Evidence map›Paper›PMID 31937765›Full record

ArticleNature communications2020

Bright ligand-activatable fluorescent protein for high-quality multicolor live-cell super-resolution microscopy.

Jiwoong Kwon, Jong-Seok Park, Minsu Kang, Soobin Choi, Jumi Park, Gyeong Tae Kim, Changwook Lee, Sangwon Cha, Hyun-Woo Rhee, Sang-Hee Shim

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Review
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  6. Microbial single-cell applications under anoxic conditions.Applied and environmental microbiology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Bleaching-Resistant Super-Resolution Fluorescence Microscopy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Transient Fluorescence Labeling: Low Affinity-High Benefits.International journal of molecular sciences · 2021
    Review
  20. Review
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

10 authors.

Jiwoong KwonCenter for Molecular Spectroscopy and Dynamics, Institute for Basic Science (IBS), Seoul, 02841, Republic of Korea.ORCID http://orcid.org/0000-0003-4761-2517
Jong-Seok ParkDepartment of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.
Minsu KangCenter for Molecular Spectroscopy and Dynamics, Institute for Basic Science (IBS), Seoul, 02841, Republic of Korea.
Soobin ChoiDepartment of Chemistry, Hankuk University of Foreign Studies, Yongin, 17035, Republic of Korea.
Jumi ParkDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.
Gyeong Tae KimDepartment of Biomedical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.ORCID http://orcid.org/0000-0002-0981-3214
Changwook LeeDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.
Sangwon ChaDepartment of Chemistry, Hankuk University of Foreign Studies, Yongin, 17035, Republic of Korea.ORCID http://orcid.org/0000-0003-2819-3417
Hyun-Woo RheeDepartment of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea. rheehw@snu.ac.kr.
Sang-Hee ShimCenter for Molecular Spectroscopy and Dynamics, Institute for Basic Science (IBS), Seoul, 02841, Republic of Korea. sangheeshim@korea.ac.kr.ORCID http://orcid.org/0000-0001-9964-7231

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We introduce UnaG as a green-to-dark photoswitching fluorescent protein capable of high-quality super-resolution imaging with photon numbers equivalent to the brightest photoswitchable red protein. UnaG only fluoresces upon binding of a fluorogenic metabolite, bilirubin, enabling UV-free reversible photoswitching with easily controllable kinetics and low background under Epi illumination. The on- and off-switching rates are controlled by the concentration of the ligand and the excitation light intensity, respectively, where the dissolved oxygen also promotes the off-switching. The photo-oxidation reaction mechanism of bilirubin in UnaG suggests that the lack of ligand-protein covalent bond allows the oxidized ligand to detach from the protein, emptying the binding cavity for rebinding to a fresh ligand molecule. We demonstrate super-resolution single-molecule localization imaging of various subcellular structures genetically encoded with UnaG, which enables facile labeling and simultaneous multicolor imaging of live cells. UnaG has the promise of becoming a default protein for high-performance super-resolution imaging.

Indexed as

BilirubinFluorescenceGreen Fluorescent ProteinsKineticsLigandsLightMicroscopy, FluorescencePhotochemical ProcessesProtein BindingSingle Molecule ImagingBilirubinGreen Fluorescent ProteinsLigands

Identifiers

PMID31937765
PMCPMC6959352

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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.