Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Assembly of microtubule-associated protein tau into filamentous inclusions underlies a
range of neurodegenerative diseases. Tau filaments adopt different conformations in …

It is now generally accepted that macromolecules do not act in isolation but “live” in a
crowded environment, that is, an environment populated by numerous different molecules …

The ordered assembly of Tau protein into abnormal filamentous inclusions is a defining
characteristic of many human neurodegenerative diseases. Thirty years ago, we reported …

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 …

The constituent paired helical filaments (PHFs) in neurofibrillary tangles are insoluble
intracellular deposits central to the development of Alzheimer's disease (AD) and other …

Aggregation of the microtubule-associated protein Tau is a hallmark of Alzheimer's disease
with Tau oligomers suspected as the most toxic agent. Tau is a client of the molecular …

Misfolding of the microtubule-binding protein tau into filamentous aggregates is
characteristic of many neurodegenerative diseases such as Alzheimer's disease and …

Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in
the aggregation process leading to the formation of insoluble intraneuronal fibrils within …

The accumulation of hyperphosphorylated fibrillar Tau aggregates in the brain is one of the
defining hallmarks of Tauopathy diseases, including Alzheimer's disease. However, the …