The endoplasmic reticulum (ER) is a fascinating network of tubules through which secretory
and transmembrane proteins enter unfolded and exit as either folded or misfolded proteins …

The cysteine (Cys) proteome is a major component of the adaptive interface between the
genome and the exposome. The thiol moiety of Cys undergoes a range of biologic …

Effector mechanisms of the unfolded protein response (UPR) in the endoplasmic reticulum
(ER) are well-characterised, but how ER proteostasis is sensed is less well understood …

Cysteine thiols are among the most reactive functional groups in proteins, and their pairing
in disulfide linkages is a common post-translational modification in proteins entering the …

Highlights•PDI is an important oxidase, reductase, isomerase and molecular
chaperone.•PDI expression is up-regulated in select types of cancers.•Silencing PDI results …

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

In eukaryotic cells, oxidative protein folding occurs in the lumen of the endoplasmic
reticulum (ER), catalyzed by ER sulfhydryl oxidase 1 (Ero1) and protein disulfide isomerase …

Free radicals originate from both exogenous environmental sources and as by-products of
the respiratory chain and cellular oxygen metabolism. Sustained accumulation of free …

The protein disulphide isomerase (PDI) gene family is a large, diverse group of enzymes
recognised for their roles in disulphide bond formation within the endoplasmic reticulum …

Protein disulfide–isomerase (PDI) was the first protein-folding catalyst to be characterized,
half a century ago. It plays critical roles in a variety of physiological events by displaying …