Oxidative damage can have a devastating effect on the structure and activity of proteins, and
may even lead to cell death. The sulfur-containing amino acids cysteine and methionine are …

Reactive oxygen, nitrogen, and sulfur species, referred to as ROS, RNS, and RSS,
respectively, are produced during normal cell function and in response to various stimuli. An …

Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent
bonds on the backbones or amino acid side chains of proteins and expand the diversity of …

Disulfide bonds between cysteine residues are important post-translational modifications in
proteins that have critical roles for protein structure and stability, as redox-active catalytic …

Cysteine sulfinic acid or S-sulfinylation is an oxidative post-translational modification
(OxiPTM) that is known to be involved in redox-dependent regulation of protein function but …

Background Reactive oxygen species-mediated cysteine sulfenic acid modification has
emerged as an important regulatory mechanism in cell signaling. The stability of sulfenic …

Protein sulfenylation is a post-translational modification of emerging importance in higher
eukaryotes. However, investigation of its diverse roles remains challenging, particularly …

Abstract Thioredoxins (Trx) and glutaredoxins (Grx) constitute families of thiol
oxidoreductases. Our knowledge of Trx and Grx in plants has dramatically increased during …

Protein oxidative modifications, also known as protein oxidation, are a major class of protein
posttranslational modifications. They are caused by reactions between protein amino acid …

Thioredoxins are ubiquitous antioxidant enzymes that play important roles in many health-
related cellular processes. As such, the fundamental knowledge of how these enzymes work …