The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.

Adapting a cytosolic enzyme that breaks down glutathione to function in the lumen of the endoplasmic reticulum challenges the long-held view that reduced glutathione fuels disulfide rearrangements during protein folding.

N-glycans commonly present in the protease domains are required for calnexin-mediated protein folding and intracellular trafficking.

Neuronal ELAV-like (nELAVL) proteins are associated with non-coding Y RNAs in stressed neurons and in the brains of Alzheimer's disease patients, suggesting a new means of regulatory protein sequestration and mRNA target regulation.

How the process of protein folding may be controlled by the Sec machinery to assist protein transport across membranes.

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

Building on previous work (Mysling et al., 2016), it is shown that angiopoietin-like protein 4 (ANGPTL4) inhibits lipoprotein lipase activity by catalyzing the unfolding of its hydrolase domain.

Proteins can fold deeper inside ribosomes with an enlarged exit tunnel.

Pulsed-labeling hydrogen exchange on the ribonuclease H family show that the major folding intermediate is conserved over three billion years of evolution, but the path leading to this intermediate varies.

Cohesin loading at centromeres depends on a conserved surface cluster of amino-acid residues on the cohesin loading protein, Scc4.