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Sulfiredoxin-1 (SRXN1) is an evolutionarily conserved redox-regulatory enzyme that plays a central role in restoring the activity of antioxidant proteins, particularly 2-Cys peroxiredoxins, under oxidative stress. It catalyzes the ATP-dependent reduction of cysteine sulfinic acid in peroxiredoxins, regenerating their peroxidase activity and maintaining cellular redox homeostasis. SRXN1 participates in deglutathionylation reactions, further contributing to the regulation of redox-mediated signaling. Its aberrant expression has been linked to cancer progression, therapeutic resistance, and poor prognosis, making it both a biomarker and a potential therapeutic target, especially in contexts of redox imbalance.
Drugs targeting SRXN1 would potentially act as enzyme inhibitors to block the reduction/regeneration of hyperoxidized peroxiredoxins, leading to enhanced oxidative stress and potential sensitization of cancer cells to therapy
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