Various genotoxic stresses trigger widespread aggregation of abundant, liquid-liquid phase separation-prone proteins, suggesting that genotoxic stress is a potential driver of disease-associated protein aggregation.

Protein biosynthesis and protein quality control jointly determine protein production costs.

A comprehensive analysis of yeast mutants has provided clues to understanding the physiological conditions caused by protein overexpression.

The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.

DynAPs reveal that biological phase separation provides the organizing principle for the complex process of dynein motor assembly in cells with motile cilia.

Dysregulated erythroblast-specific iron trafficking and regulation of iron metabolism provides evidence of a novel potential therapeutic target to reverse ineffective erythropoiesis in MDS.

Endothelial dysfunction due to cardiovascular disease risk factors explained by cardiac endothelial cell transcriptome remodelling.

Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.

The co-chaperone CHORDC1 is specifically required for epidermal growth factor receptor trafficking and signaling in Caenorhabditis elegans and in human cells.

Mechanistic insight into the chaperone-like activity of NMNAT to phosphorylated Tau reveals a connection between NAD⁺metabolism and Tau homeostasis.