The N-terminal domains enable Lon protease to discriminate and capture selected protein species for degradation by exposed hydrophobic patches and flexible linkages to the hexameric core complex.

Structural, biochemical, and proteomic analyses of a four-subunit core module of the cleavage and polyadenylation specificity factor complex reveal its molecular architecture and specific determinants of polyadenylation signal recognition in human mRNAs.

Structure-guided biochemistry defines how the coupling between nucleic acid substrate binding and ATPase activity is used by a molecular switch to load ring-shaped motor proteins onto single-stranded DNA.

A plant immune receptor evolved recognition of caterpillar peptides through key molecular changes.

A generalizable approach to understanding the logic of molecular recognition reveals the contributions of individual residues to the specificity of protein-protein interactions.

A technique called selected reaction monitoring can quantitatively detect highly diversified protein isoforms and their association with specific neuronal structures and complexes.

Allostery holds critical role in CRISPR-Cas9 specificity enhancement.

Structure/function studies of a plant pathogen effector in complex with a host disease resistance protein domain reveal the molecular basis for recognition and underpin future engineering of immunity in crops.

First structural view of a substrate-bound PIKK (PI3K-related-kinase) by cryo-EM explains phosphorylation specificity toward a short amino-acid motif shared across the PIKK family and rationalizes PIKK auto-inhibition by regulatory domain.

As a cell prepares to divide, a molecular actor known as the Origin Recognition Complex makes intricate ATP-driven movements to recruit proteins required to duplicate DNA.