Abnormal accumulation of aggregated α-synuclein (α-Syn) is seen in a variety of
neurodegenerative diseases, including Parkinson's disease (PD), multiple system atrophy …

Neurons require unique subcellular compartmentalization to function efficiently. Formed
from proteins and RNAs through liquid–liquid phase separation, membraneless organelles …

As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large
conformational space. Certain conformations lead to aggregation prone and non …

Amyloid aggregation of tau protein is implicated in neurodegenerative diseases, yet its
facilitating factors are poorly understood. Recently, tau has been shown to undergo liquid …

Drosophila eggs are highly polarised cells that use RNA–protein complexes to regulate
storage and translational control of maternal RNAs. Ribonucleoprotein granules are a class …

Phase separation has long been observed within aqueous mixtures of two or more different
compounds, such as proteins, salts, polysaccharides and synthetic polymers. A growing …

Liquid‐liquid phase separation (LLPS) has recently emerged as a possible mechanism that
enables ubiquitin‐binding shuttle proteins to facilitate the degradation of ubiquitinated …

Biomolecular condensates play numerous roles in cells by selectively concentrating client
proteins while excluding others. These functions are likely to be sensitive to the spatial …

The genetics of human disease serves as a robust and unbiased source of insight into
human biology, both revealing fundamental cellular processes and exposing the …

Aggregation of α-Synuclein, possibly caused by disturbance of proteostasis, has been
identified as a common pathological feature of Parkinson's disease (PD). However, the …