title: Endosialidase NF appears to bind polySia DP5 in a helical conformation.
authors.affiliation: Institute for Glycomics, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre, Queensland 9726, Australia.
authors.forename: Thomas
authors.initials: T
authors.lastname: Haselhorst
authors.forename: Katharina
authors.initials: K
authors.lastname: Stummeyer
authors.forename: Martina
authors.initials: M
authors.lastname: Mühlenhoff
authors.forename: Wiebke
authors.initials: W
authors.lastname: Schaper
authors.forename: Rita
authors.initials: R
authors.lastname: Gerardy-Schahn
authors.forename: Mark
authors.initials: M
authors.lastname: von Itzstein
mesh_terms: D001419:Bacteria / Q000201:enzymology; D002240:Carbohydrate Sequence; D008958:Models, Molecular; D008968:Molecular Conformation; D009439:Neuraminidase / Q000737:chemistry* / Q000378:metabolism; D009844:Oligosaccharides / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012794:Sialic Acids / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009844:Oligosaccharides; D012794:Sialic Acids; C518601:polysialic acid DP5; C035355:endo-N-acetylneuraminidase; D009439:Neuraminidase