A molecular understanding of the prion diseases requires delineation of the origin of
misfolding of the prion protein (PrP). An understanding of how different disease‐linked …

Prion diseases are a group of fatal neurodegenerative disorders that manifest as infectious,
sporadic, or familial and are all associated with the misfolding of the prion protein (PrP) …

Delineation of the effects of pathogenic mutations linked with familial prion diseases on the
structure and misfolding of prion protein (PrP) will be useful in understanding the molecular …

The structural conversion of the prion protein PrP into a transmissible, misfolded form is the
central element of prion disease, yet there is little consensus as to how it occurs. Key …

The misfolding of the prion protein (PrP) to aggregated forms is linked to several
neurodegenerative diseases. Misfolded oligomeric forms of PrP are associated with …

Intermediate states are key to understanding the molecular mechanisms governing protein
misfolding. The human prion protein (PrP) can follow various misfolding pathways, and …

Protein misfolding is a ubiquitous phenomenon associated with a wide range of diseases.
Single-molecule approaches offer a powerful tool for deciphering the mechanisms of …

Transmissible spongiform encephalopathies in mammals are believed to be caused by
PrPSc, the insoluble, oligomeric isoform of the cellular prion protein PrPC. PrPC and the …

To identify and structurally characterize the precursor conformation of the prion protein (PrP),
from which misfolding and aggregation directly commence, has been a long-standing goal …

Misfolding of the prion protein is linked to multiple neurodegenerative diseases. A better
understanding of the process requires the identification and structural characterization of …