The disulfide linkage between glutathione and protein is reversible, through the action of thiol-disulfide oxidoreductases. Glutathionylation substantially alters the functionality of enzymes ...

glutathionylation, and glycosylation) at the single-molecule level for protein chains over 1,200 residues long. These included modifications deep within the protein's sequence. Importantly ...

glutathionylation, and glycosylation). These included modifications deep within the protein’s sequence. Importantly, the method does not require the use of labels, enzymes, or additional reagents.

This realization has placed made glutaredoxin a focal point in advancing understanding of protein-S-glutathionylation as a regulatory mechanism akin to phosphorylation of proteins. We are employing a ...

This realization has placed made glutaredoxin a focal point in advancing understanding of protein-S-glutathionylation as a regulatory mechanism akin to phosphorylation of proteins. We are employing a ...

James Chun Yip Chan and colleagues at the National University of Singapore examined glutathionylation, a post-translational modification made to cysteine residues, in response to acetaminophen ...