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Thioredoxins

Known as: Thioredoxin, Thioredoxins [Chemical/Ingredient] 
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS… 
National Institutes of Health

Related topics

Related topics

24 relations
In BloodProcess of secretionProtein Disulfide-IsomerasesTXN gene

Narrower (12)

NrdH protein, E ColiTXN protein, humanThioredoxinThioredoxin 1

Broader (1)

redoxin

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
Inhibition of the Human Thioredoxin System
Mercury toxicity mediated by different forms of mercury is a major health problem; however, the molecular mechanisms underlying… 
Review
2006
Review
2006
Plant thioredoxins are key actors in the oxidative stress response.
Highly Cited
2005
Highly Cited
2005
Measurement of Thioredoxin and Thioredoxin Reductase
The thioredoxin system is ubiquitous, providing reducing equivalents to essential biosynthetic enzymes like ribonucleotide… 
Highly Cited
2002
Highly Cited
2002
Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant
Ebselen [2-phenyl-1,2-benzisoselenazol-3(2H)-one], a seleno-organic compound with glutathione peroxidase-like activity is used in… 
Review
2002
Review
2002
Redox control of cell death.
Cellular redox is controlled by the thioredoxin (Trx) and glutathione (GSH) systems that scavenge harmful intracellular reactive… 
Highly Cited
2001
Highly Cited
2001
The S-locus receptor kinase is inhibited by thioredoxins and activated by pollen coat proteins
The self-incompatibility response in Brassica allows recognition and rejection of self-pollen by the stigmatic papillae. The… 
Review
2000
Review
2000
Thioredoxin reductase two modes of catalysis have evolved.
Thioredoxin reductase (EC 1.6.4.5) is a widely distributed flavoprotein that catalyzes the NADPH-dependent reduction of… 
Highly Cited
1998
Highly Cited
1998
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins
Cytoplasmic proteins do not generally contain structural disulfide bonds, although certain cytoplasmic enzymes form such bonds as… 
Highly Cited
1996
Highly Cited
1996
A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.
We report the isolation and characterization of a new selenoprotein from a human lung adenocarcinoma cell line, NCI-H441. Cells… 
Highly Cited
1994
Highly Cited
1994
Thioredoxin-dependent peroxide reductase from yeast.
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