The range of molecular forms adopted by L1 retrotransposons reflect a tapestry of lifecycle-permissive and -restrictive host-parasite interactions occurring within cells.

This atlas and analysis of conserved ventromedial hypothalamic nucleus (VMH) neuron populations provides an unbiased starting point for the analysis of VMH circuitry and function.

The number of contacts at the interface of a protein–protein complex, together with the properties of the surface, provides a simple, but well-performing predictor of binding affinity.

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

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.

Efficient transcription from low-affinity enhancers is driven by nuclear microenvironments of transcription factors.

Common variants of the SARS-CoV-2 Spike protein and its ligand, the human ACE2 receptor, increase the binding affinity, suggesting that they could increase viral transmissibility.

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.

Affinity measurements of microRNA sites representing >1000 different pairing architectures reveal that two binding modes can mediate pairing to the microRNA 3′ region, and that microRNA G and oligo(G/C) residues are most impactful.

An anti-influenza receptor binding site antibody acquires breadth through hierarchical sets of epistatic mutations distributed across the light and heavy chains, demonstrating how mutations can interact to shape the evolution of antibody breadth in various antigen exposure regimens.