Huntington's disease (HD) is a fatal neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin (HTT) protein. The expression of mutant HTT in the baker's yeast Saccharomyces cerevisiae recapitulates many of the cellular phenotypes observed in mammalian HD models. Mutant HTT aggregation and toxicity in yeast is influenced by the presence of the Rnq1p and Sup35p prions, as ...

Prion protein family comprises proteins, which share not only similarity in their primary structure, but also similarity in their fold. These two groups of similarity presume a parceling in their respective biological function through the common biochemical properties. In this review, biochemical and structural similarities of PrP and two other proteins, Doppel and Shadoo, are evocated. Some ev...

This paper introduces APA (“Artificial Prion Assembly”): a pattern recognition system based on artificial prion crystalization. Specifically, the system exhibits the capability to classify patterns according to the resulting prion selfassembly simulated with cellular automata. Our approach is inspired in the biological process of proteins aggregation, known as prions, which are assembled as amy...

Self-propagating abnormal proteins, prions, have been identified in yeast; asparagine/glutamine-rich 'prion domains' within these proteins can inactivate the linked functional domains; new prion domains and reporters have been used to make 'synthetic prions', leading to discoveries of new natural prions.

The [URE3] nonchromosomal genetic element is a prion of Ure2p, a regulator of nitrogen catabolism in Saccharomyces cerevisiae. Ure2p1-65 is the prion domain of Ure2p, sufficient to propagate [URE3] in vivo. We show that full length Ure2p-green fluorescent protein (GFP) or a Ure2p1-65-GFP fusion protein is aggregated in cells carrying [URE3] but is evenly distributed in cells lacking the [URE3] ...

Human prion diseases are neurodegenerative disorders caused by abnormally folded prion proteins in the central nervous system. These proteins can be detected using the quaking-induced conversion assay. Compared with other bioassays, this assay is extremely sensitive and was used in the present study to determine prion distribution in sporadic Creutzfeldt-Jakob disease patients at autopsy. Altho...

E indications that the infectious agent responsible for scrapie did not contain nucleic acid (1) led to several insightful hypotheses to explain this conundrum (2). Eventually considerable data came to support one of these ideas, dubbed the prion hypothesis, also shown to be applicable to related fatal transmissible spongiform encephalopathies including Creutzfeldt–Jakob and mad cow disease (3)...

Prions are infectious proteins composed of the abnormal disease-causing isoform PrPSc, which induces conformational conversion of the host-encoded normal cellular prion protein PrPC to additional PrPSc. The mechanism underlying prion strain mutation in the absence of nucleic acids remains unresolved. Additionally, the frequency of strains causing chronic wasting disease (CWD), a burgeoning prio...