Angela L. Guillozet-Bongaarts

TL;DR: 5XFAD mice rapidly recapitulate major features of AD amyloid pathology and may be useful models of intraneuronal Aβ42-induced neurodegeneration and amyloids plaque formation.

TL;DR: Evidence that strongly suggests that truncations at both the amino- and carboxy-termini directly influence the conformation into which the molecule folds, and hence the ability of tau to polymerize into fibrils is discussed.

TL;DR: Creation of the Tau-C3 epitope appears to occur relatively early in the disease state, contemporaneous with the initial Alz50 folding event that heralds the appearance of filamentous tau in NFTs, neuropil threads, and the dystrophic neurites surrounding amyloid plaques.

TL;DR: A role for caspase-6 and N-terminal truncation of tau during neurofibrillary tangle evolution and the progression of Alzheimer's disease is suggested.

TL;DR: It is concluded that tau phosphorylation at S422 may be a protective mechanism that inhibits cleavage in vivo and found that S422E tau is more resistant to proteolysis by caspase’3 than non‐pseudophosphorylated tau.