Propagation of Tau Aggregates and Neurodegeneration

A pathway from the natively unfolded microtubule-associated protein Tau to a highly structured amyloid fibril underlies human Tauopathies. This ordered assembly causes disease and represents the gain of toxic function. In recent years, evidence has accumulated to suggest that Tau inclusions form first in a small number of brain cells, from where they propagate to other regions, resulting in neurodegeneration and disease. Propagation of pathology is often called prion-like, which refers to the capacity of an assembled protein to induce the same abnormal conformation in a protein of the same kind, initiating a self-amplifying cascade. In addition, prion-like encompasses the release of protein aggregates from…

• UO
  University of Cambridge
• EC
  European Commission
• NI
  National Institutes of Health

  Award: MC_U105184291
• MR
  Medical Research Council

  Award: MC_U105184291