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...

the molecular dynamics (md) simulation method is used to assess structural details for humanprion protein (hereafter prpn) and its asp178 asn mutant (hereafter prpm) which causes fatalfamilial insomnia disease. the results reveal that the flexibility and instability increase in prpmcould be related to specific amino acids exposed to the solvent. solvation free energy of prpm is 20kjmot1nni2 mor...

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...

The risks posed to human health by individual animal prion diseases cannot be determined a priori and are difficult to address empirically. The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein to its pathologic isoform. We used a rapid molecular conversion assay (protein misfolding cyclic amplification) to test whether brain homogena...

protein aggregation is a serious problem for both biotechnology and cell biology. diseases such as prion misfolding, alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutati...

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...

An unusual molecular structure of the prion protein, PrPsc is found only in mammals with transmissible prion diseases. Prion protein stands for either the infectious pathogen itself or a main component of it. Recent studies suggest that autophagy is one of the major functions that keep cells alive and has a protective effect against the neurodegeneration. In this study, we investigated that the...

Transgenic mice expressing human prion protein in the absence of endogenous mouse prion protein faithfully replicate human prions. These models reproduce all of the key features of human disease, including long clinically silent incubation periods prior to fatal neurodegeneration with neuropathological phenotypes that mirror human prion strain diversity. Critical contributions to our understand...