The aging lineage of budding yeast is differentiated by an early-appearing protein deposit that promotes protein quality control.

The equilibrium between solubility and aggregation of proteins in the nucleus is controlled by co-aggregates like RNA and the action of ATP as both an energy source and a destabilizing chemical agent.

Endoplasmic reticulum (ER) inheritance regulation during ER stress controls the transmission of misfolded ER proteins from mother to daughter cell in budding yeast.

Myofibril diameter is set by the controlled oligomerization of the PDZ and LIM domain protein Zasp in Drosophila.

Age-dependent protein aggregation closely resembles protein aggregation associated with neurodegenerative diseases and other amyloidoses, and initiates early functional decline in different tissues.

A theoretical basis for the spatial regulation of protein aggregation shows how aggregates can partition preferentially into intracellular liquid compartments.

Prion-like transfer of mutant huntingtin aggregates from presynaptic to postsynaptic neurons is enhanced by neuronal silencing and requires passage through the cytoplasm of Draper-expressing phagocytic glia in adult Drosophila brains.

Cryo-electron tomography reveals how a chaperone protein called TRiC reduces the ability of pathogenic mutant huntingtin proteins to form aggregates.

Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.

The bacterium Escherichia coli possesses a permissive cytoplasmic environment and the requisite molecular machinery to support the propagation of prions.