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Structural analyses have revealed novel allosteric binding sites and redox‐regulated mechanisms—through reversible oxidation, S‐nitrosylation and sulfhydration—that fine‐tune its catalytic activity, opening avenues for selective pharmacological inhibition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its pivotal regulatory role in metabolism, PTP1B modulates multiple oncogenic and inflammatory signaling pathways. In various cancer models—including breast, colon, Hodgkin lymphoma, non‐small cell lung and gastric cancers—dysregulated expression or mutation of PTP1B alters downstream cascades such as Src activation, JAK–STAT signaling and receptor tyrosine kinase endocytic sorting. Through substrate‐trapping and proteolytic fragmentation studies, PTP1B has been shown to promote invasive properties (for example, via modulation of invadopodia formation) and to influence cytokine signaling by negatively regulating STAT6 and Toll‐like receptor pathways. These findings, together with evidence that microRNAs (e.g. miR‑338‑3p) and other regulatory mechanisms control its expression in tumor cells, underscore its dual role as both a tumor promoter and, in some contexts, a tumor suppressor—and highlight its potential as a therapeutic target in cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christian Wiesmann, Kenneth J Barr, Jenny Kung, et al. 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