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 …

The accumulation of misfolded proteins presents a considerable threat to the health of
individual cells and has been linked to severe diseases, including neurodegenerative …

A common characteristic of neurodegenerative diseases like Alzheimer's disease (AD),
Parkinson's disease (PD) and Huntington's disease (HD) is the accumulation of protein …

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 …

The accumulation of misfolded proteins in insoluble aggregates within the neuronal
cytoplasm is one of the common pathological hallmarks of most adult-onset human …

Protein misfolding, aggregation and deposition are common disease mechanisms in many
neurodegenerative diseases including Parkinson's disease (PD). Accumulation of damaged …

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

Misfolded proteins are toxic to cells and the accumulation of toxic species can lead to protein
misfolding diseases, such as neurodegenerative disorders. The toxicity of misfolded proteins …