A deep mutational scan of the ADAR2 deaminase domain creates a map for designing tailored ADAR2 variants, and splitting the deaminase between residues 468 and 469 enables highly transcript-specific RNA editing.

Chemical perturbation-dependent deep mutational scanning data collected by a lab-based interdisciplinary graduate class resolves a paradox between the high evolution conservation and the high mutational tolerance of the protein ubiquitin.

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.

The absolute affinities of thousands of variant antibodies are measured in parallel using a combination of cell sorting and high-throughput DNA sequencing.

The innate immune protein PKR, which is inhibited by viral proteins that mimic its natural substrate, has access to a wide spectrum of inhibitor-evading mutations that maintain natural substrate binding.

Comprehensive analyses of how mutations in a picornavirus capsid affect viral fitness provide novel insights into viral biology, evolution, and host interactions.

Many of the synergistic interactions between mutations are modified in the context of unstable proteins in a manner that depends on how the variants promote misfolding in the cell.

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.