PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3800894-7 1986 The gel patterns showing higher-molecular-mass components are obtained when terminal sialic acid addition is prevented by the incubation of lung tissue with monensin or when terminal sialic acids are digested from the fully processed protein with neuraminidase. Sialic Acids 183-195 neuraminidase 1 Homo sapiens 247-260 2906937-2 1988 Following removal of sialic acids with the exoglycosidase, neuraminidase, [125I]N-azidophenethylspiperone photoincorporated into a protein of Mr = 54,000 with the appropriate pharmacological profile for D2 receptors. Sialic Acids 21-33 neuraminidase 1 Homo sapiens 59-72 35014832-1 2022 Human neuraminidase 1 (NEU1) is a lysosomal glycosidase that cleaves the terminal sialic acids of sialylglycoconjugates. Sialic Acids 82-94 neuraminidase 1 Homo sapiens 6-21 35014832-1 2022 Human neuraminidase 1 (NEU1) is a lysosomal glycosidase that cleaves the terminal sialic acids of sialylglycoconjugates. Sialic Acids 82-94 neuraminidase 1 Homo sapiens 23-27 35014832-5 2022 In this study, we first purified the NEU1 from the isolated crystals produced by the HEK293 NEU1-KO cell transiently overexpressing the normal NEU1 and found that the N-glycans were high-mannose or complex types carrying terminal sialic acids. Sialic Acids 230-242 neuraminidase 1 Homo sapiens 37-41 35014832-5 2022 In this study, we first purified the NEU1 from the isolated crystals produced by the HEK293 NEU1-KO cell transiently overexpressing the normal NEU1 and found that the N-glycans were high-mannose or complex types carrying terminal sialic acids. Sialic Acids 230-242 neuraminidase 1 Homo sapiens 92-96 35014832-5 2022 In this study, we first purified the NEU1 from the isolated crystals produced by the HEK293 NEU1-KO cell transiently overexpressing the normal NEU1 and found that the N-glycans were high-mannose or complex types carrying terminal sialic acids. Sialic Acids 230-242 neuraminidase 1 Homo sapiens 143-147 2633047-9 1989 Cleavage of terminal sialic acids from native C9 by neuraminidase results in an Mr 67,000 product with nearly unaltered hemolytic activity. Sialic Acids 21-33 neuraminidase 1 Homo sapiens 52-65 3225199-2 1988 Identification of neuraminidase-sensitive and neuraminidase-resistant sialic acids and their side chain O-acyl variants. Sialic Acids 70-82 neuraminidase 1 Homo sapiens 18-31 3225199-2 1988 Identification of neuraminidase-sensitive and neuraminidase-resistant sialic acids and their side chain O-acyl variants. Sialic Acids 70-82 neuraminidase 1 Homo sapiens 46-59 3630016-2 1987 When the glycomacropeptide was used as a substrate of neuraminidase, it exhibited many advantages as compared with ovomucin (high molecular substrate of the enzyme) due to increased content of sialic acids in the glycomacropeptide composition and to high solubility. Sialic Acids 193-205 neuraminidase 1 Homo sapiens 54-67 3779103-5 1986 These results indicate that differences in peripheral, neuraminidase-accessible sialic acids are important determinants of the gel electrophoretic mobility of the SMGs of the HL-60 line and sublines but are not likely related to the differentiation-resistance mechanism. Sialic Acids 80-92 neuraminidase 1 Homo sapiens 55-68 2427759-6 1986 Periodic acid and neuraminidase treatments on tissue sections suggested that the chemical nature of the antigenic determinant of YH206 antigen was carbohydrate in nature which might be masked by sialic acids. Sialic Acids 195-207 neuraminidase 1 Homo sapiens 18-31 4033233-6 1985 Treatment of young RBC with neuraminidase, which resulted in reduction of membrane-bound sialic acids to an extent similar to that of physiologically aged RBC, resulted in the concomitant exposure of PNA binding