title: Synthesis of truncated analogues for studying the process of glycosyl phosphatidylinositol modification.
abstract: Many eukaryotic proteins are modified with a glycosylphosphatidylinositol (GPI) anchor at their C-termini. This post-translational modification causes these proteins to be noncovalently tethered to the plasma membrane. The synthesis of truncated GPI anchor analogues is reported; these compounds were designed for use as soluble substrates for GPI transamidase (GPI-T), the enzyme that appends the GPI anchor onto proteins.
authors.affiliation: Department of Chemistry, 5101 Cass Avenue, Wayne State University, Detroit, Michigan 48202, USA.
authors.forename: Franklin
authors.initials: F
authors.lastname: John
authors.forename: Tamara L
authors.initials: TL
authors.lastname: Hendrickson
mesh_terms: D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D017261:Glycosylphosphatidylinositols / Q000737:chemistry*; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000737:chemistry*
chemical_list: D017261:Glycosylphosphatidylinositols; D010716:Phosphatidylinositols