Recent studies are now highlighting prion-like mechanisms of propagation of protein misfolding in a variety of common, non-infectious (that is, transmission between individuals has never been shown outside experimental conditions), neurodegenerative diseases such as Alzheimer disease (AD), frontotemporal dementia (FTD), Parkinson disease (PD ...

Jul 18, 2014 · Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen.

The universe of prion and prion-like phenomena has expanded significantly in the past several years. Here, we overview the challenges in classifying this data informatically, given that terms such as “prion-like”, “prion-related” or “prion-forming” ...

Prions are self‐perpetuating proteins able to switch between a soluble state and an aggregated‐and‐transmissible conformation. These proteinaceous entities have been widely studied in yeast, where they are involved in hereditable phenotypic adaptations.

Currently, the key difference between these proteins and prions is that although the prion-like proteins are considered to be infectious, they are not considered to be transmissible, by standard definition. Additionally, there are no known animal or human epidemics or established occupational risks.

Nov 3, 2022 · Prion and prion-like diseases are characterized by the deposition of misfolded proteins or amyloid aggregates as internal inclusion (i.e., PD and ALS) or external plaques (i.e., AD) in the CNS. The core of these insoluble deposits is made up of misfolded proteins that are unique to each disease and share no obvious homology with one another.

Jun 1, 2024 · In this review, we discuss current proposals for the ‘prion-like’ mechanisms of spread for tau and prion protein as well as discuss different influencers on structures of aggregates from tauopathies and prion diseases.

5 days ago · The prion’s dangerous, infectious nature may make this research among the last conducted with human prion protein, Liu said. Such research was restricted after an accidental exposure in a French lab led to a researchers’ death from prion disease. Human trials of any therapy that might emerge from the work remain several years away, Liu said.

This review addresses state-of-the-art computational approaches to identify prion-like proteins, describes proteome-wide analysis efforts, discusses these unique proteins' functional role, and illustrates recently validated examples in different domains of life.

Mar 1, 2020 · Prion-like behaviour is an abrupt process, an “all-or-nothing” transition between a monomeric species and an “infinite” fibrillated form. Once a nucleation point is formed, the process is unstoppable as fibrils self-propagate by recruiting and converting all …