sites and in the agglutination of these cells by autologous serum. Sialic Acids 89-101 neuraminidase 1 Homo sapiens 28-41 4063159-1 1985 Sialic acids present on luminal surfaces of vascular endothelium were determined by perfusing neuraminidase free of proteolytic activity through carotid arteries, iliac arteries and jugular veins of anaesthetized rabbits and guinea-pigs and through human umbilical veins. Sialic Acids 0-12 neuraminidase 1 Homo sapiens 94-107 4063159-2 1985 Total sialic acids released in I h from arteries and veins, determined fluorimetrically, were 24-51 X 10(6) molecules/micron 2 endothelial surface; this was more, by up to two orders of magnitude, than sialic acids releasable by neuraminidase from other types of cells, i.e. from 0.15 X 10(6) for human erythrocytes to 15 X 10(6) for human platelets. Sialic Acids 6-18 neuraminidase 1 Homo sapiens 229-242 6698805-4 1984 The sialic acids of the crude glycoproteins isolated from normal ileum were significantly less neuraminidase-susceptible and more C4 substituted (P less than 0.01) than those of the glycoproteins isolated either from normal upper small intestine (duodenum and jejunum) or from cases of Crohn"s disease of the ileum. Sialic Acids 4-16 neuraminidase 1 Homo sapiens 95-108 6698805-7 1984 The fractions differed significantly from one another with respect to the neuraminidase susceptibility of their sialic acids (P less than 0.01), the percentage of C4 (P less than 0.01) and side-chain substituted sialic acids (P less than 0.05), and the molar fucose-sialic acid ratio (P less than 0.05). Sialic Acids 112-124 neuraminidase 1 Homo sapiens 74-87 7150713-5 1982 Aggregation can be inhibited by addition of human serum albumin and neuraminidase treatment (removal of sialic acids). Sialic Acids 104-116 neuraminidase 1 Homo sapiens 68-81 6630194-0 1983 A neuraminidase from Streptococcus sanguis that can release O-acetylated sialic acids. Sialic Acids 73-85 neuraminidase 1 Homo sapiens 2-15 6841529-2 1983 Conjugated sialic acids should be freed with neuraminidase before being subjected to the action of the lyase, but these sequential enzymic reactions may be performed in one pot. Sialic Acids 11-23 neuraminidase 1 Homo sapiens 45-58 7085659-2 1982 The labeling procedure cleaves the sialic acids to a neuraminidase-sensitive 7-carbon derivative, 5-acetamido-3,5-dideoxy-L-arabino-heptulosonic acid, termed AcNeu7 (Van Lenten, L., and Ashwell, G. (1971) J. Biol. Sialic Acids 35-47 neuraminidase 1 Homo sapiens 53-66 7060593-5 1982 After denaturation with sodium dodecyl sulfate, Vibrio cholerae neuraminidase also liberated the N-acetylgalactosamine-bound sialic acids. Sialic Acids 125-137 neuraminidase 1 Homo sapiens 64-77 7060593-7 1982 The results show that distal sialic acids linked to galactose are readily available to neuraminidase, and that their negative charge gives an increased electrophoretic mobility in polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Sialic Acids 29-41 neuraminidase 1 Homo sapiens 87-100 6255459-3 1980 By either criterion, treatment of the cells with Vibrio cholerae neuraminidase to remove cell surface sialic acids rendered them resistant to infection by Sendai virus. Sialic Acids 102-114 neuraminidase 1 Homo sapiens 65-78 7354217-3 1980 Chemical analysis of the normal glycoproteins indicated that the great majority of the sialic acids were resistant to digestion with Vibrio cholerae neuraminidase, presumably due to an ester substituent at C4. Sialic Acids 87-99 neuraminidase 1 Homo sapiens 149-162 6153110-5 1980 Removal of sialic acids with neuraminidase or inhibition of glycosylation with tunicamycin reduced the microheterogeneity of both DR subunits. Sialic Acids 11-23 neuraminidase 1 Homo sapiens 29-42 7354217-4 