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.

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.

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.

An exceedingly low speed limit was estimated for a helical hairpin formation by analyzing hours-long, incessant structural transitions.

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

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

Protein feeding stimulates the production of sex pheromones and promotes fly mating in Bactrocera dorsalis.

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

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.