Prion Diseases
نویسندگان
چکیده
Stanley Prusiner introduced the term prion (proteinaceous infectious particle) and proposed that the infectious agent in prion diseases is composed mainly or entirely of an abnormal conformation of an otherwise normal host-encoded glycoprotein called the prion protein (PrP)1. This hypothesis was initially greeted with great skepticism in the scientific community but then later was widely acknowledged to be true. Prusiner was awarded the 1998 Noble Prize for Science for his ground breaking research.
منابع مشابه
A Study on The Effect of Temperature on Human Prion Protein Structure through Molecular Dynamic Simulation
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...
متن کاملMechanistic prospective for human PrPC conversion to PrPSc: Molecular dynamic insights
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...
متن کاملConformational conversion of prion protein in prion diseases.
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform. However, pathogenic mutations, modifications as well as some cofactors, such...
متن کاملComputational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. The neurodegenerative diseases such as Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob diseases, Gerstmann-Sträussler-Scheinker syndrome, Fatal Familial Insomnia, Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (or ‘mad-cow’ disease) and chronic wasting dise...
متن کاملPrions: protein aggregation and infectious diseases.
Transmissible spongiform encephalopathies (TSEs) are inevitably lethal neurodegenerative diseases that affect humans and a large variety of animals. The infectious agent responsible for TSEs is the prion, an abnormally folded and aggregated protein that propagates itself by imposing its conformation onto the cellular prion protein (PrPC) of the host. PrPC is necessary for prion replication and ...
متن کاملYeast Model for Studying Heritable Mammalian Prion Disease
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are infectious fatal neurodegenerative disorders that include a variety of human diseases, such as CreutzfeldtJacob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), kuru and fatal familial insomnia [1, 2]. Mammalian prion protein (PrP) in an abnormal aggregation-prone selfperpetuating (prion) conformation has been...
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