{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSulfiredoxin 1 (SRXN1) is an evolutionarily conserved redox‐regulatory enzyme that plays a central role in restoring the function of antioxidant proteins during oxidative stress. By catalyzing the ATP‐dependent reduction of hyperoxidized cysteine sulfinic acid in typical 2-Cys peroxiredoxins, SRXN1 regenerates their peroxidase activity and thus maintains cellular redox homeostasis. In addition, SRXN1 participates in deglutathionylation reactions that reverse glutathione adducts on critical proteins, restoring enzyme activities and further contributing to the regulation of redox‐mediated signal transduction. These mechanistic insights, together with detailed structural analyses that reveal its unique nucleotide binding and catalytic motifs, underscore the enzyme’s multifaceted role in protecting cells against oxidative and nitrosative stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn diverse disease contexts, particularly in cancer and other oxidative stress-related pathologies, aberrant SRXN1 expression has been implicated in modulating cellular responses and tumor behavior. SRXN1 is under transcriptional control of the NRF2 pathway and is upregulated in conditions such as lung injury, fibrotic lung diseases, and various malignancies. In these settings, elevated SRXN1 expression not only counteracts oxidative damage but also influences key signaling cascades – including AP-1, MAPK, and EGFR pathways – which promote cell survival, migration, and invasion. Its modulation has been directly associated with changes in epithelial-mesenchymal transition markers, implicating SRXN1 in the progression and metastasis of tumors, as well as in resistance to chemoradiotherapy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurthermore, emerging evidence indicates that SRXN1 not only serves as a guardian against oxidative stress but also acts as a pro-tumorigenic factor in a range of cancers, including colorectal, hepatocellular, esophageal squamous cell, cervical, and prostate carcinomas. In these studies, high SRXN1 levels have been correlated with enhanced cell proliferation, invasion, and metastatic potential, as well as with poor patient prognosis. Moreover, the enzyme has been linked to therapeutic resistance, suggesting that its inhibition might synergize with current treatments by disrupting ROS-mediated survival signals. Collectively, these findings highlight SRXN1 as a promising prognostic biomarker and a potential target for therapeutic intervention in malignancies driven by redox imbalances."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Thomas J Jönsson, Michael S Murray, Lynnette C Johnson, et al. 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