title: Roles for glycosylation in the anti-inflammatory molecule CD59.
authors.affiliation: Department of Biochemistry, University of Oxford, U.K.
authors.forename: P M
authors.initials: PM
authors.lastname: Rudd
authors.forename: B P
authors.initials: BP
authors.lastname: Morgan
authors.forename: M R
authors.initials: MR
authors.lastname: Wormald
authors.forename: D J
authors.initials: DJ
authors.lastname: Harvey
authors.forename: C W
authors.initials: CW
authors.lastname: van den Berg
authors.forename: S J
authors.initials: SJ
authors.lastname: Davis
authors.forename: M A
authors.initials: MA
authors.lastname: Ferguson
authors.forename: R A
authors.initials: RA
authors.lastname: Dwek
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism; D000818:Animals; D018957:CD59 Antigens / Q000096:biosynthesis / Q000737:chemistry / Q000502:physiology*; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006031:Glycosylation; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D006801:Humans; D007249:Inflammation; D008322:Mammals; D008958:Models, Molecular; D008969:Molecular Sequence Data
chemical_list: D018957:CD59 Antigens; D017261:Glycosylphosphatidylinositols; D000110:Acetylcholinesterase