{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nHuman UDP‐glucose dehydrogenase (UGDH) is a critical oxidoreductase that catalyzes the NAD⁺‐dependent conversion of UDP–glucose to UDP–glucuronic acid, a key precursor for glucuronidation and for the biosynthesis of proteoglycans and glycosaminoglycans. Detailed biochemical and structural studies have revealed that UGDH operates via two successive oxidation steps and utilizes a complex catalytic mechanism—with key active‐site residues (including, for example, Cys276 and Lys220) and defined NAD⁺– and substrate–binding regions—to promote thiohemiacetal and thioester intermediate formation. The enzyme exhibits dynamic behavior, including hysteresis and a reversible equilibrium between distinct oligomeric states, and is subject to allosteric feedback control (for example, by UDP–xylose) that triggers conformational switches mediated by packing defects in the protein core."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in UGDH expression and activity have emerged as important contributors to disease, particularly in cancer. Elevated UGDH levels can enhance the production of hyaluronan and other extracellular matrix components, thereby promoting epithelial–mesenchymal transition (EMT), tumor cell migration, invasion, and metastasis in malignancies such as glioblastoma, prostate, breast, colorectal, ovarian, and hepatocellular carcinoma. In these contexts, UGDH is subject to regulation by oncogenic transcription factors (for instance, Sp1 and KLF4) and is implicated in chemoresistance; notably, its activity and expression have been proposed as potential biomarkers for aggressive disease and field effects."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in cancer biology, UGDH is also implicated in developmental and neurological disorders as well as other pathologic conditions. Germline recessive mutations that impair UGDH stability, oligomerization, or enzymatic activity have been linked to developmental epileptic encephalopathies and abnormal brain formation, while its dysregulation in specific tissues (such as orbital fibroblasts under the influence of viral proteins) has been associated with Graves disease and altered extracellular matrix remodeling in osteoarthritis. These findings underscore the enzyme’s broader significance, making UGDH an attractive target for therapeutic intervention in diverse disease settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yannick Bontemps, Boris Vuillermoz, Frank Antonicelli, et al. 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