title: How amyloid precursor protein protects itself from cleavage.
abstract: In this issue of Structure, Tang and colleagues probe how the Flemish mutation in amyloid precursor protein (APP) affects its conformation and cleavage by γ-secretase. They provide molecular insight into how an extracellular inhibitory element and cholesterol interactions affect the generation of Aβ peptides.
authors.affiliation: Department of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.
authors.forename: Hsiang-Kai
authors.initials: HK
authors.lastname: Lin
authors.affiliation: Department of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA. Electronic address: pvdwel@pitt.edu.
authors.forename: Patrick C A
authors.initials: PC
authors.lastname: van der Wel
mesh_terms: D016229:Amyloid beta-Peptides / Q000096:biosynthesis*; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry* / Q000235:genetics*; D000818:Animals; D006801:Humans; D009154:Mutation
chemical_list: D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor