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- W2806052492 endingPage "S546" @default.
- W2806052492 startingPage "S535" @default.
- W2806052492 abstract "Tau protein plays a major role in the pathogenesis of Alzheimer’s disease. Despite many decades of intensive research, the cause of the conformational switch that leads to the remodeling of the highly flexible conformational ensemble of intrinsically disordered protein tau into insoluble filaments is still elusive. We show here that truncation of tau may play a causative role in this conformational change, as evidenced by results obtained from in vitro experiments and from transgenic animal models. This conformational change is a common denominator of pathological tau protein assemblies, and a salient drug target. The long-running research of truncated tau has led to the generation of the first active tau vaccine that has entered clinical trials." @default.
- W2806052492 created "2018-06-13" @default.
- W2806052492 creator A5012058569 @default.
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- W2806052492 creator A5088031089 @default.
- W2806052492 date "2018-06-12" @default.
- W2806052492 modified "2023-09-26" @default.
- W2806052492 title "Tau Conformation as a Target for Disease-Modifying Therapy: The Role of Truncation" @default.
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