EC Number |
General Information |
Reference |
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3.2.1.18 | malfunction |
mutations in the NEU1 gene are causative of sialidosis, a severe lysosomal storage disorder showing autosomal recessive mode of inheritance |
730767 |
3.2.1.18 | malfunction |
mutations of residues expected to interact directly with the sialic acid N5-acetyl (A160, M87, I105) and C7-C9 glycerol side-chain (E113, Y179, Y181) reduce enzymatic activity. Truncations at the N- or C-terminus of more than 10 residues abolish enzyme activity |
717641 |
3.2.1.18 | malfunction |
neuraminidase insertion mutant virus shows increased particles formation, in pseudotyped particles system, activity compared to the wild-type virus. Compared with the wild-type AH N1, from A/California/05/2009/H1N1, the wild-type 09N1 exhibits higher neuraminidase activity and releases more pseudoparticles. Deletion/insertion of the 09s60 segment does not alter this relationship. The infectivity of pseudoparticles harboring neuraminidase in combination with the hemagglutinin from HPAI H5N1 (AH H5) is decreased by insertion of 09s60 into AH N1 and is increased by deletion of 09s60 from 09N1, the mutation also alters the oligomeric structure, overview |
-, 718265 |
3.2.1.18 | malfunction |
neuraminidase insertion mutant virus shows increased particles formation, in pseudotyped particles system, activity compared to the wild-type virus. Compared with the wild-type AH N1, the wild-type 09N1 exhibits higher neuraminidase activity and releases more pseudoparticles. Deletion/insertion of the 09s60 segment does not alter this relationship. The infectivity of pseudoparticles harboring neuraminidase in combination with the hemagglutinin from HPAI H5N1 (AH H5, from A/Hong Kong/156/97/H5N1) is decreased by insertion of 09s60 into AH N1 and is increased by deletion of 09s60 from 09N1, the mutation also alters the oligomeric structure, overview |
-, 718265 |
3.2.1.18 | malfunction |
the absence of Neu1 results in the increased sialylation of the cell surface proteins, probably affecting multiple receptors for phagocytosis. Macrophages from the Neu1-deficient mice show increased sialylation and impaired phosphorylation of FcgammaRas well as markedly reduced phosphorylation of Syk kinase in response to treatment with immunoglobulin G-opsonized beads |
704674 |
3.2.1.18 | metabolism |
NEU3 regulates the detergent resistant membranes ganglioside content and is as a modulator of Akt phosphorylation |
730792 |
3.2.1.18 | metabolism |
NEU4 long is a downstream component of the PI3K/Akt signaling pathway required for retinoic acid-induced differentiation of neuroblastoma SK-N-BE cells |
729807 |
3.2.1.18 | more |
low-glycosylation in och1-defective Pichia pastoris enhances the immunogenicity of recombinant neuraminidase and elicits similar antibody titers with less antigen when compared with hyper- and non-glycosylated neuraminidases after vaccination of mice |
-, 718099 |
3.2.1.18 | more |
the amino terminal region of the PIV5 hemagglutinin-neuraminidase protein determines the F protein specificity in promoting cell-cell fusion |
718056 |
3.2.1.18 | more |
trans-sialidase 1 model structure complexed with the Sia derivative 3-fluoro-5-N-acetyl-9-benzamido-2,9-dideoxy-neuraminic acid |
717137 |