Evidence map›Paper›PMID 27534893›Full record

ArticleScientific reports2016

Single molecule super-resolution imaging of proteins in living Salmonella enterica using self-labelling enzymes.

Britta Barlag, Oliver Beutel, Dennis Janning, Frederik Czarniak, Christian P Richter, Carina Kommnick, Vera Göser, Rainer Kurre, Florian Fabiani, Marc Erhardt and 2 more

Open access · goldAbstract 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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
13.1field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
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  8. Recent biomedical advances enabled by HaloTag technology.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Interrogating surfaceChemical science · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

12 authors at 2 institutions in 1 country.

Britta BarlagAbt. Mikrobiologie, Universität Osnabrück, Osnabrück, Germany.
Oliver BeutelAbt. Biophysik, Universität Osnabrück, Osnabrück, Germany.
Dennis JanningAbt. Neurobiologie, Universität Osnabrück, Osnabrück, Germany.
Frederik CzarniakAbt. Mikrobiologie, Universität Osnabrück, Osnabrück, Germany.
Christian P RichterAbt. Biophysik, Universität Osnabrück, Osnabrück, Germany.
Carina KommnickAbt. Mikrobiologie, Universität Osnabrück, Osnabrück, Germany.
Vera GöserAbt. Mikrobiologie, Universität Osnabrück, Osnabrück, Germany.
Rainer KurreCALMOS, Universität Osnabrück, Osnabrück, Germany.
Florian FabianiHelmholtz Centre for Infection Research, Braunschweig, Germany.
Marc ErhardtHelmholtz Centre for Infection Research, Braunschweig, Germany.
Jacob PiehlerAbt. Biophysik, Universität Osnabrück, Osnabrück, Germany.
Michael HenselAbt. Mikrobiologie, Universität Osnabrück, Osnabrück, Germany.
Osnabrück University · DEHelmholtz Centre for Infection Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The investigation of the subcellular localization, dynamics and interaction of proteins and protein complexes in prokaryotes is complicated by the small size of the cells. Super-resolution microscopy (SRM) comprise various new techniques that allow light microscopy with a resolution that can be up to ten-fold higher than conventional light microscopy. Application of SRM techniques to living prokaryotes demands the introduction of suitable fluorescent probes, usually by fusion of proteins of interest to fluorescent proteins with properties compatible to SRM. Here we describe an approach that is based on the genetically encoded self-labelling enzymes HaloTag and SNAP-tag. Proteins of interest are fused to HaloTag or SNAP-tag and cell permeable substrates can be labelled with various SRM-compatible fluorochromes. Fusions of the enzyme tags to subunits of a type I secretion system (T1SS), a T3SS, the flagellar rotor and a transcription factor were generated and analysed in living Salmonella enterica. The new approach is versatile in tagging proteins of interest in bacterial cells and allows to determine the number, relative subcellular localization and dynamics of protein complexes in living cells.

Indexed as

Bacterial ProteinsBacterial Secretion SystemsFluorescent DyesMolecular ImagingRecombinant Fusion ProteinsSalmonella entericaStaining and LabelingBacterial ProteinsBacterial Secretion SystemsFluorescent DyesRecombinant Fusion Proteins

Identifiers

PMID27534893
PMCPMC4989173
OpenAlexW2517119085

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.