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Protein-methionine-S-oxide reductase

Known as: methionine sulfoxide reductase, peptide methionine sulfoxide reductase 
 
National Institutes of Health

Papers overview

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Review
2003
Review
2003
Most reactive oxygen species (ROS) can oxidize methionine (Met) residues of proteins to methionine sulfoxide (MetO). However… Expand
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Highly Cited
2002
Highly Cited
2002
Selenoprotein R (SelR) is a mammalian selenocysteine-containing protein with no known function. Here we report that cysteine… Expand
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Highly Cited
2002
Highly Cited
2002
Many organisms have been shown to possess a methionine sulfoxide reductase (MsrA), exhibiting high specificity for reduction the… Expand
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Highly Cited
2001
Highly Cited
2001
Oxidation of proteins by reactive oxygen species is associated with aging, oxidative stress, and many diseases. Although free and… Expand
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Highly Cited
2001
Highly Cited
2001
Oxidation of methionine residues to methionine sulfoxide can lead to inactivation of proteins. Methionine sulfoxide reductase… Expand
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Highly Cited
2001
Highly Cited
2001
Mycoplasma genitalium is the smallest self-replicating microorganism and is implicated in human diseases, including urogenital… Expand
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Highly Cited
1999
Highly Cited
1999
Previous studies have shown that the pathophysiology of Alzheimer's disease (AD) is linked to oxidative stress. Oxidative damage… Expand
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Highly Cited
1999
Highly Cited
1999
We have investigated the ability of methionine sulfoxide reductase (MsrA) to maintain optimal calmodulin (CaM) function through… Expand
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Highly Cited
1998
Highly Cited
1998
The yeast peptide-methionine sulfoxide reductase (MsrA) was overexpressed in a Saccharomyces cerevisiae null mutant of msrA by… Expand
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Highly Cited
1997
Highly Cited
1997
A gene homologous to methionine sulfoxide reductase (msrA) was identified as the predicted ORF (cosmid 9379) in chromosome V of… Expand
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