Many protein and nucleoprotein complexes exist as helical polymers. As a result, much effort
has been invested in develo** methods for using electron microscopy to determine the …

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 …

Predicting protein interactions in the cellular environment still remains a challenge in the
AlphaFold era. Protein interactions, similarly to their structures, sample a continuum from …

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 …

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

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

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

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

We used electron cryo-microscopy (cryo-EM) to determine the structures of Aβ40 filaments
from the leptomeninges of individuals with Alzheimer's disease and cerebral amyloid …

Tau protein misfolding and aggregation are pathological hallmarks of Alzheimer's disease
and over twenty neurodegenerative disorders. However, the molecular mechanisms of tau …