijit MaityUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Oleksandr GlushonkovIntegrated Structural Biology Grenoble (ISBG), Université Grenoble Alpes, CNRS, CEA, EMBL, Grenoble, France.
Isabel AyalaUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Pascale TacnetUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Jip WulffeléUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Philippe FrachetUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Bernhard BrutscherUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Dominique BourgeoisUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.
Virgile AdamUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.ORCID 0000-0003-2209-7846

Funding

Agence Nationale de la Recherche ANR-20-CE11-0013-01Agence Nationale de la Recherche ANR-22-CE11-0011-01Agence Nationale de la Recherche ANR-22-CE13-0046CNRS research Infrastructure "INFRANALYTICS" FR2054
6 · The paper itself

Abstract

The maturation speed of fluorescent proteins is a crucial parameter that influences cellular brightness, effective labeling efficiency, and temporal resolution in fluorescence microscopy. Green-to-red photoconvertible fluorescent proteins (PCFPs) used in pulse-chase experiments and super-resolution techniques such as Photoactivated Localization Microscopy (PALM), single-particle-tracking PALM (sptPALM), and Minimal Fluorescence Photon Fluxes Microscopy (MINFLUX) may be hampered by slow maturation. We systematically characterized the maturation speed of mEos-derived PCFPs in Escherichia coli and found that, in contrast to pcStar and mEosEM, several variants such as mEos2, mEos3.1, mEos3.2, and mEos4b mature extremely slowly. Strikingly, the oxidation step in these PCFPs is fast and not rate-limiting. Through a structure-guided mutagenesis strategy, we developed a strategy to reduce the day-long maturation time of mEos4b by nearly two orders of magnitude without significantly impacting its molecular brightness and photophysical performance under single-molecule imaging conditions.

Indexed as

Green Fluorescent ProteinsLuminescent ProteinsProtein EngineeringEscherichia coliMicroscopy, FluorescenceGreen Fluorescent ProteinsLuminescent Proteinschromophorefluorescent proteinsmaturationNMRprotein engineeringspectroscopysuper resolution microscopyX‐ray crystallography

Identifiers

PMID40671276
PMCPMC12267110

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.