Evidence map›Paper›PMID 37622897›Full record

ReviewBiosensors2023

Fluorescent Probes for Mammalian Thioredoxin Reductase: Mechanistic Analysis, Construction Strategies, and Future Perspectives.

Zilong Song, Chengwu Fan, Jintao Zhao, Lei Wang, Dongzhu Duan, Tong Shen, Xinming Li

Open access · goldAbstract readReview
In one paragraph

Review in Biosensors, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Selenium Nucleophilicity and Electrophilicity in the Intra- and Intermolecular SChemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  3. Review
  4. 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

7 authors at 3 institutions in 1 country.

Zilong SongNatural Medicine Research & Development Center, Lanzhou Jiaotong University, Lanzhou 730070, China.ORCID 0000-0003-4056-0881
Chengwu FanNatural Medicine Research & Development Center, Lanzhou Jiaotong University, Lanzhou 730070, China.
Jintao ZhaoSchool of Chemistry and Chemical Engineering, Nanjing University of Science & Technology, Nanjing 210094, China.
Lei WangNatural Medicine Research & Development Center, Lanzhou Jiaotong University, Lanzhou 730070, China.
Dongzhu DuanShaanxi Key Laboratory of Phytochemistry, College of Chemistry and Chemical Engineering, Baoji University of Arts and Sciences, Baoji 721013, China.ORCID 0000-0001-5635-819X
Tong ShenNatural Medicine Research & Development Center, Lanzhou Jiaotong University, Lanzhou 730070, China.
Xinming LiSchool of Chemistry and Chemical Engineering, Nanjing University of Science & Technology, Nanjing 210094, China.
Lanzhou Jiaotong University · CNNanjing University of Science and Technology · CNBaoji University of Arts and Sciences · CN

Funding

Natural Science Foundation of Gansu Province 22JR5RA376Young Scholars Science Foundation of Lanzhou Jiaotong University 1200061139
6 · The paper itself

Abstract

The modulation of numerous signaling pathways is orchestrated by redox regulation of cellular environments. Maintaining dynamic redox homeostasis is of utmost importance for human health, given the common occurrence of altered redox status in various pathological conditions. The cardinal component of the thioredoxin system, mammalian thioredoxin reductase (TrxR) plays a vital role in supporting various physiological functions; however, its malfunction, disrupting redox balance, is intimately associated with the pathogenesis of multiple diseases. Accordingly, the dynamic monitoring of TrxR of live organisms represents a powerful direction to facilitate the comprehensive understanding and exploration of the profound significance of redox biology in cellular processes. A number of classic assays have been developed for the determination of TrxR activity in biological samples, yet their application is constrained when exploring the real-time dynamics of TrxR activity in live organisms. Fluorescent probes offer several advantages for in situ imaging and the quantification of biological targets, such as non-destructiveness, real-time analysis, and high spatiotemporal resolution. These benefits facilitate the transition from a poise to a flux understanding of cellular targets, further advancing scientific studies in related fields. This review aims to introduce the progress in the development and application of TrxR fluorescent probes in the past years, and it mainly focuses on analyzing their reaction mechanisms, construction strategies, and potential drawbacks. Finally, this study discusses the critical challenges and issues encountered during the development of selective TrxR probes and proposes future directions for their advancement. We anticipate the comprehensive analysis of the present TrxR probes will offer some glitters of enlightenment, and we also expect that this review may shed light on the design and development of novel TrxR probes.

Indexed as

Fluorescent DyesThioredoxin-Disulfide ReductaseAnimalsBiological AssayHumansMammalsFluorescent DyesThioredoxin-Disulfide Reductase1,2-dithiolanediselenidedisulfidefluorescent proberedox chemistryselenenylsulfidethioredoxinthioredoxin reductase

Identifiers

PMID37622897
PMCPMC10452626
OpenAlexW4385812290

What OpenQuestion holds

Textmetadata
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.