The molecular mechanism behind how emetine inhibits the ribosome of the human malaria parasite, along with structural details of the complex formed, is revealed at high resolution using cryo-electron microscopy.

The pro-apoptotic BH3-protein Bim contains two distinct binding sites for anti-apoptotic proteins that together confer resistance of Bim/Bcl-2 and Bim/Bcl-XL complexes to BH3-mimetic drugs under development for use in humans.

The cellular and molecular substrates that underlie the programmed behavioral response to a gustatory sex pheromone have been identified.

Cryo-electron microscopic structures of 5-HT₃A receptor in complex with first and second generations of clinically used setron reveal the molecular basis for their binding modes and mechanisms of inhibitory action.

A second anti-apoptotic protein binding site in PUMA confers resistance to BH3 mimetic drugs and binds the protein to membranes.

A small RNA molecule called miR-124 controls pheromone production and sexual behaviour in Drosophila by regulating sex-specific gene expression in males.

Multi-body refinement in RELION allows high-resolution reconstruction and visualisation of molecular motions in cryo-EM single-particle data sets with continuous forms of structural heterogeneity.

Minimal genetic modifications of endogenous mosquito genes allow the tissue-specific expression of anti-malarial effectors and convert them into efficient non-autonomous gene drives.

A high-throughput, activity-based selection identifies many phage-derived inhibitors of Cas9 from human fecal and oral metagenomes, with at least one inhibitor acting via a novel mechanism.

Analyses of detailed clinical and entomological data from cohort studies reveal how anti-parasite and anti-disease immunity against P. falciparum develop as a function of age and transmission intensity.