Prion, or PrPSc, is the pathological isoform of the cellular prion protein (PrPC) and it is the
etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and …

We have compiled a comprehensive list of the articles published in the year 2000 that
describe work employing commercial optical biosensors. Selected reviews of interest for the …

The mechanisms underlying prion-linked neurodegeneration remain to be elucidated,
despite several recent advances in this field. Herein, we show that soluble, low molecular …

Prion diseases are associated with the conversion of the α-helix rich prion protein (PrPC)
into a β-structure-rich insoluble conformer (PrPSc) that is thought to be infectious. The …

The susceptibility of sheep to scrapie is known to involve, as a major determinant, the nature
of the prion protein (PrP) allele, with the VRQ allele conferring the highest susceptibility to …

Transmissible spongiform encephalopathies are fatal neurodegenerative diseases
associated with the accumulation of a protease-resistant form of the prion protein (PrP) …

Prions induce a fatal neurodegenerative disease in infected host brain based on the
refolding and aggregation of the host-encoded prion protein PrPC into PrPSc. Structurally …

Sheep is a unique example among mammalian species to present a strong correlation
between genotype and prion disease susceptibility phenotype. Indeed a well-defined set of …

Aggregation and misfolding of the prion protein (PrP) are thought to be the cause of a family
of lethal neurodegenerative diseases affecting humans and other animals. Although the …

In pathologies due to protein misassembly, low oligomeric states of the misfolded proteins
rather than large aggregates play an important biological role. In prion diseases the lethal …