Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.

Msp1, a membrane-integral AAA ATPase at mitochondria and peroxisomes, selectively recognizes uncomplexed substrate molecules in vivo while avoiding substrates stabilized by binding partners.

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.

Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.

A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.

A 3.2 Å resolution structure of Vps4 provides a detailed model for protein substrate binding and translocation by AAA ATPases.

The projections from discrete areas to motor cortex increase over disease course in motoneuron disease model with selective spatial and temporal patterns.

TRIP13 inactivates the spindle assembly checkpoint by converting MAD2 from its active ‘closed’ state to its inactive ‘open’ state.

Msp1 recruits substrates at the open seam of the spiral oligomer and extracts them with functionally adapted elements.