Structure-led protein engineering can expand the effector recognition profile of plant intracellular NLR immune receptors, providing a proof-of-principle for the development of novel disease resistance mechanisms in plants.

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.

Legionella effector RavZ evades host autophagy by extracting LC3-PE from the membrane before deconjugation.

A biosensor resource has been developed to monitor the intracellular interactions of RAS family proteins with effector molecules and the effects of inhibitors as an aid to drug development.

Development, validation, and use of an effector membrane translocation biosensor platform reveals G protein coupling selectivity signatures for 100 GPCRs that range from remarkable selectivity to full promiscuity toward the different G protein subtypes.

Structural and biochemical analysis of a protein called Ecp6, which is produced by a tomato fungus, reveals how the protein prevents plants from launching an immune response to the chitin in fungal cell walls.

A plant pathogen effector evolved a short linear motif to subvert autophagic defenses by antagonising a host cargo receptor.

Lentiviral protein transduction offers a new approach for administration of custom-designed nucleases, leading to high-efficacy targeted gene editing and reduced off-target activity after virus-directed delivery of programmable nuclease proteins.

A G protein in striatal neurons forms preassembled complexes with its downstream enzyme, adenylyl cyclase, which has implications for the pathophysiology of movement disorders.

Comparative structural studies reveal how the cytoplasmic tails of Eph receptors can differentiate different downstream target proteins via highly specific SAM–SAM domain interactions.