title: Assembly of Alzheimer-like filaments from full-length tau protein.
abstract: The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease.
authors.affiliation: Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: R A
authors.initials: RA
authors.lastname: Crowther
authors.forename: O F
authors.initials: OF
authors.lastname: Olesen
authors.forename: M J
authors.initials: MJ
authors.lastname: Smith
authors.forename: R
authors.initials: R
authors.lastname: Jakes
authors.forename: M
authors.initials: M
authors.lastname: Goedert
mesh_terms: D000544:Alzheimer Disease / Q000473:pathology*; D003001:Cloning, Molecular; D004926:Escherichia coli; D006801:Humans; D015151:Immunoblotting; D008854:Microscopy, Electron; D010766:Phosphorylation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000648:ultrastructure; D016875:tau Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000648:ultrastructure*
chemical_list: D011994:Recombinant Proteins; D016875:tau Proteins