Human thioredoxin reductase (TrxR) is a selenoprotein with a central role in cellular redox
homeostasis, utilizing a highly reactive and solvent-exposed selenocysteine (Sec) residue in …

Significance: The dual-specificity phosphatases (DUSPs) constitute a heterogeneous group
of cysteine-based protein tyrosine phosphatases, whose members exert a pivotal role in cell …

Irreversible oxidation of Cys residues to sulfinic/sulfonic forms typically impairs protein
function. We found that persulfidation (CysSSH) protects Cys from irreversible oxidative loss …

Abstract TXNL1 (also named TRP32, for thioredoxin related protein of 32 kDa) is a cytosolic
thioredoxin-fold protein expressed in all cell types and conserved from yeast to mammals …

The human Phosphatase of Regenerative Liver (PRL) family comprises three members
(PRL‐1,‐2,‐3; gene name PTP 4A1, PTP 4A2, PTP 4A3) that are highly expressed in a …

S-nitrosylation of proteins occurs as a consequence of the derivatization of cysteine thiols
with nitric oxide (NO) and is often associated with diseases and protein malfunction …

H 2 O 2 can cause oxidative damage associated with age-related diseases such as diabetes
and cancer but is also used to initiate diverse responses, including increased antioxidant …

Significance: Redox-regulated control of protein tyrosine phosphatases (PTPs) through
inhibitory reversible oxidation of their active site is emerging as a novel and general …

Introduction: Phosphatases of regenerating livers (PRLs) are novel oncogenes that interact
with many well-established cell signaling pathways that are misregulated in cancer, and are …

Similar to other intracellular pathogens, Leishmania parasites are known to evade the
antimicrobial effector functions of host immune cells. To date, however, only a few virulence …