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… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1975-2017
010203019752017

Papers overview

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Highly Cited
2010
Highly Cited
2010
Iron is an essential nutrient for cells. It is unknown how iron, after its import into the cytosol, is specifically delivered to… (More)
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Highly Cited
2007
Highly Cited
2007
Salicylic acid (SA) is a plant signaling molecule that mediates the induction of defense responses upon attack by a variety of… (More)
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Highly Cited
2006
Highly Cited
2006
The transcription factors Aft1 and Aft2 from Saccharomyces cerevisiae regulate the expression of genes involved in iron… (More)
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Highly Cited
2004
Highly Cited
2004
Glutaredoxins catalyze glutathione-dependent thiol disulfide oxidoreductions via a GSH-binding site and active cysteines… (More)
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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… (More)
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Highly Cited
2001
Highly Cited
2001
Glutaredoxin (Grx) is a glutathione-dependent hydrogen donor for ribonucleotide reductase. Today glutaredoxins are known as a… (More)
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Highly Cited
1999
Highly Cited
1999
Glutaredoxins are members of a superfamily of thiol disulfide oxidoreductases involved in maintaining the redox state of target… (More)
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Highly Cited
1998
Highly Cited
1998
The practical exploitation of the vast numbers of sequences in the genome sequence databases is crucially dependent on the… (More)
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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… (More)
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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… (More)
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