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.

Yeast populations lose mutational robustness during evolution in one environment but not in another due to the collective effect of a large number of idiosyncratic epistatic interactions.

Greater phenotypic variation is exposed by mutations in a gene regulatory system compared to mutations in its constitutive components, namely the transcription factor and the promoter, alone.

A complete mutational scan of a protein-DNA interface shows that pairwise epistatic interactions among amino acids determine a transcription factor's specificity for DNA and facilitate the evolution of new functions.

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

CR9114, one of the most broadly neutralizing anti-influenza antibodies characterized to date, acquires affinity to divergent HA subtypes sequentially, due to higher order interactions between the nested sets of mutations required for binding each distinct subtype.

Enzyme evolution is reversible on a structural and functional (phenotypic) level, but through a different mutational pathway that leads to genotypic incompatibility with the ancestor.

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

Orthologous proteins display different mutational robustness that can be leveraged to improve prediction of functional sequences.

A combined theoretical and experimental study revealed the mechanistic and structural basis of mutational effects on allostery and provided insights into the intrinsic connection of intra- and inter-domain properties.