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Redox-sensitive proteins is a broad, non-specific term referring to any proteins that contain amino acid residues—most commonly cysteine—that can undergo reversible oxidation or reduction reactions. These modifications are typically triggered by changes in cellular redox status, such as during oxidative stress. Redox-sensitive proteins play diverse roles in cells, including regulating signal transduction pathways, gene expression, metabolism, and protein synthesis. They are found throughout various cellular compartments but are less likely to be extracellular; significant proportions localize to chloroplasts and mitochondria. The term does not refer to a single molecule or therapeutic target but rather describes a functional property shared by many different proteins across multiple families and biological processes[1][2]. **Note:** "Redox-sensitive protein" is not a canonical name for an individual molecular target; it refers generically to any protein with redox-modifiable residues. There is no single receptor or enzyme called "redox-sensitive protein," so this entry should be considered incorrect for structured drug-target information purposes[1][2].
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