Despite the activity of cellular quality-control mechanisms, subsets of mature and newly
synthesized polypeptides fail to fold properly and form insoluble aggregates. In some cases …

Loss of protein homeostasis is a hazardous situation that jeopardizes cellular functionality
and viability Cells have developed mechanisms that supervise protein integrity and direct …

Limited detoxification capacity often directs aggregation-prone, potentially hazardous,
misfolded proteins to be deposited in designated cytosolic compartments known as …

Many devastating neurodegenerative diseases are driven by the misfolding of normal
proteins into a pathogenic abnormal conformation. Examples of such protein misfolding …

Prion diseases are associated with the conformational conversion of cellular prion protein
(PrPC) to pathological β-sheet isoforms (PrPSc), which is the infectious agent beyond …

A conformational change of the cellular prion protein (PrP c) underlies formation of PrP Sc,
which is closely associated with pathogenesis and transmission of prion diseases. The …

Prion diseases are a group of fatal neurodegenerative disorders characterised by the
accumulation of misfolded prion protein (PrP Sc) in the brain. The critical relationship …

The molecular basis for neuronal death in prion disease is not established, but putative
pathogenic roles for both disease-related prion protein (PrP Sc) and accumulated cytosolic …

The misfolding and aggregation of specific proteins is a common hallmark of many
neurodegenerative disorders, including highly prevalent illnesses such as Alzheimer's and …

Protein misfolding underlies many neurodegenerative diseases, including the transmissible
spongiform encephalopathies (prion diseases). Although cells typically recognize and …