2023
DOI: 10.1126/sciadv.adf8169
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Structure of the immunoregulatory sialidase NEU1

Abstract: Sialic acids linked to glycoproteins and glycolipids are important mediators of cell and protein recognition events. These sugar residues are removed by neuraminidases (sialidases). Neuraminidase-1 (sialidase-1 or NEU1) is a ubiquitously expressed mammalian sialidase located in lysosomes and on the cell membrane. Because of its modulation of multiple signaling processes, it is a potential therapeutic target for cancers and immune disorders. Genetic defects in NEU1 or in its protective protein cathepsin A (PPCA… Show more

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Cited by 5 publications
(4 citation statements)
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“…In addition, G9P[13] and RVC infection significantly upregulated the expression of genes encoding proteins associated with SA catabolism with the most prominent change in expression of the gene encoding RENBP enzyme known for its catabolic role in SA metabolism [ 51 ]. Similar effect of these viruses was observed for the expression of gene encoding NEU1—sialidase which removes terminal SA from glycans [ 52 ]. In addition, G9P[13] infection was associated with downregulation of another catalytic enzyme—NPL.…”
Section: Resultsmentioning
confidence: 58%
“…In addition, G9P[13] and RVC infection significantly upregulated the expression of genes encoding proteins associated with SA catabolism with the most prominent change in expression of the gene encoding RENBP enzyme known for its catabolic role in SA metabolism [ 51 ]. Similar effect of these viruses was observed for the expression of gene encoding NEU1—sialidase which removes terminal SA from glycans [ 52 ]. In addition, G9P[13] infection was associated with downregulation of another catalytic enzyme—NPL.…”
Section: Resultsmentioning
confidence: 58%
“…Human NEU1, GLB1 and CTSA were expressed as secreted proteins in Sf9 insect cells, infected with recombinant baculovirus, and purified as previously described [33,34], except that a TEV protease cleavage site was included between the hexahistidine tag and the catalytic domains of NEU1 and CTSA proteins. NEU1 enzymatic activity assays were carried out in 50 mM sodium acetate buffer, pH 4.5, with 100 mM NaCl and 1 mM of the fluorogenic substrate 4-methylumbelliferyl N-acetyl-α-D-neuraminic acid (4MU-NANA, BioSynth EM05195).…”
Section: Methodsmentioning
confidence: 99%
“…Coordinates for NEU1 were from the PDB (8DU5) [33]. Initial coordinates for HS tetramers were generated from previous reports [35].…”
Section: Molecular Dockingmentioning
confidence: 99%
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