A DNA–protein complex can find target sequences of bases in another DNA molecule by sliding along it.

A bacterial protein can be programmed with short RNA molecules to stimulate genome editing at specific sites in human cells.

Fluorescence resonance energy transfer has been used to explore the interactions between DNA polymerases, sliding clamps and clamp loaders as DNA is replicated in human cells.

COPII vesicles regulate the metabolism of cholesterol through the selective transport of secretory proteins.

Some of the mutations that occur during influenza evolution can only be tolerated in conjunction with other mutations that increase the stability of a viral protein.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Computer simulations reveal that viral nucleic acids have an ideal structure for being packaged into outer protein shells called capsids.

A modified form of Green Fluorescent Protein integrated into an ammonium transporter provides a sensor that can be used to monitor transport activity in vivo.

A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

Proteins implicated in Alzheimer’s disease, including amyloid precursor protein and ApoE receptors, interact with each other and with a signalling molecule called agrin to influence the development of the neuromuscular junction.