Evidence map›Paper›PMID 33959634›Full record

ArticleFrontiers in molecular biosciences2021

Enhanced UnaG With Minimal Labeling Artifact for Single-Molecule Localization Microscopy.

Sangyoon Ko, Jiwoong Kwon, Sang-Hee Shim

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

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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

5 citing papers in PubMed.

  1. bioRxiv : the preprint server for biology · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Editorial: Mechanisms of Fluorescent Proteins.Frontiers in molecular biosciences · 2021
    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

3 authors.

Sangyoon KoCenter for Molecular Spectroscopy and Dynamics, Institute of Basic Science, Seoul, South Korea.
Jiwoong KwonCenter for Molecular Spectroscopy and Dynamics, Institute of Basic Science, Seoul, South Korea.
Sang-Hee ShimCenter for Molecular Spectroscopy and Dynamics, Institute of Basic Science, Seoul, South Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We introduced enhanced UnaG (eUnaG), a ligand-activatable fluorescent protein, for conventional and super-resolution imaging of subcellular structures in the mammalian cells. eUnaG is a V2L mutant of UnaG with twice brighter bulk fluorescence. We previously discovered the reversible fluorescence switching behavior of UnaG and demonstrated the high photon outputs and high localization numbers in single-molecule localization microscopy (SMLM). In this study, we showed that the fluorescence of eUnaG can be switched off under blue-light illumination, while a high concentration of fluorogenic ligands in the buffer can efficiently restore the fluorescence, as in UnaG. We demonstrated the capacity of eUnaG as an efficient protein label in mammalian cells, as well as for SMLM by utilizing its photoswitchable nature. While cytosolic UnaG proteins showed aggregated patches and fluorescence reduction at high expression levels, eUnaG-labeled protein targets successfully formed their proper structures in mammalian cells without notable distortion from the endogenous structure in the majority of transiently expressing cells. In particular, eUnaG preserved the vimentin filament structures much better than the UnaG. eUnaG provided similarly high single-molecule photon count distribution to UnaG, thus also similarly high resolution in the super-resolution images of various subcellular structures. The sampling coverage analysis of vimentin filaments in SMLM images showed the improvement of labeling efficiency of eUnaG. eUnaG is a high-performance fluorescent protein for fluorescence and single-molecule localization imaging in green emission with minimal labeling artifact.

Indexed as

bilirubinfluorescent proteinphotoswitchingsingle-molecule localization microscopysuper-resolution (SR) imagingUnaG

Identifiers

PMID33959634
PMCPMC8093618

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