A cargo recognition α-helix was identified in Nup358, which is required for activation of a dynein-dependent transport pathway that is essential for brain development.

The details of how the enzyme DNA polymerase α initiates the polymerization of nucleotides in DNA replication, a critical step in the synthesis of new chromosomal DNA, have been revealed in atomic detail.

Simple insertions switch α-helical coiled coils into a novel fibrous protein fold that is periodically interspersed with short β-strands.

Input from computational models has enabled the detection of allosteric communication that modulates the gating mechanism of a bacterial outer-membrane protein.

Structures of CdiB outer membrane transporters reveal the channel-gating mechanism for the secretion of large bacterial toxins.

Deleting the first helix of the α-catenin actin-binding domain results in a slip bond interaction between the cadherin–catenin complex and F-actin, such that the binding interaction is stable at low force.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

The structure of the VemP-stalled ribosome reveals a helix-double turn-helix conformation of the nascent chain within the ribosomal tunnel, illustrating how secondary structure formation directly at the peptidyltransferase center of the ribosome can induce translational arrest.

The in-depth structural and functional work provide a deeper understanding as to how the epithelial sodium channel is a heteromeric ion channel that is regulated by Na⁺ and proteolysis.

Cryo-EM and X-ray structures of α-xenorhabdolysin in soluble and pore form of Xenorhabdus nematophila give novel insights into the mechanism of action of bi-component α-pore-forming toxins.