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 …

Converging evidence continues to point towards Tau aggregation and pathology formation
as central events in the pathogenesis of Alzheimer's disease and other Tauopathies …

A wide range of macromolecules can undergo phase separation, forming biomolecular
condensates in living cells. These membraneless organelles are typically highly dynamic …

Many intrinsically disordered proteins (IDPs) may undergo liquid–liquid phase separation
(LLPS) and participate in the formation of membraneless organelles in the cell, thereby …

Condensed states of proteins, including liquid-like membraneless organelles and solid-like
aggregates, contribute in fundamental ways to the organisation and function of the cell …

Exosomes may mediate cell-to-cell communication by transporting various proteins and
nucleic acids to neighboring cells. Some protein and RNA cargoes are significantly enriched …

The formation and viscoelastic properties of condensates of intrinsically disordered proteins
(IDPs) is dictated by amino acid sequence and solution conditions. Because of the …

Aggregation of the microtubule-associated protein tau plays a major role in Alzheimer's
disease and several other neurodegenerative disorders. An exciting recent development is …

A multitude of cellular processes involve biomolecular condensates, which has led to the
suggestion that diverse pathogenic mutations may dysregulate condensates. Although proof …

Liquid–liquid phase separation (LLPS) of proteins into biomolecular condensates has
emerged as a fundamental principle underpinning cellular function and malfunction. Indeed …