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Sialic acid-containing cell surface glycoproteins are a diverse group of proteins found on the extracellular surface of nearly all vertebrate cells, as well as some microbial pathogens. These glycoproteins feature one or more sialic acid residues at terminal positions of their oligosaccharide chains. The sialylation of these proteins governs a wide array of biological processes: they mediate cell-cell recognition, regulate immune response, protect cells from enzymatic degradation, control the lifetime of glycoproteins, and serve as critical ligands for immune lectins and selectins. Sialic acids confer a strong negative surface charge, contribute to hydration, and create recognition motifs for pathogens and host defense molecules. Altered sialylation on cell surface glycoproteins plays a significant role in cancer progression, inflammation, and pathogen evasion, making them notable therapeutic targets and disease biomarkers.
Blocking or modulating sialic acid-mediated cell signaling or cell-cell interactions Inhibiting sialylation to affect immune evasion (especially in cancer) Disrupting sialic acid-dependent pathogen attachment (relevant in infectious disease) Modulating complement activation by interfering with sialic acid recognition
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