{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUSP17L11 is a member of the ubiquitin‐specific protease family, enzymes that remove ubiquitin moieties from protein substrates and thereby modulate their stability and activity. Although none of the provided abstracts mention USP17L11 directly, many of these studies describe cell death and neuroprotective signaling cascades in which dynamic ubiquitination events play critical roles. For example, several studies demonstrate that death‐associated protein kinase 1 (DAPK1) is activated in settings of cerebral ischemia and other stress conditions, where it phosphorylates substrates such as NMDA receptor subunits and tau protein to promote apoptotic and necrotic neuronal death."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn parallel, a series of investigations have unraveled unexpected roles for vascular endothelial growth factor‐B (VEGF‐B) in non‐traditional angiogenic processes, such as the regulation of endothelial lipid uptake, metabolic adjustments in type 2 diabetes, and the survival and neuroprotective functions of vascular and neural cells. These works describe how VEGF‐B signaling—notably through VEGF receptor 1 and neuropilin 1—coordinates lipid transport and mitochondrial metabolism, improves insulin sensitivity, and even modulates inflammatory and regenerative responses in tissues ranging from the brain to the kidney."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond these specific pathways, a broader network of ubiquitin‐mediated regulation underpins many of the signaling events described in the literature. Studies highlighting molecules such as cereblon (CRBN) and components of E3 ubiquitin ligase complexes reveal that precise control of protein ubiquitination and deubiquitination is essential for modulating inflammation, energy metabolism, and even synaptic plasticity. Although USP17L11 itself is not directly featured in these reports, its putative deubiquitinating activity positions it as a likely regulator of key mediators in these diverse pathways. In particular, USP17L11 could conceivably influence the turnover and function of proteins involved in neuronal survival, vascular homeostasis, and metabolic adaptation, much like other deubiquitinases that have been shown to affect these processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "41"}]}, {"type": "t", "text": " This integrated perspective supports the idea that further investigation of USP17L11 may reveal important insights into how deubiquitination governs cellular homeostasis in health and disease.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Weihong Tu, Xin Xu, Lisheng Peng, et al. 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