Deep mutagenesis reveals that mutations rarely alter the inclusion of highly-included exons.

A massively parallel analysis of the effects of mutations on amyloid beta nucleation provide the first comprehensive atlas of how mutations alter the formation of amyloid fibrils.

Deep mutagenesis of a clamp-loader complex reveals a critical hydrogen-bonded junction that is important for allosteric communication in oligomeric AAA+ ATPases.

A high-throughput technique to characterize the substrate specificities of tyrosine kinases identifies the key features of kinases and substrates that enforce accurate signaling from T cell receptors.

Deep mutagenesis experiments demonstrate that while cancer-causing mutations in Ras selectively alter regulatory interactions with GTPase-activating proteins, Ras is also activated by many mutations that decrease protein stability.

A deep mutational coupling study demonstrates the ability of sequence coevolution methods to reveal the pattern of amino acid interactions underlying protein function.

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

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

Experimental determination of residue contacts from mutational data allows model discrimination and identification of in vivo functional conformations of proteins.

Gene knock-out of the omega-1 ribonuclease of Schistosoma mansoni eggs resulted in immunologically impaired phenotype, showcasing the novel application of CRISPR/Cas9 genome editing and utility for functional genomics in schistosomes.