1.8.4.2 2 glutathione + COX2-disulfide - 1.8.4.2 2 glutathione + pilin FimA-disulfide - 1.8.4.2 2 glutathione + protein AtlS-disulfide - 1.8.4.2 2 glutathione + protein-disulfide - 1.8.4.2 2 glutathione + SCO1-disulfide - 1.8.4.2 2 glutathione + SCO2-disulfide - 1.8.4.2 GSH + AtlS - 1.8.4.2 GSH + protein disulfide - 1.8.4.2 GSH + protein disulfide physiological function 1.8.4.2 GSH + protein disulfide reductive degradation and assembly of proteins 1.8.4.2 GSH + protein disulfide modulation of enzymatic activity from latent to active form and vice versa 1.8.4.2 GSH + protein disulfide major contributor to the inactivation of oxytoxin by lactating mammary gland 1.8.4.2 GSH + protein disulfide enzyme not directly involved in the subcellular processing of receptor-bound internalized insulin 1.8.4.2 GSH + protein disulfide feedback control via insulin in the liver 1.8.4.2 GSH + protein disulfide synthesis of protein disulfide bond 1.8.4.2 GSH + protein disulfide disulfide bonding step in folding pathway of many periplasmic and outer membrane proteins with structural disulfide bonds 1.8.4.2 GSH + protein disulfide initial step in sequential insulin degradation 1.8.4.2 GSH + protein disulfide enzyme plays a role in formation of intramonomer bonds common to all immunoglobulin molecules 1.8.4.2 GSH + protein-disulfide - 1.8.4.2 additional information bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery 1.8.4.2 additional information ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the the reduction of the cysteinyls in the heme binding site of apocytochrome c 1.8.4.2 additional information StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis 1.8.4.2 additional information the enzyme is required for efficient disulfide bond formation in the periplasm 1.8.4.2 additional information COA6 interacts with COX2 and SCO proteins in vivo 1.8.4.2 SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues -