prpc conversion to prpsc isoform is the main known cause for prion diseases including crutzfeldt-jakob, gerstmann-sträussler-sheinker syndrome and fatal familial insomnia in human. the precise mechanism underling this conversion is yet to be well understood. in the present work,  using the coordinate file of prpc (available on the protein data bank) as a starting structure, separate molecular d...

Background & Aims: The normal form of the prion protein is called PrPC and its infectious form is called PrPSc. This protein functions like a crystallized core for the transformation of PrPc into an abnormal PrPSc. The aim of the present study was to investigate the effect of temperature on human prion protein structure through molecular dynamic simulation. Methods: In this research, the GROMAC...

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...

Prion diseases are fatal neurodegenerative that affect mammals, including humans. The hallmark of prion is the protein: misfolded and aggregated form protein PrPSc binds to cellular PrPC induces conformational conversion. Although gene polymorphisms correlate with varying degrees susceptibility host develop diseases, how residue substitutions modulate structural dynamics towards pathological mi...

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...

Abstract: Bovine Spongiform Encephalopathy (BSE) has a place with the uncommon cluster of continuously progressive neurological infections identified as Transmissible Encephalopathies (TSEs). TSE sicknesses are described by long incubation periods ranging from while for transmissible mink encephalopathy, to several years BSE. consistence testaments sort CEP (Certificate Suitability). During 198...

Mice lacking expression of the prion protein are protected against infection with prion disease. Neurodegeneration in prion disease requires the formation of the abnormal isoform of the prion protein (PrP(Sc)) from host prion protein. Therefore expression of normal host prion protein is necessary for prion disease. In the present investigation, it was demonstrated that PrP(Sc) and a peptide res...

Prion-linked diseases, such as mad cow disease, scrapie, and the human genetic disorder Creutzfeldt-Jakob disease, are fatal neurodegenerative diseases correlated with changes in the secondary structure of neural prion protein. We expressed recombinant chicken prion protein in Escherichia coli and purified the protein to homogeneity. Circular dichroism spectra of the 26 kDa recombinant protein ...

The cellular prion protein has been identified as a metalloprotein that binds copper. There have been some suggestions that prion protein also influences zinc and manganese homeostasis. In this study we used a series of cell lines to study the levels of zinc and manganese under different conditions. We overexpressed either the prion protein or known transporters for zinc and manganese to determ...

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...