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The local fitness landscape of an antigenic region in influenza neuraminidase was determined by combinatorial mutagenesis and next-generation sequencing.

Distinct surfaces of an interbacterial competition cell wall toxin mediate interactions with different cellular binding partners, resulting in an inherent evolutionary trade-off across the toxin superfamily.

Complete mapping of human-adaptive mutations to the avian influenza PB2 protein shows how selection at key molecular interfaces combines with evolutionary accessibility to shape viral host adaptation.

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

Deep mutational scanning provides new insights into how mutations alter the expression and activity of the potassium ion channel Kir2.1, which is associated with many diseases.

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.

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.

Deep mutational scanning of a synthetic allosteric chimera revealed that a sparse set of mutations on the protein surface improved regulation.

An approach called deep mutational scanning is improving our understanding of amyloid beta aggregation.

Environmental conditions strongly impact the fitness effects of Hsp90, resulting in the selection of Hsp90 sequences in nature that are robust to a variety of stressful conditions.