Protein Disulfide-Isomerases

Known as: Glycosylation Site Binding Protein, S-S rearrangase, Protein Disulfide-Isomerases [Chemical/Ingredient] 
A family of isomerase enzymes that reside in the endoplasmic reticulum and act as chaperones during protein folding. They catalyze the rearrangement… (More)
National Institutes of Health

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Highly Cited
2008
Highly Cited
2008
Thiol isomerases, including protein disulfide isomerase (PDI), catalyze disulfide oxidation, reduction, and isomerization… (More)
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Review
2006
Review
2006
Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease… (More)
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Highly Cited
2005
Highly Cited
2005
Protein disulfide isomerases (PDIs) are molecular chaperones that contain thioredoxin (TRX) domains and aid in the formation of… (More)
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Highly Cited
2005
Highly Cited
2005
NAD(P)H oxidase, the main source of reactive oxygen species in vascular cells, is known to be regulated by redox processes and… (More)
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Highly Cited
2001
Highly Cited
2001
Cholera toxin is assembled from two subunits in the periplasm of Vibrio cholerae and disassembled in the analogous compartment of… (More)
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Highly Cited
1999
Highly Cited
1999
Native protein disulfide bond formation in the endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p… (More)
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Review
1998
Review
1998
Prolyl 4-hydroxylases (EC 1.14,11.2) catalyze the formation of 4-hydroxyproline in collagens and other proteins with collagen… (More)
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Highly Cited
1998
Highly Cited
1998
 
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Highly Cited
1997
Highly Cited
1997
Light-regulated translation of chloroplast messenger RNAs (mRNAs) requires trans-acting factors that interact with the 5… (More)
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Highly Cited
1993
Highly Cited
1993
The transcription of genes encoding soluble proteins that reside in the endoplasmic reticulum (ER) is induced when unfolded… (More)
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