Journal article
Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis
Abstract
Sialidase (neuraminidase, EC 3.2.1.18) catalyses the hydrolysis of terminal sialic acid residues of glyconjugates. Sialidase has been well studied in viruses and bacteria where it destroys the sialic acid-containing receptors at the surface of host cells1–3, and mobilizes bacterial nutrients4. In mammals, three types of sialidases, lysosomal, plasma membrane and cytosolic, have been described5,7. For lysosomal sialidase in humans, the primary …
Authors
Pshezhetsky AV; Richard C; Michaud L; Igdoura S; Wang S; Elsliger M-A; Qu J; Leclerc D; Gravel R; Dallaire L
Journal
Nature Genetics, Vol. 15, No. 3, pp. 316–320
Publisher
Springer Nature
Publication Date
March 1997
DOI
10.1038/ng0397-316
ISSN
1061-4036
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceBase SequenceCells, CulturedChromosome MappingChromosomes, Human, Pair 6Cloning, MolecularDNA PrimersDNA Transposable ElementsFrameshift MutationHumansLysosomal Storage DiseasesLysosomesMolecular Sequence DataMutationNeuraminidasePoint MutationPolymerase Chain ReactionPolymorphism, Single-Stranded ConformationalRecombinant ProteinsSequence Homology, Amino AcidSkin