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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.

A novel high-throughput method for measuring many weak protein-peptide affinities simultaneously reveals how calcineurin, a human phosphatase essential for the immune response, recognizes its peptide substrates.

Pre-existing enhancers interpret T cell signaling strength in an analogue manner to direct quantitative changes in gene expression within the context of an overall digital response.

The study of the interactions between 65,356 variants of the SARS-CoV-2 receptor binding domain and a panel of monoclonal antibodies shows that Omicron’s escape is driven by a small number of large effect mutations.

DNA motifs tuned for low affinity binding of BMP-induced pMad/Medea transcription factors function to restrict gene activation to small subsets of the many Drosophila neurons that exhibit active BMP signaling.

Faster ligand-binding kinetics of integrin low-affinity states suggests that integrin binding to ligand and intracellular adapters and the actin cytoskeleton precedes their stabilization, together with tensile force, of the high-affinity, extended-open integrin conformation.

Both the polypeptide and attached O-glycans N-terminal to the A1 domain in von Willebrand factor lower its affinity for its ligand GPIbα on platelets, its stability, and structural dynamics and decrease population of a high-affinity, intermediate state in unfolding.

ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.

Characterization of Ca²⁺ selectivity and non-conductance mechanism induced by pore mutation N617D in the skeletal muscle DHPR.

A method for measuring p300 chromatin occupancy in specific lineages of mouse tissues was used to map endothelial enhancers and to identify previously unrecognized angiogenesis-related sequence motifs.