The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Roughly one quarter of all genes code for integral membrane proteins that are inserted into
the plasma membrane of prokaryotes or the endoplasmic reticulum membrane of …

Nature programs the structural folding of an enzyme that allows its on-demand
biofunctionality; however, it is still a long-standing challenge to manually modulate an …

Liquid–liquid phase separation (LLPS) is a novel principle for explaining the precise spatial
and temporal regulation in living cells. LLPS compartmentalizes proteins and nucleic acids …

Ageing is a major risk factor for the development of many diseases, prominently including
neurodegenerative disorders such as Alzheimer disease and Parkinson disease. A hallmark …

Nature achieves differentiation of specific and nonspecific binding in molecular interactions
through precise control of biomolecules in space and time. Artificial systems such as …

Biomolecular condensates, membrane-less entities arising from liquid–liquid phase
separation, hold dichotomous roles in health and disease. Alongside their physiological …

Proteins that self-assemble into polyhedral shell-like structures are useful molecular
containers both in nature and in the laboratory. Here we review efforts to repurpose diverse …

The endoplasmic reticulum (ER) is an important site for protein folding and maturation in
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …

Abstract Chaperone-mediated autophagy (CMA), a proteolytic system contributing to the
degradation of intracellular proteins in lysosomes, is upregulated in tumors for pro …