PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34662214-5 2022 Here, we utilize N-glycan profiling by nanoLC-chip QTOF mass cytometry to characterize the bacterial neuraminidase-associated compositional shift of the macrophage glycocalyx, which revealed a decrease in sialylated and an increase in fucosylated and high mannose structures. n-glycan 17-25 neuraminidase 1 Homo sapiens 101-114 34662214-9 2022 Together, these findings strongly suggest that while neuraminidase-mediated N-glycan modification impaired both macrophage phagocytosis and galvanotaxis, yet to be defined mechanisms other than NanH may play a more important role in bioelectrical control of macrophage trafficking, which potentially triggers dissemination. n-glycan 76-84 neuraminidase 1 Homo sapiens 53-66 35014832-7 2022 Second, we compared the effects of single amino acid substitution at the N-sequons, including N186Q, N343Q, and N352Q, each one N-glycan reduction from one NEU1 molecule. n-glycan 128-136 neuraminidase 1 Homo sapiens 156-160 35014832-14 2022 The third N-glycan at the N352-sequon contributes to the self-aggregation of NEU1. n-glycan 10-18 neuraminidase 1 Homo sapiens 77-81 30641224-9 2019 Relative abundances of several N-glycan structures were dramatically altered by the neuraminidase treatment, which selectively removed sialic acid residues. n-glycan 31-39 neuraminidase 1 Homo sapiens 84-97 33629527-3 2021 The influenza A virus (IAV) proteins hemagglutinin (HA) and neuraminidase (NA) have multiple N-glycosylation sites, and alteration of N-glycan micro- and macroheterogeneity can have strong effects on virulence and immunogenicity. n-glycan 134-142 neuraminidase 1 Homo sapiens 60-73 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. n-glycan 62-70 neuraminidase 1 Homo sapiens 38-51 19714866-11 2009 The N-terminal N-glycan of NEU1 is indispensable for its function, whereas the C-terminal N-glycan appears to be non-essential. n-glycan 15-23 neuraminidase 1 Homo sapiens 27-31 19133226-0 2009 Active 1918 pandemic flu viral neuraminidase has distinct N-glycan profile and is resistant to trypsin digestion. n-glycan 58-66 neuraminidase 1 Homo sapiens 31-44 24386838-1 2013 To determine the functions of N-carbohydrate chains in human parainfluenza virus type 3 hemagglutinin-neuraminidase(HN) protein, a PCR-based site-directed mutagenesis method was used to obtain N-glycan mutants. n-glycan 193-201 neuraminidase 1 Homo sapiens 102-115 19421409-5 2009 RESULTS: High mannose, bi and tri-antennary nonbisected and bisected complex N-glycan, N-acetyl glucosamine and galactose were expressed by drusen, retinal pigment epithelium, Bruch"s membrane, and photoreceptors while N-acetyl galactosamine and fucose were absent; treatment with neuraminidase exposed subterminal galactose in both sites and sparse N-acetyl galactosamine residues in drusen alone. n-glycan 77-85 neuraminidase 1 Homo sapiens 281-294 17846903-7 2008 High mannose, bi/tri-nonbisected and bisected complex N-glycan, N-acetyl glucosaminyl, galactosyl and sialyl residues were found to be expressed by drusen, while treatment with neuraminidase exposed subterminal N-acetyl galactosamine and galactosyl residues. n-glycan 54-62 neuraminidase 1 Homo sapiens 177-190