Sialidase-2 is an enzyme that in humans is encoded by the NEU2gene.[5][6][7]
This gene belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS-7 cells confirmed that this gene encodes a functional sialidase. Its cytosolic localization was demonstrated by cell fractionation experiments.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Monti E, Preti A, Rossi E, Ballabio A, Borsani G (Jun 1999). "Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases". Genomics. 57 (1): 137–143. doi:10.1006/geno.1999.5749. PMID10191093.
Chavas LM, Tringali C, Fusi P, et al. (2005). "Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition". J. Biol. Chem. 280 (1): 469–75. doi:10.1074/jbc.M411506200. PMID15501818.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Hart ML, Saifuddin M, Uemura K, et al. (2003). "High mannose glycans and sialic acid on gp120 regulate binding of mannose-binding lectin (MBL) to HIV type 1". AIDS Res. Hum. Retroviruses. 18 (17): 1311–1317. doi:10.1089/088922202320886352. PMID12487819.
Bassi MT, Sperandeo MP, Incerti B, et al. (2000). "SLC7A8, a gene mapping within the lysinuric protein intolerance critical region, encodes a new member of the glycoprotein-associated amino acid transporter family". Genomics. 62 (2): 297–303. doi:10.1006/geno.1999.5978. PMID10610726.