Protein misfolding is a major driver of ageing‐associated frailty and disease pathology.
Although all cells possess multiple, well‐characterised protein quality control systems to …

In Huntington's disease, as in other neurodegenerative diseases, it was initially thought that
insoluble protein aggregates are the toxic species. However, growing evidence implicates …

An evolutionary conserved response of cells to proteotoxic stress is the organized
sequestration of misfolded proteins into subcellular deposition sites. In Saccharomyces …

The brain has a limited capacity to self-protect against protein aggregate-associated
pathology, and mounting evidence supports a role for phagocytic glia in this process. We …

Increasing evidence in recent years indicates that protein misfolding and aggregation,
leading to ER stress, are central factors of pathogenicity in neurodegenerative diseases …

Huntington's disease (HD) is a neurodegenerative disorder caused by an expanded CAG
trinucleotide repeat in the huntingtin gene (HTT). Molecular chaperones have been …

Amyotrophic lateral sclerosis is a rapidly progressing neurodegenerative disease
associated with protein misfolding and aggregation. Most cases are characterized by TDP …

Huntington's Disease (HD) is a hereditary neurodegenerative disorder caused by the
expansion of a CAG triplet repeat in the HTT gene, resulting in the production of an aberrant …

Significance: Impairment of the ubiquitin-proteasome system (UPS) has been implicated in
the pathogenesis of a wide variety of neurodegenerative disorders, including Alzheimer's …

Stress pathways monitor intracellular systems and deploy a range of regulatory mechanisms
in response to stress. One of the best-characterized pathways, the UPR (unfolded protein …