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Discovering mechanisms of signaling-mediated cysteine oxidation.
Cysteine pK(a) values for the bacterial peroxiredoxin AhpC.
Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.
Endosomal H2O2 production leads to localized cysteine sulfenic acid formation on proteins during lysophosphatidic acid-mediated cell signaling.
Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC.
Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.
Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.
Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins.
H2O2 oxidation of cysteine residues in c-Jun N-terminal kinase 2 (JNK2) contributes to redox regulation in human articular chondrocytes.
Differential peroxiredoxin hyperoxidation regulates MAP kinase signaling in human articular chondrocytes.