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glutaredoxin

Known as: Glutaredoxins, Glutaredoxins [Chemical/Ingredient], Thioltransferase 
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced… Expand
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2019
Review
2019
The tripeptide glutathione (GSH) and its oxidized form glutathione disulfide (GSSG) constitute a key redox couple in cells. In… Expand
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Review
2018
Review
2018
Abstract Over the last decade, a dual character of cell response to oxidative stress, eustress versus distress, has become… Expand
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Review
2017
Review
2017
This review provides a comprehensive overview of the functional roles of disulfide bonds and their relevance to human disease… Expand
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Review
2004
Review
2004
Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the reducing power of glutathione to… Expand
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Highly Cited
2002
Highly Cited
2002
Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative… Expand
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Review
2000
Review
2000
  • A. Holmgren
  • Antioxidants & redox signaling
  • 2000
  • Corpus ID: 23329523
Selenium is an essential trace element with known antioxidant properties. Cytosolic thioredoxin reductase from mammalian cells is… Expand
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Highly Cited
1997
Highly Cited
1997
In Escherichia coli, two pathways use NADPH to reduce disulfide bonds that form in some cytoplasmic enzymes during catalysis: the… Expand
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Highly Cited
1994
Highly Cited
1994
Human plasma glutathione peroxidase (GSH-Px) is a distinct extracellular selenoenzyme that detoxifies hydroperoxides when used… Expand
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Highly Cited
1990
Highly Cited
1990
Homogeneous native and recombinant porcine liver thioltransferase (glutaredoxin), bovine thymus and human placenta… Expand
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Review
1989
Review
1989
  • A. Holmgren
  • The Journal of biological chemistry
  • 1989
  • Corpus ID: 23356953
 
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