1980 The sialic acids of the tumor glycoproteins were significantly different from normal, in that they were less resistant to digestion with neuraminidase (p greater than 0.01), and therefore had a lower percentage of substitution at C4 (p greater than 0.01). Sialic Acids 4-16 neuraminidase 1 Homo sapiens 137-150 928327-3 1977 To study the role played by sialic acids of transferrin molecule in the formation of complexes with insulin the author used transferrin untreated and treated with neuraminidase, an enzyme splitting the sialic acid molecules from grycoprotein specifically. Sialic Acids 28-40 neuraminidase 1 Homo sapiens 163-176 39290-1 1979 Frog sartorius muscle fibres were incubated with the enzyme neuraminidase which is known to remove surface-bound sialic acids. Sialic Acids 113-125 neuraminidase 1 Homo sapiens 60-73 1245486-8 1976 The first group of proteins contains sialic acids linked to the penultimate galactosyl/N-acetylgalactosaminyl residues, which are efficiently labeled only after pretreatment with neuraminidase. Sialic Acids 37-49 neuraminidase 1 Homo sapiens 179-192 985458-0 1976 Increase in sialic acids removable by neuraminidase during the shape change of platelets. Sialic Acids 12-24 neuraminidase 1 Homo sapiens 38-51 985458-2 1976 The shape change associated with activation gave rise to an increase in sialic acids removable by neuraminidase. Sialic Acids 72-84 neuraminidase 1 Homo sapiens 98-111 4850957-4 1974 Transitional mucosa showed increased levels of total hexosamines and sialic acid as compared with the normal and this was accompanied by an increase in neuraminidase-sensitive sialic acids. Sialic Acids 176-188 neuraminidase 1 Homo sapiens 152-165 32911203-6 2020 These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity. Sialic Acids 120-132 neuraminidase 1 Homo sapiens 42-46 4705641-1 1973 The role of the surface charge of human red blood cells (RBC"s) in affecting RBC aggregation by macromolecules was studied by comparing the behavior of normal RBC"s with that of RBC"s treated with neuraminidase, which removes the sialic acids from the cell membrane and reduces the zeta potential. Sialic Acids 230-242 neuraminidase 1 Homo sapiens 197-210 32911203-6 2020 These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity. Sialic Acids 120-132 neuraminidase 1 Homo sapiens 163-167 30866786-1 2019 Influenza virus haemagglutinin (HA) and neuraminidase (NA) are involved in the recognition and modulation of sialic acids on the cell surface as the virus receptor. Sialic Acids 109-121 neuraminidase 1 Homo sapiens 40-53 32609845-7 2020 Uptake of influenza virus particles by platelets requires binding to sialoglycans and results in the removal of sialic acids by the virus neuraminidase, a trigger for hepatic clearance of platelets. Sialic Acids 112-124 neuraminidase 1 Homo sapiens 138-151 31649671-4 2019 Here, we initiated a comprehensive study on the modulation of TLR4 sialylation in Leishmania donovani (L. d)-infected macrophages by a mammalian sialidase/neuraminidase-1 (Neu1) having substrate specificity toward alpha2,3-linked sialic acids. Sialic Acids 230-242 neuraminidase 1 Homo sapiens 145-170 31649671-4 2019 Here, we initiated a comprehensive study on the modulation of TLR4 sialylation in Leishmania donovani (L. d)-infected macrophages by a mammalian sialidase/neuraminidase-1 (Neu1) having substrate specificity toward alpha2,3-linked sialic acids. Sialic Acids 230-242 neuraminidase 1 Homo sapiens 172-176 31649671-14 2019 This novel finding establishes a link between enhanced alpha2,3-linked sialic acids on TLR4 and reduced membrane-bound Neu1 which plays a significant role for inhibiting downstream signaling to establish successful infection in the host cells. Sialic Acids 71-83 