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 …

Tau is well established as a microtubule-associated protein in neurons. However, under
pathological conditions, aberrant assembly of tau into insoluble aggregates is accompanied …

Post-translational modifications (PTMs) on tau have long been recognized as affecting
protein function and contributing to neurodegeneration. The explosion of information on …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

None of the proposed mechanisms of Alzheimer's disease (AD) fully explains the distribution
patterns of the neuropathological changes at the cellular and regional levels, and their …

Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Investigation of macromolecular structure and dynamics is fundamental to understanding
how macromolecules carry out their functions in the cell. Significant advances have been …

Liquid–liquid phase separation occurs via a multitude of transient, noncovalent, and
intermolecular interactions resulting in phase transition of intrinsically disordered …

Tau is a microtubule-associated protein responsible mainly for stabilizing the neuronal
microtubule network in the brain. Under normal conditions, tau is highly soluble and adopts …