This review provides a comprehensive overview of the functional roles of disulfide bonds
and their relevance to human disease. The critical roles of disulfide bonds in protein …

Protein action in nature is largely controlled by the level of expression and by post-
translational modifications. Post-translational modifications result in a proteome that is at …

The mechanism of activation of transglutaminase 2 (TG2) in the extracellular matrix remains
a fundamental mystery in our understanding of the biology of this multifunctional mammalian …

Protein disulfide bonds link pairs of cysteine residues in polypeptide chains. Many of these
bonds serve a purely structural or energetic role, but a growing subset of cleavable disulfide …

Cells constantly face the challenge of managing oxidants. In aerobic organisms, oxygen
(O2) is used for energy production, generating reactive oxygen species (ROS) as byproducts …

Disulfide Bonds in Protein Folding and Stability | Oxidative Folding of Proteins: Basic
Principles, Cellular Regulation and Engineering | Books Gateway | Royal Society of Chemistry …

Cysteine residues in cytosolic proteins are maintained in their reduced state, but can
undergo oxidation owing to posttranslational modification during redox signaling or under …

Transglutaminase 2 (TG2) catalyzes transamidation or deamidation of its substrates and is
ordinarily maintained in a catalytically inactive state in the intestine and other organs …

Whereas the role of mammalian thioredoxin (Trx) as an intracellular protein cofactor is
widely appreciated, its function in the extracellular environment is not well-understood. Only …

During the last decades, Raman spectroscopy has been routinely used for probing the
conformational features of disulfide linkages in peptides and proteins. However, the …