Structure of tau protein and assembly into paired helical filaments.
Over the past few years the systematic investigation of paired helical filament assembly from tau protein in vitro has become feasible. We review our current understanding of the structure and conformations of tau protein and how this affects tau's assembly into the pathological paired helical filaments in Alzheimer's disease.
Friedhoff
P
P
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.
von Bergen
M
M
Mandelkow
E M
EM
Mandelkow
E
E
D000544:Alzheimer Disease / Q000473:pathology*; D000818:Animals; D001923:Brain Chemistry; D004195:Disease Models, Animal; D006801:Humans; D016874:Neurofibrillary Tangles / Q000737:chemistry* / Q000648:ultrastructure; D019600:Neuropil Threads / Q000737:chemistry* / Q000648:ultrastructure; D010766:Phosphorylation; D011487:Protein Conformation; D017510:Protein Folding; D020033:Protein Isoforms / Q000737:chemistry; D012995:Solubility; D016875:tau Proteins / Q000737:chemistry* / Q000235:genetics
D020033:Protein Isoforms; D016875:tau Proteins