The collagen superfamily of proteins now contains at least 19 proteins formally defined as
collagens and an additional ten proteins that have collagen-like domains. The most …

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 …

During the maturation of extracellular proteins, disulfide bonds that chemically cross-link
specific cysteines are often added to stabilize a protein or to join it covalently to other …

Carbonic anhydrases (CAs I-VII) are products of a gene family that encodes seven isozymes
and several homologous, CA-related proteins. All seven isozymes have been cloned …

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 …

Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded
proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond …

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 …

Protein disulfide isomerase (PDI) is a very efficient catalyst of folding of many disulfide‐
bonded proteins. A great deal is known about the catalytic functions of PDI, while little is …

The cell surface of mammalian cells is capable of reductively cleaving disulfide bonds of
exogenous membrane-bound macromolecules (for instance, the interchain disulfide of …