Evidence map›Paper›PMID 26732634›Full record

ArticleScientific reports2016

Rational design of ultrastable and reversibly photoswitchable fluorescent proteins for super-resolution imaging of the bacterial periplasm.

Mariam El Khatib, Alexandre Martins, Dominique Bourgeois, Jacques-Philippe Colletier, Virgile Adam

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Complex Multistate Photophysics of a Rhodanine Photoswitch.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Article
  5. Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  6. Photoswitchable Fluorescent Proteins: Mechanisms on Ultrafast Timescales.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
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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

5 authors.

Mariam El KhatibUniv. Grenoble Alpes, IBS, F-38044 Grenoble, France.
Alexandre MartinsUniv. Grenoble Alpes, IBS, F-38044 Grenoble, France.
Dominique BourgeoisUniv. Grenoble Alpes, IBS, F-38044 Grenoble, France.
Jacques-Philippe ColletierUniv. Grenoble Alpes, IBS, F-38044 Grenoble, France.
Virgile AdamUniv. Grenoble Alpes, IBS, F-38044 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phototransformable fluorescent proteins are central to several nanoscopy approaches. As yet however, there is no available variant allowing super-resolution imaging in cell compartments that maintain oxidative conditions. Here, we report the rational design of two reversibly switchable fluorescent proteins able to fold and photoswitch in the bacterial periplasm, rsFolder and rsFolder2. rsFolder was designed by hybridisation of Superfolder-GFP with rsEGFP2, and inherited the fast folding properties of the former together with the rapid switching of the latter, but at the cost of a reduced switching contrast. Structural characterisation of the switching mechanisms of rsFolder and rsEGFP2 revealed different scenarios for chromophore cis-trans isomerisation and allowed designing rsFolder2, a variant of rsFolder that exhibits improved switching contrast and is amenable to RESOLFT nanoscopy. The rsFolders can be efficiently expressed in the E. coli periplasm, opening the door to the nanoscale investigation of proteins localised in hitherto non-observable cellular compartments.

Indexed as

Models, MolecularEscherichia coliGene ExpressionHydrogen BondingLuminescent ProteinsMicroscopy, FluorescenceMolecular ImagingMutationPeriplasmProtein ConformationQuantitative Structure-Activity RelationshipLuminescent Proteins

Identifiers

PMID26732634
PMCPMC4702087

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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.