neuraminidase 1 Homo sapiens 119-123 30716138-4 2019 Knockout of MUC1 in HT29-MTX cells or removal of MUC1 sialic acids by neuraminidase treatment reduced Salmonella apical invasion but did not affect lateral invasion that is not hampered by a defensive barrier. Sialic Acids 54-66 neuraminidase 1 Homo sapiens 70-83 30866786-1 2019 Influenza virus haemagglutinin (HA) and neuraminidase (NA) are involved in the recognition and modulation of sialic acids on the cell surface as the virus receptor. Sialic Acids 109-121 neuraminidase 1 Homo sapiens 55-57 30866786-8 2019 Using recombinant viruses with altered HA bindings preference between alpha2,3- and alpha2,6-linked sialic acids, we also found that NA function against different substrates is correlated with the HA-receptor specificity. Sialic Acids 100-112 neuraminidase 1 Homo sapiens 133-135 30214141-4 2018 The extracts were treated with neuraminidase A to cleave the sialic acids in MUC5AC. Sialic Acids 61-73 neuraminidase 1 Homo sapiens 31-44 29341588-5 2018 To investigate the substrate activity of 9- O-acetylated sialic acids (Neu5,9Ac2), we synthesized an acetylated fluorogenic hNEU substrate 2"-(4-methylumbelliferyl)-9- O-acetyl-alpha-d- N-acetylneuraminic acid. Sialic Acids 57-69 neuraminidase 1 Homo sapiens 124-128 28096183-2 2017 The primary pneumococcal neuraminidase, NanA, which is a sialidase that catalyzes the cleavage of terminal sialic acids from host glycoconjugates, is involved in both of these processes. Sialic Acids 107-119 neuraminidase 1 Homo sapiens 25-38 29483296-3 2018 Here, we describe biochemical characterisation of recombinant NanH, including its action on host-relevant sialoglycans such as sialyl Lewis A and sialyl Lewis X (SLeA/X), and on human cell-attached sialic acids directly, uncovering that it is a highly active broad specificity sialidase. Sialic Acids 198-210 neuraminidase 1 Homo sapiens 62-66 27917893-1 2016 Neuraminidase 1 (NEU1) is a lysosomal sialidase catalyzing the removal of terminal sialic acids from sialyloconjugates. Sialic Acids 83-95 neuraminidase 1 Homo sapiens 0-15 27825034-1 2017 We studied the ability of monoclonal Abs (mAbs) recognizing the major hemagglutinin (HA) antigenic sites to inhibit neuraminidase (NA) cleavage of sialic acids on fetuin. Sialic Acids 147-159 neuraminidase 1 Homo sapiens 116-129 27917893-1 2016 Neuraminidase 1 (NEU1) is a lysosomal sialidase catalyzing the removal of terminal sialic acids from sialyloconjugates. Sialic Acids 83-95 neuraminidase 1 Homo sapiens 17-21 26829325-9 2016 Utilising peptide N-glycosidase-F and neuraminidase to remove N-glycans and sialic acids, respectively, we found that N-glycan composition (but not sialylation alone) were responsible for this reduction in molecular weight. Sialic Acids 76-88 neuraminidase 1 Homo sapiens 38-51 26824057-4 2015 Cleavage of LAMP1 sialic acids by NEU1 limits the extent of lysosomal exocytosis. Sialic Acids 18-30 neuraminidase 1 Homo sapiens 34-38 24578376-7 2014 The removal of sialic acids by neuraminidase induces iPS-MBMC and hES cells differentiation, prompting an ectoderm commitment. Sialic Acids 15-27 neuraminidase 1 Homo sapiens 31-44 25926653-5 2015 Pretreatment of RD cells with neuraminidase (NA) and trypsin greatly reduced the binding, suggesting that the binding was mediated by sialic acids on glycoproteins. Sialic Acids 134-146 neuraminidase 1 Homo sapiens 30-43 25033754-1 2015 Neuraminidase (NA) is the second most abundant influenza surface glycoprotein and contributes to virus replication in several ways, most notably by removing sialic acids from the host and viral glycoproteins, releasing newly formed virus particles from infected cells. Sialic Acids 157-169 neuraminidase 1 Homo sapiens 0-13 26640816-11 2015 