Amyloid fibrils are cross-β–rich aggregates that are exceptionally stable forms of protein
assembly. Accumulation of tau amyloid fibrils is involved in many neurodegenerative diseases, …

Tau protein in vitro can undergo liquid–liquid phase separation (LLPS); however, observations
of this phase transition in living cells are limited. To investigate protein state transitions in …

Alzheimer's disease (AD) is characterized by the presence of tau filaments in the brain whose
structure was recently solved. The formation of AD filaments is routinely modeled in vitro …

G protein-coupled receptors (GPCRs) have long been shown to exist as oligomers with
functional properties distinct from those of the monomeric counterparts, but the driving factors of …

The aggregation of the tau protein is central to several neurodegenerative diseases,
collectively known as tauopathies. High-resolution views of tau tangles accumulated under …

Prion-like spread of disease-specific tau conformers is a hallmark of all tauopathies. A 19-residue
probe peptide containing a P301L mutation and spanning the R2/R3 splice junction of …

Prion-like spread of disease-specific tau conformers is a hallmark of all tauopathies. We
used a 19-residue probe peptide spanning the R2/R3 splice junction of tau to induce …

In the Tauopathy subfamily of neurodegenerative diseases, the intrinsically disordered
protein (IDP), Tau, undergoes a transition from its native disordered state into insoluble, …

The recent discovery by cryo-electron microscopy that the neuropathological hallmarks of
different tauopathies, including Alzheimer's disease, corticobasal degeneration (CBD), and …

G protein-coupled receptors (GPCRs) have long been shown to exist as oligomers with
functional properties distinct from those of the monomeric counterparts, but the driving factors of …