Cysteine residues in proteins are subject to diverse redox chemistry. Oxidation of cysteine to
S-nitrosocysteine, cysteine sulfenic and sulfinic acids, disulfides and persulfides are a few …

Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows
cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide …

By nature of the reversibility of the addition of glutathione to low pKa cysteine residues, the
post-translational modification of S-glutathionylation sanctions a cycle that can create a …

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 …

Glutathione (GSH) is the major non-protein thiol in humans and other mammals, which is
present in millimolar concentrations within cells, but at much lower concentrations in the …

Significance: Redox homeostasis consists of an intricate network of reactions in which
reactive molecular species, redox modifications, and redox proteins act in concert to allow …

Background The poultry industry is a growing livestock sector, which generates large
volumes of by-products with negative environmental impacts that must be revalorized …

Protein S-glutathionylation serves a regulatory role in proteins and modulates distinct
biological processes implicated in health and diseases. Despite challenges in analyzing the …

Comprehensive analysis of the post-translational modifications (PTMs) on proteins at
proteome level is crucial to elucidate the regulatory mechanisms of various biological …

In recent decades, peptides as potential drugs were more and more explored with the
development of non-oral medicine. There into, sulfur-containing peptide is one of the most …