Publicação
Fucosyltransferase IX: characterization and biological role
| dc.contributor.advisor | Costa, Júlia | |
| dc.contributor.author | Brito, Catarina | |
| dc.date.accessioned | 2010-06-02T14:23:07Z | |
| dc.date.available | 2010-06-02T14:23:07Z | |
| dc.date.issued | 2007-09 | |
| dc.description.abstract | α3/4-Fucosyltransferases (α3/4-FUTs) are glycosyltransferases (GTs) that catalyze the transfer of fucose in an α3/4-linkage onto the N-acetylglucosamine residue from acceptors containing the type II or type I (Galβ4/3GlcNAc, respectively) structures, thus synthesizing the fucosylated Lewis (Le) carbohydrate determinants. Fucosyltransferase IX (FUT9), the most recently identified member of the family, presents the higher divergence from the other FUTs and its sequence is the only highly conserved among species. FUT9 synthesizes the Lewisx (Lex) epitope (Galβ4(Fucα3)GlcNAc). Recent evidence has suggested that it is the enzyme responsible for the synthesis of Lex in the mouse brain. Lex expression has been described in glycoproteins, proteoglycans and glycolipids from the central nervous system (CNS) of diverse species, including rodents and humans. | en_US |
| dc.identifier.uri | http://hdl.handle.net/10362/3666 | |
| dc.language.iso | eng | en_US |
| dc.title | Fucosyltransferase IX: characterization and biological role | en_US |
| dc.type | doctoral thesis | |
| dspace.entity.type | Publication | |
| my.embargo.terms | null | en_US |
| rcaap.rights | openAccess | en_US |
| rcaap.type | doctoralThesis | en_US |