Moreover, a neuraminidase (sialidase), a component of the viral envelope of Newcastle Disease, Mumps, and Sendai viruses, can cleave sialic acids on the surface of malignant cells thereby unmasking cancer antigens and exposing them to the immune system. Sialic Acids 133-145 neuraminidase 1 Homo sapiens 12-25 17685443-4 2007 We treated cells with neuraminidase to remove sialic acids; as expected, this decreased total cell surface charge. Sialic Acids 46-58 neuraminidase 1 Homo sapiens 22-35 24076232-4 2014 METHODS: RBCs are treated with neuraminidase to specifically remove sialic acids from their surface followed by the evaluation of their deformability, zeta potential and membrane proteins. Sialic Acids 68-80 neuraminidase 1 Homo sapiens 31-44 22853823-3 2012 RESULTS: We demonstrated that the attachment of EV71 to RD and SK-N-SH cells was diminished after the removal of cell surface sialic acids by neuraminidase. Sialic Acids 126-138 neuraminidase 1 Homo sapiens 142-155 22152306-6 2011 In addition, neuraminidase treatment of apoC-III which removes the sialic acids from its glycan chain decreases its potential to inhibit LPL. Sialic Acids 67-79 neuraminidase 1 Homo sapiens 13-26 20711574-5 2010 The surface-displayed recombinant NanH protein was expressed as a fully active sialidase and also transferred sialic acids from pNP-alpha-sialoside, a sialic acid donor substrate, to human-type asialo-N-glycans. Sialic Acids 110-122 neuraminidase 1 Homo sapiens 34-38 20587060-12 2010 If the cells were treated with neuraminidase to remove cis-acting sialic acids that hinder the interaction of the virus with Sn, the amount of infected cells with macrophage grown virus increased. Sialic Acids 66-78 neuraminidase 1 Homo sapiens 31-44 19714866-1 2009 BACKGROUND: Neuraminidase-1 (NEU1) catabolizes the hydrolysis of sialic acids from sialo-glycoconjugates. Sialic Acids 65-77 neuraminidase 1 Homo sapiens 12-27 19714866-1 2009 BACKGROUND: Neuraminidase-1 (NEU1) catabolizes the hydrolysis of sialic acids from sialo-glycoconjugates. Sialic Acids 65-77 neuraminidase 1 Homo sapiens 29-33 24261589-0 2013 Influenza A penetrates host mucus by cleaving sialic acids with neuraminidase. Sialic Acids 46-58 neuraminidase 1 Homo sapiens 64-77 24261589-1 2013 BACKGROUND: Influenza A virus (IAV) neuraminidase (NA) cleaves sialic acids (Sias) from glycans. Sialic Acids 63-75 neuraminidase 1 Homo sapiens 36-49 24261589-1 2013 BACKGROUND: Influenza A virus (IAV) neuraminidase (NA) cleaves sialic acids (Sias) from glycans. Sialic Acids 77-81 neuraminidase 1 Homo sapiens 36-49 20826457-7 2010 Cleavage by neuraminidase of sialic acids, as well as lectin binding to sialic acids on the surfaces, enhanced the engulfment of apoptotic cells and blebs. Sialic Acids 29-41 neuraminidase 1 Homo sapiens 12-25 19735140-7 2009 Neuraminidase action leads to an important decrease in the interphase charge density by removing sialic acids from the cell soft surface layer. Sialic Acids 97-109 neuraminidase 1 Homo sapiens 0-13 17685443-11 2007 Because neuraminidase inhibited directional motility, we also conclude that sialic acids are required constituents of some cell surface molecule(s) through which electric fields mount a polarized transmembrane response. Sialic Acids 76-88 neuraminidase 1 Homo sapiens 8-21 15099204-6 2004 Cells were treated with (i) alpha-galactosidase, and then (ii) neuraminidase, which digests sialic acids, including NeuGc epitopes. Sialic Acids 92-104 neuraminidase 1 Homo sapiens 63-76 16314420-8 2006 We postulate that neuraminidase-1 catalyzes removal of the terminal sialic acids from carbohydrate chains of microfibrillar glycoproteins and other adjacent matrix glycoconjugates, unmasking their penultimate galactosugars. Sialic Acids 68-80 