Evidence map›Paper›PMID 21782895›Full record

ReviewBiochimica et biophysica acta2011

Thioredoxin glutathione reductase: its role in redox biology and potential as a target for drugs against neglected diseases.

Stefanie Prast-Nielsen, Hsin-Hung Huang, David L Williams

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 75 citations in OpenAlex.

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  16. Chemical Biology of HChemical reviews · 2018
    Review
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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 at 2 institutions in 2 countries.

Stefanie Prast-NielsenDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm SE-17177, Sweden. stefanie.prast-nielsen@ki.se
Hsin-Hung Huang
David L Williams
Rush University Medical Center · USKarolinska Institutet · SE

Funding

Redox Balance & Drug Development in Schistosoma mansoniR01AI065622 · NIAID · RUSH UNIVERSITY MEDICAL CENTER · PI WILLIAMS, DAVID LEE · 2007 to 2011
$1.4M
NIAID NIH HHS AI065622NIAID NIH HHS R01 AI065622
6 · The paper itself

Abstract

backgroundThere are two, largely autonomous antioxidant pathways in many organisms, one based on thioredoxin and one based on glutathione, with each pathway having a unique flavoprotein oxidoreductase to maintain them in a reduced state. A recently discovered protein, thioredoxin glutathione reductase (TGR) potentially connects these two pathways. In a large group of parasitic worms, responsible for hundreds of millions of infections in humans and animals, untold morbidity and significant mortality, TGR is the sole enzyme present to maintain redox balance. SCOPE OF REVIEW: In this review, the current understanding of the biochemical properties of TGR enzymes is compared to the related enzymes thioredoxin reductase and glutathione reductase. The role of the rare amino acid selenocysteine is discussed. An overview of the potential to target TGR for drug development against a range of parasitic worms and preliminary results to identify TGR inhibitors for schistosomiasis treatment is presented. MAJOR

conclusionsTGR has properties that are both unique and common to other flavoprotein oxidoreductases. TGR plays a fundamentally different and essential role in the redox biology of parasitic flatworms. Therefore, TGR is a promising target for drug development for schistosomiasis and other trematode and cestode infections. GENERAL SIGNIFICANCE: TGR may have differing functions in host organisms, but through analyses to understand its ability to reduce both glutathione and thioredoxin we can better understand the reaction mechanisms of an important class of enzymes. The unique properties of TGR in parasitic flatworms provide promising routes to develop new treatments for diseases.

Indexed as

AnimalsHumansMultienzyme ComplexesNADH, NADPH OxidoreductasesOxidation-ReductionMultienzyme ComplexesNADH, NADPH Oxidoreductasesthioredoxin glutathione reductase

Identifiers

PMID21782895
PMCPMC3210934
OpenAlexW1968796392

What OpenQuestion holds

Textmetadata
LicenceTDM
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.