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.

The structure of a substrate-engaged AAA+ unfoldase suggests a model for processive unfolding that is supported by biochemical data.

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

A study of solute and macromolecule trafficking in plants reveals a previously undescribed route for carbon distribution in growing root tissues.

Studies of Lowe syndrome patient cells, which lack the inositol 5-phosphatase OCRL, suggest that a defect in endocytosis plays a role in the pathological manifestations of the disease.

Systematic analyses of DNA replication machinery components in human cells reveal a requirement of MCM-dependent de novo loading or mobilization of cohesin at replication forks in establishing sister-chromatid cohesion.

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.

HIV-1 capsids enter the host cell nucleus, where they are partially disrupted to release the viral genome upon completion of reverse transcription.

The mitochondrial protein unfoldase ClpX activates the first enzyme in heme biosynthesis, ALAS, by targeted unfolding that gates access of cofactor to the ALAS active site.

New biophysical methods and analyses visualize in real-time a chain of coordinated single-molecular events on a living cell, enabling the inner workings of a mechanoreceptor important to biology to be elucidated.