BACKGROUND Parkinson's disease (PD) is a slowly progressive neurodegenerative disorder which affects widespread areas of the brainstem, basal ganglia and cerebral cortex. A number of proteins are known to accumulate in parkinsonian brains including ubiquitin and α-synuclein. Prion diseases are sporadic, genetic or infectious disorders with various clinical and histopathological features caused ...

Mammalian and fungal prions arise de novo; however, the mechanism is poorly understood in molecular terms. One strong possibility is that oxidative damage to the non-prion form of a protein may be an important trigger influencing the formation of its heritable prion conformation. We have examined the oxidative stress-induced formation of the yeast [PSI+] prion, which is the altered conformation...

Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving conversion from the normal cellular prion protein to the pathogenic misfolded conformation (PrPSc). This conversion has been used for in vitro assays including serial protein misfolding amplification and real-time quaking induced conversion (RT-QuIC). RT-QuIC can be used for the ...

Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of forming several distinct self-templating conformers. In prion diseases, these different structures, called prion strains (or variants), confer dramatic variation in disease pathology and transmission. Aggregate stability has been found to be a key determinant of the diverse pathological consequences ...

• STI1 is a co-chaperone involved in the correct client proteins' folding. Extracellular crucial for CNS maintenance and homeostasis. expression associated with tumor progression impaired survival of patients. can be biomarker therapeutic target several malignancies. Stress inducible protein 1 (STI1) acting Hsp70 Hsp90 proteins’ folding therefore cellular Besides being expressed cytosol, also f...

NMR structures of recombinant prion proteins from various species expressed in Escherichia coli have been solved during the past years, but the fundamental question of the relevancy of these data relative to the naturally occurring forms of the prion protein has not been directly addressed. Here, we present a comparison of the cellular form of the bovine prion protein isolated and purified from...

In this paper we will review various aspects of the biology of prions and focused on what is currently known about the mammalian PrP prion. Also briefly describe the prions of yeast and other fungi. Prions are infectious proteins behaving like genes, ie proteins that not only contain genetic information in its tertiary structure, ie its shape, but are also able to transmit and replicate in a ma...

possibly other neurodegenerative diseases as well. data suggest that the UPR may represent a new therapeutic target for drug development to treat prion disease and emergence of clinical disease in prion-infected mice, whereas untreated animals all succumbed to disease. These pharmacological inhibition would be neuroprotective. The compound prevented neurodegeneration and the used a newly descri...

Prion strains (or variants) are structurally distinct amyloid conformations arising from a single polypeptide sequence. The existence of prion strains has been well documented in mammalian prion diseases. In many cases, prion strains manifest as variation in disease progression and pathology, and in some cases, these prion strains also show distinct biochemical properties. Yet, the underlying b...