Evidence map›Paper›PMID 40238862›Full record

ArticleScience advances2025

A palette of bright and photostable monomeric fluorescent proteins for bacterial time-lapse imaging.

Nathan Fraikin, Agathe Couturier, Romain Mercier, Christian Lesterlin

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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. Serendipitous crystal structure of mJuniper, a rationally designed cyan fluorescent protein.Acta crystallographica. Section F, Structural biology communications · 2026
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  10. Phenylacetic acid mediatesMicrobiology (Reading, England) · 2026
    Article
  11. Article
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  14. Conjugative delivery of toxin genesJournal of bacteriology · 2025
    Article
  15. Article
  16. 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

4 authors.

Nathan FraikinMolecular Microbiology and Structural Biochemistry (MMSB), Université Lyon 1, CNRS, Inserm, UMR5086, 69007 Lyon, France.ORCID 0000-0002-0329-5313
Agathe CouturierMolecular Microbiology and Structural Biochemistry (MMSB), Université Lyon 1, CNRS, Inserm, UMR5086, 69007 Lyon, France.ORCID 0000-0003-0923-253X
Romain MercierMolecular Microbiology and Structural Biochemistry (MMSB), Université Lyon 1, CNRS, Inserm, UMR5086, 69007 Lyon, France.
Christian LesterlinMolecular Microbiology and Structural Biochemistry (MMSB), Université Lyon 1, CNRS, Inserm, UMR5086, 69007 Lyon, France.ORCID 0000-0002-9108-0848

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent proteins (FPs) are pivotal for examining protein production, localization, and dynamics in live bacterial cells. However, the use of FPs in time-lapse imaging is frequently constrained by issues such as oligomerization or limited photostability. Here, we report the engineering of novel cyan, green, yellow, and red FPs that exhibit improved photostability and aggregation properties while retaining high in vivo brightness. We first derived superfolder green fluorescent protein into mChartreuse, a brighter, more photostable, and monomeric fluorophore. mChartreuse was further derived into cyan and yellow variants with enhanced photostability and dispersibility. We also report a mutation that eliminates residual oligomerization in red FPs derived from

Indexed as

Luminescent ProteinsTime-Lapse ImagingEscherichia coliGreen Fluorescent ProteinsMicroscopy, FluorescenceMutationGreen Fluorescent ProteinsLuminescent Proteins

Identifiers

PMID40238862
PMCPMC12002091

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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.