protein disulfide isomerase activity

Known as: disulphide bond formation, protein thiol-disulphide exchange, protein thiol-disulfide exchange 
Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins. [EC:5.3.4.1, GOC:vw, http://en.wikipedia.org/wiki… (More)
National Institutes of Health

Papers overview

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2007
2007
Many virulence factors secreted by pathogenic Gram-negative bacteria belong to the autotransporter (AT) family. ATs consist of a… (More)
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Highly Cited
2006
Highly Cited
2006
Stress proteins located in the cytosol or endoplasmic reticulum (ER) maintain cell homeostasis and afford tolerance to severe… (More)
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Review
2006
Review
2006
Reactive oxygen species, either directly or via the formation of lipid peroxidation products, may play a role in enhancing… (More)
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2004
2004
S-nitrosothiols (RSNOs) regulate several aspects of platelet physiology including inhibition of activation, adhesion and… (More)
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Review
2002
Review
2002
Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and… (More)
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Highly Cited
2001
Highly Cited
2001
In the Gram-positive, antibiotic-producing bacterium Streptomyces coelicolor A3(2), the thiol-disulphide status of the hyphae is… (More)
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Review
2000
Review
2000
The folding of many secretory proteins depends upon the formation of disulphide bonds. Recent advances in genetics and cell… (More)
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1993
1993
PROTEIN disulphide isomerase (PDI)1,2 is a highly abundant and ubiquitous eukaryotic protein that is essential for viability in… (More)
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Highly Cited
1993
Highly Cited
1993
PROTEINS that contain disulphide bonds are often slow to fold in vitro because the oxidation and correct pairing of the cysteine… (More)
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Highly Cited
1992
Highly Cited
1992
BEING topologically equivalent to the extracellular space, the lumen of the endoplasmic reticulum (ER) provides a unique folding… (More)
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