Skip to search formSkip to main contentSkip to account menu

Thioredoxin Reductase (NADPH)

Known as: NADP Thioredoxin Reductase, Thioredoxin Reductase, Reductase, NADP-Thioredoxin 
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1… 
National Institutes of Health

Related topics

Related topics

10 relations

Narrower (3)

ANTR-C protein, ArabidopsisNTRA protein, ArabidopsisNTRC protein, Arabidopsis
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2009
Highly Cited
2009
Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase*
Ribonucleotide reductase (RNR) catalyzes the rate-limiting step in deoxyribonucleotide synthesis essential for DNA replication… 
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… 
Highly Cited
2008
Highly Cited
2008
Cell Death by SecTRAPs: Thioredoxin Reductase as a Prooxidant Killer of Cells
Background SecTRAPs (selenium compromised thioredoxin reductase-derived apoptotic proteins) can be formed from the selenoprotein… 
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… 
Highly Cited
2001
Highly Cited
2001
The biochemistry of selenium and the glutathione system.
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
2000
Highly Cited
2000
Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH.
A procedure for detecting proteins that contain H(2)O(2)-sensitive cysteine (or selenocysteine) residues was developed as a means… 
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
1996
Highly Cited
1996
Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.
The possible relationship of selenium to immunological function which has been suggested for decades was investigated in studies… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)