Alzheimer's disease (AD) is the most common neurodegenerative disorder seen in age-
dependent dementia. There is currently no effective treatment for AD, which may be …

Tau protein is involved in various cellular processes, including having a canonical role in
binding and stabilization of microtubules in neurons. Tauopathies are neurodegenerative …

N ε-lysine acetylation was discovered more than half a century ago as a post-translational
modification of histones and has been extensively studied in the context of transcription …

Alzheimer disease (AD) is a heterogeneous disease with a complex pathobiology. The
presence of extracellular β-amyloid deposition as neuritic plaques and intracellular …

Converging evidence continues to point towards Tau aggregation and pathology formation
as central events in the pathogenesis of Alzheimer's disease and other Tauopathies …

Neurofibrillary tangles, one of the neuropathologic hallmarks of Alzheimer's disease, have a
dynamic lifespan of maturity that associates with progressive neuronal dysfunction and …

Tau is well established as a microtubule-associated protein in neurons. However, under
pathological conditions, aberrant assembly of tau into insoluble aggregates is accompanied …

Alzheimer's disease (AD) is characterized by two major pathological lesions in the brain,
amyloid plaques and neurofibrillary tangles (NFTs) composed mainly of amyloid-β (Aβ) …

Tau is a microtubule-associated protein that has a role in stabilizing neuronal microtubules
and thus in promoting axonal outgrowth. Structurally, tau is a natively unfolded protein, is …

Disrupted homeostasis of the microtubule binding protein tau is a shared feature of a set of
neurodegenerative disorders known as tauopathies. Acetylation of soluble tau is an early …