Several lines of evidence suggest that a defective protein folding is a central event in both Alzheimer's and prion disease. Although the two disorders are very different clinically, neuropathologically, and biochemically, ...

The aggregation of proteins into amyloid fibrils is the hallmark feature of a group of late-onset degenerative diseases including Alzheimer, Parkinson, and prion diseases. We report here that microcin E492, a peptide ...

Background: One of the main features of Alzheimer’s disease (AD) is the presence of Aβ deposits, which accumulate in the brain years before the onset of symptoms. We and others have demonstrated that cerebral Aβ-amyloidosis ...

Prions are the infectious agents responsible for prion diseases, which appear to be composed exclusively by the misfolded prion protein (PrPSc). Disease is transmitted by the autocatalytic propagation of PrPSc misfolding ...

Prions are the proteinaceous infectious agents responsible for Transmissible Spongiform Encephalopathies. Compelling evidence supports the hypothesis that prions are composed exclusively of a misfolded version of the prion ...

The central event in protein misfolding disorders (PMDs) is the accumulation of a misfolded form of a naturally expressed protein. Despite the diversity of clinical symptoms associated with different PMDs, many similarities ...

Prion diseases are fatal and infectious neurodegenerative disorders characterized by the accumulation of an abnormally folded form of the prion protein ( PrP), termed PrPSc. Prion replication triggers endoplasmic reticulum ...

The main event in the pathogenesis of prion diseases is the conversion of the cellular prion protein (PrPC) into the abnormal, protease-resistant prion protein (PrPres). PrPC is a GPI-anchored protein located in lipid rafts ...

Akey molecular pathway implicated in diverse neurodegenerative diseases is the misfolding, aggregation, and accumulation of proteins in the brain. Compelling evidence strongly supports the hypothesis that accumulation ...