Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

Upon the emergence of SARS-CoV-2 in the human population, it was conjectured that for
this coronavirus the dynamic intra-host heterogeneity typical of RNA viruses would be toned …

Abnormal behavior of α-synuclein and prion proteins is the hallmark of Parkinson's disease
(PD) and prion illnesses, respectively, being complex neurological disorders. A primary …

Since prion diseases result from infection and neurodegeneration of the central nervous
system (CNS), experimental characterizations of prion strain properties customarily rely on …

Recent developments in atomic force microscopy (AFM) image analysis have made three-
dimensional (3D) structural reconstruction of individual particles observed on 2D AFM height …

Amyloid-beta (Aβ42) aggregates are characteristic Alzheimer's disease signatures, but
probing how their nanoscale architectures influence their growth and decay remains …

Prions replicate via the autocatalytic conversion of cellular prion protein (PrP C) into fibrillar
assemblies of misfolded PrP. While this process has been extensively studied in vivo and in …

Structural polymorphism has been demonstrated for both in vitro and ex vivo amyloid fibrils
associated with disease. The manner in which different filament structures are assembled …

Simple Summary Prions are novel infectious agents that consist only of protein. It is known
that in the same host species, different strains of prion can occur that differ by the cells that …

Protein aggregation in the form of amyloid fibrils has long been associated with the onset
and development of various amyloidoses, including Alzheimer's, Parkinson's or prion …