Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

Abnormal assembly of tau, α-synuclein, TDP-43 and amyloid-β proteins into amyloid
filaments defines most human neurodegenerative diseases. Genetics provides a direct link …

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 …

Abundant filamentous inclusions of tau are characteristic of more than 20
neurodegenerative diseases that are collectively termed tauopathies. Electron cryo …

Intermediate species in the assembly of amyloid filaments are believed to play a central role
in neurodegenerative diseases and may constitute important targets for therapeutic …

Strong genetic evidence supports an imbalance between production and clearance of
amyloid β-protein (Aβ) in people with Alzheimer disease (AD). Microglia that are potentially …

Recent Aβ-immunotherapy trials have yielded the first clear evidence that removing
aggregated Aβ from the brains of symptomatic patients can slow the progression of …

Biomolecular condensates, membrane-less entities arising from liquid–liquid phase
separation, hold dichotomous roles in health and disease. Alongside their physiological …

Many age-dependent neurodegenerative diseases, such as Alzheimer's and Parkinson's,
are characterized by abundant inclusions of amyloid filaments. Filamentous inclusions of the …

The seeded growth of pathogenic protein aggregates underlies the pathogenesis of
Alzheimer's disease (AD), but how this pathological cascade is initiated is not fully …