Tau in PHF is known to be highly phosphorylated and immunochemical study has indicated
the similarity of the phosphorylation between PHF-tau and fetal tau. We have determined the …

Research on the molecular pathogenesis of Alzheimer's disease (AD) has made great
strides over the last decade. This progress is the result of protein chemical analysis of two …

As neurons age, their survival depends on eliminating a growing burden of damaged,
potentially toxic proteins and organelles—a capability that declines owing to aging and …

To gain insight into the abnormal phosphorylation of PHF-tau, we have determined the
phosphorylation sites by identifying phosphopeptides by means of ion spray mass …

Tau with unusually slow mobilities in sodium dodecyl sulfate-polyacrylamide gel
electrophoresis was purified from the Sarkosyl-insoluble pellet of Alzheimer's disease brain …

Amyloid β protein (Aβ), a pathogenic molecule associated with Alzheimer's disease, is
produced by γ-secretase, which cleaves the β-carboxyl terminal fragment (βCTF) of β …

γ-Cleavage of β-amyloid precursor protein (APP) in the middle of the cell membrane
generates amyloid β protein (Aβ), and ϵ-cleavage,∼ 10 residues downstream of the γ …

We have investigated tibiquitinated paired helical filaments, which pro&e a proteinaceous
smear in 'SDS-polyacrylamide gel electrophoresis and immunoblotting. The smear …

Several lines of evidence suggest that enhanced oxidative stress is involved in the
pathogenesis and/or progression of Alzheimer's disease (AD). Amyloid β-protein (Aβ) that …

Fetal tau and tau in paired helical filaments show similar immunoreactivities with several
phosphorylation-dependent paired helical filament-polyclonals and monoclonals …