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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… 
National Institutes of Health

Related topics

Related topics

26 relations
In BloodPDIA2 genePDIA3P1 genePDIA4 gene

Broader (1)

Isomerase

Narrower (8)

LQY1 protein, ArabidopsisP4hb protein, mouseP4hb protein, ratPDI-1 protein, Trypanosoma brucei

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2002
Highly Cited
2002
Structure-Based Analysis of the Herpes Simplex Virus Glycoprotein D Binding Site Present on Herpesvirus Entry Mediator HveA (HVEM)
ABSTRACT Binding of herpes simplex virus (HSV) envelope glycoprotein D (gD) to a cell surface receptor is an essential step of… 
Highly Cited
1999
Highly Cited
1999
Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase*
Protein disulfide isomerase (PDI) facilitates proper folding and disulfide bonding of nascent proteins in the endoplasmic… 
1998
1998
Molecular Evolution of the Domain Structures of Protein Disulfide Isomerases
Abstract. Protein disulfide isomerase (PDI) is an enzyme that promotes protein folding by catalyzing disulfide bridge… 
1998
1998
Targeting of endoplasmic reticulum-associated proteins to axons and dendrites in rotavirus-infected neurons
Highly Cited
1995
Highly Cited
1995
Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase.
The mechanism of action of the bacterial periplasm protein DsbA in introducing disulfide bonds into proteins was studied by its… 
Highly Cited
1995
Highly Cited
1995
Constitutive Overexpression of Secreted Heterologous Proteins Decreases Extractable BiP and Protein Disulfide Isomerase Levels in Saccharomyces cerevisiae
High‐level gene expression does not always lead to corresponding high‐level secretion of heterologous proteins in yeast. The rate… 
1994
1994
Protein folding activities of Escherichia coli protein disulfide isomerase.
DsbA is an Escherichia coli periplasmic protein that mediates disulfide bond formation in newly secreted proteins in vivo… 
Highly Cited
1994
Highly Cited
1994
Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum.
Highly Cited
1992
Highly Cited
1992
Protein disulfide isomerase activity is released by activated platelets
The release of protein disulfide isomerase by activated platelets was hypothesized on the basis of reported intermolecular and… 
Highly Cited
1988
Highly Cited
1988
Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER
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