neuraminidase 1 Homo sapiens 18-33 16575520-5 2006 However, the current evidence suggests that even these neuraminidase-resistant strains might interact with sialic acids located in context different from that of the sialic acids used by the neuraminidase-sensitive strains. Sialic Acids 166-178 neuraminidase 1 Homo sapiens 55-68 16575520-5 2006 However, the current evidence suggests that even these neuraminidase-resistant strains might interact with sialic acids located in context different from that of the sialic acids used by the neuraminidase-sensitive strains. Sialic Acids 166-178 neuraminidase 1 Homo sapiens 191-204 16575520-5 2006 However, the current evidence suggests that even these neuraminidase-resistant strains might interact with sialic acids located in context different from that of the sialic acids used by the neuraminidase-sensitive strains. Sialic Acids 107-119 neuraminidase 1 Homo sapiens 55-68 15950996-2 2005 The influenza neuraminidase (NA) can cleave both alpha2,3- and alpha2,6-linked sialic acids, but all influenza NAs have a marked preference for the non-human alpha2,3 linkage. Sialic Acids 79-91 neuraminidase 1 Homo sapiens 14-27 15950996-2 2005 The influenza neuraminidase (NA) can cleave both alpha2,3- and alpha2,6-linked sialic acids, but all influenza NAs have a marked preference for the non-human alpha2,3 linkage. Sialic Acids 79-91 neuraminidase 1 Homo sapiens 29-31 9466714-6 1997 Upon neuraminidase treatment, which cleaves sialic acids, these differences in molecular weight were abolished. Sialic Acids 44-56 neuraminidase 1 Homo sapiens 5-18 12487819-7 2002 Removal of sialic acids from rgp120 with NA enhanced MBL binding. Sialic Acids 11-23 neuraminidase 1 Homo sapiens 41-43 11300878-1 2001 Neuraminidase is a surface glycoprotein of influenza viruses that cleaves terminal sialic acids from carbohydrates. Sialic Acids 83-95 neuraminidase 1 Homo sapiens 0-13 9804253-8 1998 In all cases, HMFG-1 reactivity could be restored by predigestion with keratanase or neuraminidase which removes keratan sulphates and sialic acids, respectively. Sialic Acids 135-147 neuraminidase 1 Homo sapiens 85-98 9474014-2 1998 The isoelectric points of the variant and normal CD13 were 3.3 and 4.1, respectively, and both points converged at 4.4 after treatment with neuraminidase, indicating that more sialic acids are bound to the variant CD13 than normal. Sialic Acids 176-188 neuraminidase 1 Homo sapiens 140-153 14730275-7 2004 Experimental studies demonstrate that viral NA exposes pneumococcal receptors on host cells by removing terminal sialic acids. Sialic Acids 113-125 neuraminidase 1 Homo sapiens 44-46 11814568-5 2002 Similar to EBA-175, the binding of EBP2/BAEBL to human erythrocytes was dependent on sialic acids because neuraminidase treatment of those erythrocytes rendered them incapable of binding, but differed from EBA-175 in that trypsin treatment decreased EBP2/BAEBL binding by only twofold compared to a 10-fold reduction in EBA-175 binding. Sialic Acids 85-97 neuraminidase 1 Homo sapiens 106-119 11264365-2 2001 The HA binds to sialyloligosaccharide viral receptors, while the NA removes sialic acids from the host cell and viral sialyloligosaccarides. Sialic Acids 76-88 neuraminidase 1 Homo sapiens 65-67 9874196-1 1998 The neuraminidase of influenza virus is a surface glycoprotein that catalyzes the hydrolysis of glycosidic linkages between terminal sialic acids and adjacent sugar moieties. Sialic Acids 133-145 neuraminidase 1 Homo sapiens 4-17 9406434-8 1997 Sialic acid-induced heterogeneity has been documented for many enzymes, but neuraminidase treatment can often remove sialic acids and produce gel patterns that are easier to interpret. Sialic Acids 117-129 neuraminidase 1 Homo sapiens 76-89 1999142-9 