Journal
JOURNAL OF ALZHEIMERS DISEASE
Volume 64, Issue -, Pages S535-S546Publisher
IOS PRESS
DOI: 10.3233/JAD-179942
Keywords
Aggregation; Alzheimer's disease; conformational ensemble; immunotherapy; tau protein; truncation
Categories
Funding
- VEGA grant [2/0177/15]
- EU structural funds [ITMS 26240220008]
- Axon Neuroscience SE
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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.
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