title: Structural principles of tau and the paired helical filaments of Alzheimer's disease.
abstract: Tau, a major microtubule-associated protein in brain, forms abnormal fibers in Alzheimer's disease and several other neurodegenerative diseases. Tau is highly soluble and adopts a natively unfolded structure in solution. In the paired helical filaments of Alzheimer's disease, small segments of tau adopt a beta-conformation and interact with other tau molecules. In the filament core, the microtubule-binding repeat region of tau has a cross-beta structure, while the rest of the protein retains its largely unfolded structure and gives rise to the fuzzy coat of the filaments.
authors.affiliation: Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany. mand@mpasmb.desy.de
authors.forename: Eckhard
authors.initials: E
authors.lastname: Mandelkow
authors.forename: Martin
authors.initials: M
authors.lastname: von Bergen
authors.forename: Jacek
authors.initials: J
authors.lastname: Biernat
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Mandelkow
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D006801:Humans; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D016875:tau Proteins