Evidence map›Paper›PMID 31227705›Full record

ArticleNature communications2019

A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage.

Xinming Li, Baoxin Zhang, Chaoxian Yan, Jin Li, Song Wang, Xiangxu Wei, Xiaoyan Jiang, Panpan Zhou, Jianguo Fang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
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  6. Review
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  8. Article
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  10. Article
  11. Review
  12. Recent Progress on NIR Fluorescent Probes for Enzymes.Molecules (Basel, Switzerland) · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Onopordopicrin from the new genusJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  19. Review
  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

9 authors at 1 institution in 1 country.

Xinming LiState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Baoxin ZhangState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Chaoxian YanState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Jin LiState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Song WangState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Xiangxu WeiState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Xiaoyan JiangState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Panpan ZhouState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
Jianguo FangState Key Laboratory of Applied Organic Chemistry & College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China. fangjg@lzu.edu.cn.ORCID http://orcid.org/0000-0002-2884-3363
Lanzhou University · CN

Funding

National Science Foundation of China | National Natural Science Foundation of China-Yunnan Joint Fund (NSFC-Yunnan Joint Fund) 21572093National Science Foundation of China | National Natural Science Foundation of China-Yunnan Joint Fund (NSFC-Yunnan Joint Fund) 21778028
6 · The paper itself

Abstract

Small molecule probes are indispensable tools to explore diverse cellular events. However, finding a specific probe of a target remains a high challenge. Here we report the discovery of Fast-TRFS, a specific and superfast fluorogenic probe of mammalian thioredoxin reductase, a ubiquitous enzyme involved in regulation of diverse cellular redox signaling pathways. By systematically examining the processes of fluorophore release and reduction of cyclic disulfides/diselenides by the enzyme, structural factors that determine the response rate and specificity of the probe are disclosed. Mechanistic studies reveal that the fluorescence signal is switched on by a simple reduction of the disulfide bond within the probe, which is in stark contrast to the sensing mechanism of published probes. The favorable properties of Fast-TRFS enable development of a high-throughput screening assay to discover inhibitors of thioredoxin reductase by using crude tissue extracts as a source of the enzyme.

Indexed as

AnimalsBiological ProductsComplex MixturesDisulfidesDrug DiscoveryFluorescent DyesHeLa CellsHigh-Throughput Screening AssaysHumansIntravital MicroscopyMicroscopy, FluorescenceMolecular ImagingMolecular ProbesOxidation-ReductionRecombinant ProteinsRNA, Small InterferingBiological ProductsComplex MixturesDisulfidesFluorescent DyesMolecular ProbesRecombinant ProteinsRNA, Small InterferingThioredoxin Reductase 1Txnrd1 protein, rat

Identifiers

PMID31227705
PMCPMC6588570
OpenAlexW2951781521

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.