{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSIRPα functions as a key myeloid cell checkpoint receptor that, upon engaging its ligand CD47 on neighboring cells, transmits an inhibitory “don’t‐eat‐me” signal that prevents phagocytosis. This receptor–ligand interaction is exploited by tumor cells to avoid immune clearance and plays a central role in xenotransplant rejection. Blockade of the CD47–SIRPα axis – whether by monoclonal antibodies, engineered fusion proteins, or CD47‐redirected “Velcro” variants – restores macrophage‐mediated phagocytosis of tumor cells and has been shown to curb primary tumor growth and metastasis in diverse models. 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By recruiting intracellular phosphatases such as SHP‐2, SIRPα helps to dampen pro‐inflammatory signaling cascades—including MAPK and NF‐κB pathways—after exposure to microbial products like LPS, which in turn is critical for maintaining tissue homeostasis and proper immune cell development."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural and mechanistic studies of SIRPα have further delineated its ligand‐binding features and underscored its broader roles in tissue physiology beyond immune regulation. Detailed crystallographic and mutational analyses have identified critical residues that determine its specificity for CD47, paving the way for novel engineering approaches aimed at fine‐tuning this interaction. 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