1991 Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the glycosidase-treated receptor-[125I]hCG complex also revealed that neuraminidase was able to remove the sialic acids from both subunits of the receptor-bound hormone. Sialic Acids 177-189 neuraminidase 1 Homo sapiens 140-153 9249154-2 1997 Neuraminidase enzymes recognize and cleave terminal sialic acids from cell surfaces. Sialic Acids 52-64 neuraminidase 1 Homo sapiens 0-13 9253768-0 1997 Determination of viral neuraminidase specificity for membrane-bound sialic acids by cell electrophoresis. Sialic Acids 68-80 neuraminidase 1 Homo sapiens 23-36 9253768-1 1997 The ability of the influenza virus neuraminidase (NA) to cleave specific sialic acids was measured by cell electrophoresis. Sialic Acids 73-85 neuraminidase 1 Homo sapiens 35-48 8556161-7 1995 By reversed-phase HPLC of tryptic digested neuraminidase treated rFVIIa the glycopeptides containing the heavy chain N-glycosylated site elute as two peaks compared to the four peaks corresponding to glycopeptides with 0 to 3 N-acetyl-neuraminic acids seen for untreated rFVIIa. Sialic Acids 226-251 neuraminidase 1 Homo sapiens 43-56 8590756-6 1995 The sensitivity of neurochordin D to neuraminidase suggests the presence of sialic acids. Sialic Acids 76-88 neuraminidase 1 Homo sapiens 37-50 7627976-4 1995 Removal of most of the sialic acids from SW1990 mucins by neuraminidase greatly enhanced binding of two other MUC1 peptide specific antibodies, HMFG-2 and SM-3. Sialic Acids 23-35 neuraminidase 1 Homo sapiens 58-71 8512075-3 1993 Incubation of r-HuEPO with neuraminidase caused the slowest migrating species to diminish first in response, indicating that these contained the highest numbers of sialic acids. Sialic Acids 164-176 neuraminidase 1 Homo sapiens 27-40 1591399-6 1992 A decrease in mass by neuraminidase digestion, however, determined the average number of sialic acids in the molecule. Sialic Acids 89-101 neuraminidase 1 Homo sapiens 22-35 1725500-1 1991 Agglutination of human erythrocytes by the lectin concanavalin A is enhanced when the erythrocytes are pretreated with neuraminidase, which removes sialic acids, or with pronase, which degrades both the glycophorins and band 3 protein. Sialic Acids 148-160 neuraminidase 1 Homo sapiens 119-132 1702721-6 1990 Furthermore, treatment of CD45 proteins with O-glycanase or neuraminidase resulted in the loss of both CD45R0 and CD45RB epitopes, although reactivity of the anti-CD45R0 and anti-CD45RB mAb was not affected by mAb preincubation with either sialic acids or sialyllactose in solution. Sialic Acids 240-252 neuraminidase 1 Homo sapiens 60-73 9148865-2 1997 The L-ALP from the sera of normal adults and various liver diseases was found to show different chromatographic behaviours on DSA affinity column with multiple peaks of ALP activity after the L-ALP was treated with neuraminidase to remove the terminal sialic acids on the sugar chain of L-ALP. Sialic Acids 252-264 neuraminidase 1 Homo sapiens 215-228 8642261-9 1996 Removal of terminal sialic acids with neuraminidase or protease treatment of cells abrogated cell adhesion to both selectin substrates. Sialic Acids 20-32 neuraminidase 1 Homo sapiens 38-51 1761628-4 1991 rtPA was treated with neuraminidase which removes the sialic acids from the carbohydrate chains. Sialic Acids 54-66 neuraminidase 1 Homo sapiens 22-35 34662214-4 2022 One hypothesis is that Salmonella can alter the electrical properties of the macrophages by modifying host cell surface glycan composition, which is supported by the fact that cleavage of surface-exposed sialic acids with a bacterial neuraminidase severely impairs macrophage galvanotaxis, as well as phagocytosis. Sialic Acids 204-216 neuraminidase 1 Homo sapiens 234-247