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The Selenoprotein Glutathione Peroxidase 4: From Molecular Mechanisms to Novel Therapeutic Opportunities Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm PNAS Oxidant induced glutathionylation at protein disulfide bonds ScienceDirect Decoupling stability and release in disulfide bonds with antibody small molecule conjugates Chemical Science (RSC Publishing) DOI:10.1039 C6SC01831A
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The Selenoprotein Glutathione Peroxidase 4: From Molecular Mechanisms to  Novel Therapeutic Opportunities
Disulfide bond formation by exported glutaredoxin indicates glutathione's  presence in the E. coli periplasm | PNAS
Oxidant-induced glutathionylation at protein disulfide bonds - ScienceDirect
Decoupling stability and release in disulfide bonds with antibody-small  molecule conjugates - Chemical Science (RSC Publishing)  DOI:10.1039/C6SC01831A

glutathione disulfide reduction Thiol−Disulfide Exchange between Glutaredoxin and Glutathione

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