Macromolecular structure determination by electron cryo-microscopy (cryo-EM) is limited by
the alignment of noisy images of individual particles. Because smaller particles have weaker …

A defining pathological feature of most neurodegenerative diseases is the assembly of
proteins into amyloid that form disease-specific structures. In Alzheimer's disease, this is …

The landscape of pharmacological treatment for Alzheimer's disease (AD) has undergone
significant transformations with the advent of disease-modifying therapies (DMTs) targeting …

Mice transgenic for human mutant P301S tau are widely used as models for human
tauopathies. They develop neurodegeneration and abundant filamentous inclusions made …

The abnormal assembly of tau protein in neurons is a pathological hallmark of multiple
neurodegenerative diseases, including Alzheimer's disease (AD). Assembled tau associates …

Cryoelectron microscopy (cryo-EM) has provided unprecedented insights into amyloid fibril
structures, including those associated with disease. However, these structures represent the …

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

Recombinant proteins play pivotal roles in numerous applications including industrial
biocatalysts or therapeutics. Despite the recent progress in computational protein structure …

ATTR amyloidosis results from the conversion of transthyretin into amyloid fibrils that deposit
in tissues causing organ failure and death. This conversion is facilitated by mutations in …

Amyloid formation by α-synuclein (αSyn) occurs in Parkinson's disease, multiple system
atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn …