A hallmark of neurodegenerative proteinopathies is the formation of misfolded protein
aggregates that cause cellular toxicity and contribute to cellular proteostatic collapse …

Protein folding is a complex, multisystem process characterized by heavy molecular and
cellular footprints. Chaperone machinery enables proper protein folding and stable …

Mammalian cells remove misfolded proteins using various proteolytic systems, including the
ubiquitin (Ub)-proteasome system (UPS), chaperone mediated autophagy (CMA) and …

Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and
their aggregates by protein quality control (PQC), of which molecular chaperones are an …

Background Although there is a range of different symptoms across neurodegenerative
diseases, they have been noted to have common pathogenic features. An archetypal feature …

Recent evidence indicates that diverse neurodegenerative diseases might have a common
cause and pathological mechanism—the misfolding, aggregation and accumulation of …

A characteristic of many neurodegenerative diseases, including Alzheimer's disease (AD),
Parkinson's disease (PD), Huntington's disease (HD), and amyotrophic lateral sclerosis …

Neurodegenerative diseases, such as Alzheimer's, Parkinson's, Creutzfeldt–Jacob,
Huntington's diseases and amyotrophic lateral sclerosis, are mainly characterized by the …

One of the hallmark features in the neurodegenerative disorders (NDDs) is the accumulation
of aggregated and/or non-functional protein in the cellular milieu. Post-translational …

Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and
includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist …