Linking deep mutational scanning with engineered transcriptional reporters in human cell lines establishes a generalizable method for exploring pharmacogenomics, structure, and function across broad classes of drug receptors.

The minimal twister sister (TS)-like self-cleaving ribozymes, revealed by deep mutational scanning, represent some of the very few human/primate ribozymes.

Deep mutational scanning was used to comprehensively quantify the effects of mutations to influenza hemagglutinin and shows that the virus possesses a high inherent mutational tolerance at key antigenic sites.

By measuring the impacts of thousands of mutations on potassium channel trafficking and function, we illuminate the molecular basis of folding, structure–function relationships, and how these are altered in disease.

Deep mutational scanning of Env proteins from two transmitted-founder strains of HIV shows how the accessible evolutionary space changes as the virus evolves.

An unbiased mutational screen decodes the molecular basis of phage receptor interactions, identifies key functional regions determining activity and host range, and demonstrates the potential for engineering therapeutic phages.

Deep mutational scanning of homologous proteins shows conservation in allosteric mechanisms but differences in molecular details within the protein family.

Comprehensive mutational characterisation of VIM-2 metallo-beta-lactamase deciphered the residues responsible for key functional behavior, including translocation, stability, substrate recognition and catalysis.

Endoplasmic reticulum proteostasis factors enhance the mutational tolerance of influenza hemagglutinin, a model secretory pathway protein and therapeutic target, particularly improving the fitness of temperature-sensitive variants.

Deep mutational scanning reveals interactions in the MET kinase domain that are critical for regulation and cancer-related signaling.