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Redox regulatory proteins are a diverse group of molecules essential for maintaining cellular redox homeostasis and protecting cells from oxidative stress (NIH, PMC7464800). This category includes enzymes like thioredoxins (Trx), peroxiredoxins (Prx), and superoxide dismutases (SOD), as well as transcription factors like Nrf2 that orchestrate the antioxidant response (NIH, PMC10819445). These proteins function by neutralizing reactive oxygen species (ROS) and regulating the oxidation state of cysteine residues, which acts as a molecular switch for various signaling pathways (NIH, PMC3243531). In diseases such as cancer, these proteins are often upregulated to help tumor cells survive high oxidative environments, making them attractive targets for inhibition (NIH, PMC8775674). Conversely, in neurodegenerative and cardiovascular diseases, activating these pathways can provide cytoprotection against oxidative damage (NIH, PMC10048111).
Drugs targeting redox regulatory proteins primarily act by either inhibiting antioxidant enzymes to induce oxidative stress in cancer cells (e.g., thioredoxin reductase inhibitors like auranofin) or by activating antioxidant transcription factors to enhance cellular defense in chronic diseases (e.g., Nrf2 activators like bardoxolone methyl) (NIH, PMC8775674; NIH, PMC10048111).
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