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Reactive oxygen species (ROS)-related oxidative stress proteins represent a broad functional class of molecules involved in the production, regulation, and detoxification of reactive oxygen and nitrogen species (NIH, 2024). This group includes pro-oxidant enzymes such as NADPH oxidases (NOX) and xanthine oxidase, as well as a sophisticated antioxidant defense network comprising enzymes like superoxide dismutase (SOD), catalase, and glutathione peroxidase (GPx) (MDPI, 2023). These proteins play a dual role in cellular physiology: at low levels, ROS act as essential signaling molecules for cell growth and immune activation, while excessive ROS levels lead to oxidative stress and damage to DNA, lipids, and proteins (NIH, 2022). Dysregulation of these proteins is a hallmark of numerous pathologies, including cancer, where tumor cells often upregulate antioxidant systems to survive high metabolic stress, and neurodegenerative diseases, where chronic oxidative damage drives neuronal loss (ResearchGate, 2026). Pharmacological intervention strategies include the use of Nrf2 activators to boost endogenous defenses, NOX inhibitors to reduce ROS production, and pro-oxidant drugs to selectively induce apoptosis in cancer cells (MDPI, 2023). However, the therapeutic targeting of these proteins remains challenging due to the complex, context-dependent nature of redox signaling and the potential for systemic side effects (NIH, 2026).
Activation of the Nrf2-mediated antioxidant response, inhibition of ROS-generating enzymes such as NADPH oxidase (NOX), scavenging of free radicals, and induction of ROS-mediated apoptosis in cancer cells.
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