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

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Protein Disulfide-Isomerases

Papers overview

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2007
2007
Limited tolerance towards folded elements during secretion of the autotransporter Hbp.
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
S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
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
Oxidative stress and redox regulation of lung inflammation in COPD.
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
Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption.
S-nitrosothiols (RSNOs) regulate several aspects of platelet physiology including inhibition of activation, adhesion and… (More)
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Review
2002
Review
2002
Regulation of inducible peroxide stress responses.
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
Defining the disulphide stress response in Streptomyces coelicolor A3(2): identification of the sigmaR regulon.
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
Pathways for protein disulphide bond formation.
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
Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
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
Crystal structure of the DsbA protein required for disulphide bond formation in vivo
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
Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
BEING topologically equivalent to the extracellular space, the lumen of the endoplasmic reticulum (ER) provides a unique folding… (More)
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