Prion diseases share common clinical and pathological characteristics such as spongiform
neuronal degeneration and deposition of an abnormal form of a host-derived protein, termed …

Prions, which cause fatal neurodegenerative disorders such as Creutzfeldt‐Jakob disease,
are misfolded and infectious protein aggregates. Currently, there are no treatments available …

Recent computational advancements in the simulation of biochemical processes allow
investigating the mechanisms involved in protein regulation with realistic physics-based …

The prion protein (PrPC) is a central player in neurodegenerative diseases, such as prion
diseases or Alzheimer's disease. In contrast to disease-promoting cell surface PrPC …

PrP Sc, a misfolded, aggregation-prone isoform of the cellular prion protein (PrP C), is the
infectious prion agent responsible for fatal neurodegenerative diseases of humans and …

Prion diseases arise from the conformational conversion of the cellular prion protein (PrPC)
into a self-replicating prion isoform (PrPSc). Although this process has been studied mostly …

Introduction Prion diseases are rare and fatal neurodegenerative disorders. The key
molecular event in these disorders is the misfolding of the physiological form of the cellular …

The in vitro degradation profile and the cytotoxicity of the degradation products of a silk
fibroin (SF)-based nerve conduit (SilkBridge), with a complex three-layered wall architecture …

Prion diseases are neurodegenerative disorders caused by misfolded prion proteins.
Although rare, the said diseases are always fatal; they commonly cause death within months …

Prions are deadly infectious agents made of PrP Sc, a misfolded variant of the cellular prion
protein (PrP C) which self-propagates by inducing misfolding of native PrP C. PrP Sc can …