A generalizable approach to understanding the logic of molecular recognition reveals the contributions of individual residues to the specificity of protein-protein interactions.

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

Forcing protein associations across the proteome reveals the cell's tolerance for diverse protein interactions and reveals the interactions that affect growth.

A biosensor resource has been developed to monitor the intracellular interactions of RAS family proteins with effector molecules and the effects of inhibitors as an aid to drug development.

The resurrection of ancient ancestral intrinsically disordered proteins reveals the evolution of a protein-protein interaction in molecular detail.

An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.

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

Affinity capture of polyribosomes followed by RNAseq(ACAPSeq) is a technique that harnesses massively parallel sequencing to identify protein-protein interactions from any source from which polyribosomes can be purified.

Generation of a new fly line library for analysing protein–protein interactions in vivo.

The placement of single methyl groups at certain positions in the sequence of small model transmembrane proteins consisting solely of leucines and isoleucines can modulate highly specific, productive interactions with the transmembrane domain of the erythropoietin receptor.