Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Combined Automated Annotation using Multiple IEA Methods
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
In silico identification of new putative pathogenic variants in the NEU1 sialidase gene affecting enzyme function and subcellular localization.
Widespread macromolecular interaction perturbations in human genetic disorders.
New Insights into Molecular Organization of Human Neuraminidase-1: Transmembrane Topology and Dimerization Ability.
A reference map of the human binary protein interactome.
Structure of the immunoregulatory sialidase NEU1.
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Crystal structure of NEU1 (GH33 six-bladed beta-propeller); NEU1 removes terminal sialic acid from glycans on lysosomal products and cell-surface proteins, is catalytically inactive alone and is activated ~150-fold by CTSA, forming a megadalton lysosomal multienzyme complex with CTSA and GLB1.
Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis.
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Cloning and characterization of human lysosomal neuraminidase; the enzyme is compartmentalized in lysosomes, occurs in a complex with beta-galactosidase and protective protein/cathepsin A (PPCA), restores neuraminidase activity in a PPCA-dependent manner, and is deficient in sialidosis and galactosialidosis.
NEU1,4 hydrolyze PSAP(195-273):GM3:PE
NEU1 hydrolyses Neu5Ac from glycoconjugates
Defective NEU1 does not hydrolyse Neu5Ac from glycoconjugates
Exocytosis of specific granule lumen proteins