cryo-EM reveals the properties of distinct conformations occupied during activation of the lipid scramblase nhTMEM16 and provides new insights into its interactions with the lipid environment.

L-amino acids are agonists of calcium-sensing receptor, and act jointly with calcium and phosphate ions to control receptor function.

Aurora A kinase, an anti-cancer drug target, can be activated by two independent mechanisms.

Several new magneto-mechanical and magneto-thermal mechanisms of ion channel activation in magnetogenetics are proposed that may explain some of the mysteries that challenge current understanding of the magnetogenetics experiments.

A combined FRET- and electrophysiology-based approach is used to study ATP/ADP ADP binding to the stimulatory nucleotide binding site of ATP-sensitive K+ channels and investigate their activation mechanism.

Closed-ring and open-spiral assembly of the multi-subunit neuronal kinase CaMKII suggest a mechanism for how active subunits shuttle between individual assemblies, propagating stimulatory signals.

Cryo-EM structures of 70S•RelA ribosome complexes reveal how cognate deacyl-tRNA activates RelA.

The structural basis for Her2's role as a dedicated heterodimerization partner for other EGFR family receptors is elucidated with long-timescale atomistic simulations.

Structural, computational and functional approaches reveal the role of an extended acidic chamber near the nucleotide binding site in activation of P2X3 receptor channels by divalent-bound ATP.