The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Post-translational modifications (PTMs) on tau have long been recognized as affecting
protein function and contributing to neurodegeneration. The explosion of information on …

The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are
involved in myriad cellular processes. Their distribution in various cellular compartments …

The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

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), a common neurodegenerative disease in the elderly and the most
prevalent cause of dementia, is characterized by progressive cognitive impairment. The …

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 …

Most neurodegenerative diseases are characterized by intracellular aggregates of insoluble
proteins. As for the majority of these disorders, aetiology and pathogenesis are only poorly …

In 1975, tau protein was isolated as a microtubule-associated factor from the porcine brain.
In the previous year, a paired helical filament (PHF) protein had been identified in …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …