The first disulfide linkage-employing drug conjugate that exploits the reversible nature of this
unique covalent bond was recently approved for human use. Increasing numbers of drug …

Cellular mechanisms governing redox homeostasis likely involve their integration with other
stresses. Endoplasmic reticulum (ER) stress triggers complex adaptive or proapoptotic …

The prevailing view is that disulfide bonds have been added during evolution to enhance
the stability of proteins that function in a fluctuating cellular environment. However, recent …

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 isomerases (PDIs) constitute a family of structurally related enzymes which
catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins …

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly
divergent proteins that are involved in the processing and maturation of secretory proteins in …

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) derived from intravascular cells is required for thrombus
formation. However, it remains unclear whether platelet PDI contributes to the process …

Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the
oxidation, reduction and isomerization of protein disulfides. In the endoplasmic reticulum …

The catalysis of disulphide (single bondSsingle bondSsingle bond) bonds is the most
important characteristic of protein disulphide isomerase (PDI) family. Catalysis occurs in the …