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.

Motif length plays a critical role in the specification of biological function within a conserved family of RNA-binding proteins.

The LOVdeg tag is a versatile tool for bacterial optogenetics, offering modular, blue light-inducible protein degradation for a range of synthetic biology and metabolic engineering applications.

Light-sensitive allosteric switch module, a broadly applicable protein engineering method, is used for the regulation of protein activity with tight temporal control and spatial precision.

Protein engineering of a reversibly switchable fluorescent protein enables post-hoc reversible and repeatable marking of elevated calcium concentrations using blue light.

Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.

Effector target-guided engineering has developed plant NLR immune receptors that bind and recognize stealthy pathogen effector proteins, demonstrating new disease resistance profiles in planta, and offering a promising approach to protect crops against plant pathogens.

Protein engineering and large-scale screening has led to the development of sensitive red fluorescent indicators that detect neural activity with high sensitivity in various animal models.

Two sets of modular components are sufficient to rewire MAPKs to regulate proteins through ubiquitination – a complementary pair of protein interaction domains and a phosphodegron.

Co-aggregation, amyloid formation, and unidirectional cross-seeding of prolactin and galanin for their efficient storage in secretory granules of pituitary and subsequent functional hormone release.