{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPeroxiredoxin‐1 (PRDX1) is a highly versatile thiol‐based peroxidase that plays a central role in cellular antioxidant defense and redox signaling. It rapidly reduces hydrogen peroxide and other peroxides through a conserved cysteine‐dependent mechanism, yet during turnover the catalytic cysteine may become oxidized to sulfinic acid—a modification that can be reversed by dedicated repair systems such as sulfiredoxin. In addition, PRDX1 is subject to a range of post‐translational modifications (for example, phosphorylation, acetylation, and S‑nitrosylation) that alter its peroxidase activity, oligomerization state, and susceptibility to hyperoxidation. These modifications enable PRDX1 not only to detoxify reactive oxygen species but also to serve as a redox sensor that modulates its interactions with other proteins, thereby integrating oxidative signals with cell cycle and stress‐response pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThrough redox‐sensitive protein–protein interactions, PRDX1 actively participates in signal transduction. Under conditions of increased hydrogen peroxide, it can relay oxidizing equivalents to target proteins involved in stress and apoptosis signaling. For instance, transient formation of mixed disulfide intermediates with kinases such as apoptosis signal–regulating kinase 1 (ASK1) and with regulatory phosphatases modulates downstream MAPK cascades. In other settings, PRDX1 interacts with factors like MST1, TOPK, and TRAF6, thereby either impeding or facilitating the initiation of apoptotic and inflammatory responses. Moreover, via a specific binding with the transcription factor FOXO3, PRDX1 influences the expression of redox‐responsive genes and regulatory microRNAs in an H₂O₂ dose‐dependent manner."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of PRDX1 is increasingly recognized in diverse pathological conditions, notably in cancer and degenerative diseases. Elevated expression and/or aberrant modification of PRDX1 is associated with enhanced tumor cell survival, angiogenesis, and resistance to chemotherapy in breast, prostate, colorectal, and liver cancers, while its altered redox state may compromise DNA integrity, telomere maintenance, and cell cycle regulation. Changes in PRDX1 expression or subcellular localization have also been linked to neurodegeneration, inflammatory vascular disorders, and even impaired sperm function. Together, these studies underscore that PRDX1 functions not only as a peroxidase but also as a critical modulator of redox‐dependent signaling pathways that dictate cell fate, making it a promising target for therapeutic intervention in a host of oxidative stress–related diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "S H Kim, M Fountoulakis, N Cairns, et al. 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