The identification of a conserved α-helical domain in monkeypox virus H3 protein as critical for heparan sulfate binding unveils a novel therapeutic target, validated through AI and molecular dynamics simulations, offering potential for broad-spectrum antiviral development.

Enterovirus A71 adaptation to bind heparan sulfate as receptor comes with compensation that destabilizes its virus capsid.

Single-molecule tracking at scale, analyzing millions of cells and thousands of compounds per day, demonstrates that measuring protein motion provides mechanistic insights relevant to drug discovery.

A single amino acid change in a neuronal ion channel called KCNQ2 blocks ion flow, prevents protein localization on axons, and results in severe epilepsy and slowed neurological development.