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Issue title: Alzheimer’s Disease: New Beginnings
Guest editors: G. Perry, J. Avila, P.I. Moreira, A.A. Sorensen and M. Tabaton
Article type: Review Article
Authors: Novak, Petr | Cehlar, Ondrej | Skrabana, Rostislav | Novak, Michal; *
Affiliations: Institute of Neuroimmunology, Slovak Academy of Sciences, Bratislava, Slovakia
Correspondence: [*] Correspondence to: Prof. Michal Novak, Institute of Neuroimmunology SAS, Dubravska cesta 9, 84510 Bratislava, Slovakia, Slovak Republic. Tel.: +421905609558; E-mail: [email protected].
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.
Keywords: Aggregation, Alzheimer’s disease, conformational ensemble, immunotherapy, tau protein, truncation
DOI: 10.3233/JAD-179942
Journal: Journal of Alzheimer's Disease, vol. 64, no. s1, pp. S535-S546, 2018
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