| http://purl.uniprot.org/citations/8344946 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8344946 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8344946 | http://www.w3.org/2000/01/rdf-schema#comment | "Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons. Mammalian neurofilaments are composed of three polypeptide subunits, designed as NF-L, NF-M, and NF-H, all of which are phosphorylated. Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues. In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively. The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry. For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain. For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain. Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites. Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)85471-6"xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)85471-6"xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Hart G.W."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Hart G.W."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Cotter R.J."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Cotter R.J."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Cleveland D.W."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Cleveland D.W."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Chevrier M.R."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Chevrier M.R."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Dong D.L.-Y."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Dong D.L.-Y."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Xu Z.-S."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/author | "Xu Z.-S."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/pages | "16679-16687"xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/pages | "16679-16687"xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/title | "Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M."xsd:string |
| http://purl.uniprot.org/citations/8344946 | http://purl.uniprot.org/core/title | "Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M."xsd:string |