Thiol proteins may potentially act as redox signaling adaptor proteins, adjusting reactive
oxygen species intermediates to specific signals and redox signals to cell homeostasis. In …

Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox
proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide …

Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin
superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in …

Significance: Protein disulfide isomerase (PDI) and its homologs have essential roles in the
oxidative folding and chaperone-mediated quality control of proteins in the secretory …

Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

Vascular cell NADPH oxidase complexes are key sources of signaling reactive oxygen
species (ROS) and contribute to disease pathophysiology. However, mechanisms that fine …

Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase
(PDI) and its homologs, which contain varying combinations of catalytically active and …

The endoplasmic reticulum (ER) is an essential cellular compartment in which an enormous
number of secretory and cell surface membrane proteins are synthesized and subjected to …

Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We
showed previously that vascular and macrophage oxidase complexes are regulated by the …

Thiol-disulfide oxidoreductases of the human protein disulfide isomerase (PDI) family
promote protein folding in the endoplasmic reticulum (ER), while also assisting the …