Amyloid protein aggregation is a key factor in the development of variety serious diseases humans, commonly named as amyloidoses (Alzheimers and Parkinsons diseases, type II diabetes, etc.), determinant protein-based inheritance lower eukaryotes. In yeast, translation termination Sup35 one most extensively studied amyloidogenic proteins. Aggregation (induction [PSI+] prion) decreases its functi...

Prion diseases or transmissible spongiform encephalopathies (TSEs) are rare neurodegenerative disorders that can be acquired either by direct transmission, inherited through dominant mutations in the prion protein gene or via an unknown sporadic cause. This latter group constitutes the vast majority of cases. Like many neurodegenerative diseases the hallmarks of oxidative damage can be readily ...

Prion formation involves the conversion of proteins from a soluble form into an infectious amyloid form. Most yeast prion proteins contain glutamine/asparagine-rich regions that are responsible for prion aggregation. Prion formation by these domains is driven primarily by amino acid composition, not primary sequence, yet there is a surprising disconnect between the amino acids thought to have t...

Effective recognition and quantitative analysis of the prion protein are important in drug discovery and diagnosis for prion diseases, such as bovine spongiform encephalopathy and Creutzfeldt-Jakob diseases. We have developed a high-throughput method for a specific and sensitive determination of prion protein on a solid-phase membrane, based on a chemiluminescence reaction of aptamer with 3,4,5...