Reversible oxidation of cysteine residues within proteins occurs naturally during normal
cellular homeostasis and can increase during oxidative stress. Cysteine oxidation often …

Bacteria possess the ability to adapt to changing environments. To enable this, cells use
reversible post-translational modifications on key proteins to modulate their behavior …

Melatonin is a ubiquitous indolamine that plays important roles in various aspects of
biological processes in mammals. In Saccharomyces cerevisiae, melatonin has been …

The yeast peroxiredoxin Ahp1, like related anti-oxidant enzymes in other species,
undergoes urmylation, a lysine-directed conjugation to ubiquitin-like modifier Urm1. Ahp1 …

Malaria remains a major global health problem, creating a constant need for research to
identify druggable weaknesses in P. falciparum biology. As important components of cellular …

Protein disulfide isomerase, containing thioredoxin (Trx) domains, serves as a vital enzyme
responsible for oxidative protein folding (the formation, reduction, and isomerization of …

Peroxiredoxins, a highly conserved family of thiol oxidoreductases, play a key role in oxidant
detoxification by partnering with the thioredoxin system to protect against oxidative stress. In …

Protein disulfide isomerases (PDIs) function in forming the correct disulfide bonds in client
proteins, thereby aiding the folding of proteins that enter the secretory pathway. Recently …

To prevent the accumulation of reactive oxygen species and limit associated damage to
biological macromolecules, cells express a variety of oxidant-detoxifying enzymes, including …

Identifying direct substrates of enzymes has been a long-term challenge. Here, we present a
strategy using live cell chemical cross-linking and mass spectrometry to identify the putative …