Prion Protein Scrapie and the Normal Cellular Prion Protein [PDF]
Prion, 2015 Prions are infectious proteins and over the past few decades, some prions have become renowned for their causative role in several neurodegenerative diseases in animals and humans.
Munn, Alan L +7 more
core +4 more sources
Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles. [PDF]
PLoS Pathogens, 2006 Transmission of prions between species is limited by the "species barrier," which hampers a full characterization of human prion strains in the mouse model.
Romolo Nonno +14 more
doaj +3 more sources
Prion protein and prion disease at a glance [PDF]
Journal of Cell Science, 2021 ABSTRACT Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the
Zhu, Caihong, Aguzzi, Adriano
openaire +3 more sources
Frontiers in Cell and Developmental Biology, 2014 The cellular prion protein (PrP(C)) has been widely investigated ever since its conformational isoform, the prion (or PrP(Sc)), was identified as the etiological agent of prion disorders. The high homology shared by the PrP(C)-encoding gene among mammals, its high turnover rate and expression in every tissue strongly suggest that PrP(C) may possess key
Gasperini, Lisa, Legname, Giuseppe
openaire +4 more sources
Prion protein self-peptides modulate prion interactions and conversion [PDF]
, 2009 Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A. +12 more
core +1 more source
Prions and Prion-like Proteins [PDF]
Journal of Biological Chemistry, 2014 Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen.
openaire +2 more sources
Conformational conversion of prion protein in prion diseases [PDF]
Acta Biochimica et Biophysica Sinica, 2013 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.
Zheng, Zhou, Gengfu, Xiao
openaire +2 more sources
Early increase and late decrease of purkinje cell dendritic spine density in prion-infected organotypic mouse cerebellar cultures. [PDF]
PLoS ONE, 2013 Prion diseases are infectious neurodegenerative diseases associated with the accumulation of protease-resistant prion protein, neuronal loss, spongiform change and astrogliosis.
Jody L Campeau +4 more
doaj +1 more source
Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases
Viruses, 2021 Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death.
Zoe J. Lambert +3 more
doaj +1 more source
Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro [PDF]
, 2007 Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrPSc, an aberrant conformer of a normal cellular protein PrPC.
Oxley, David +9 more
core +1 more source