protein aggregation is thought to be the pathological driving force responsible for neurodegenerative disorders such as alzheimer’s, parkinson’s, huntington’s, frontotemporal dementia, dementia with lewy bodies and prion diseases, however, it is not yet clear whether, or to what extent, the misfolded proteins are the cause of the diseases rather than the consequences. the aggregated proteins th...

We develop a mathematical model that describes concentration dynamics of PrP (Prion Protein Cellular) and Scrapie) prion proteins at the neuron scale includes effect unfolded protein response (UPR). first introduce single taking UPR mechanism into account. investigate it propose stability study among which bifurcation analysis with respect to three its parameters. Then, we generalize two neuron...

Replicating amyloids, called prions, are responsible for transmissible neurodegenerative diseases in mammals and some heritable phenotypes in fungi. The transmission of prions between species is usually inhibited, being highly sensitive to small differences in amino acid sequence of the prion-forming proteins. To understand the molecular basis of this prion interspecies barrier, we studied the ...

Prion diseases and prion-like protein misfolding diseases involve the accumulation of abnormally aggregated forms of the normal host proteins, such as prion protein and Tau protein. These proteins are special because of their self-duplicating and transmissible characteristics. Such abnormally aggregated proteins mainly formed in neurons, cause the neurons dysfunction, and finally lead to invari...

Significance We present evidence that alleviating nitrergic stress during early phases of neurodegeneration reduces neuroinflammatory posttranslational nitric oxide signaling and glycation-assisted dysfunction in the hippocampus prion-diseased mice, a mechanism which might be applicable to other protein-misfolding neurodegenerative conditions. confirmed pharmacological suppression activity form...

Prion diseases and prion-like protein misfolding diseases are related to the accumulation of abnormal aggregates of the normal host proteins including prion proteins and Tau protein. These proteins possess self-templating and transmissible characteristics. The crowded physiological environments where the aggregation of these amyloidogenic proteins takes place can be imitated in vitro by the add...

Many protein-misfolding diseases are caused by proteins carrying prion-like domains. These proteins show sequence similarity to yeast prion proteins, which can interconvert between an intrinsically disordered and an aggregated prion state. The natural presence of prions in yeast has provided important insight into disease mechanisms and cellular proteostasis. However, little is known about prio...