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TRPV channels share general mechanisms of activation while exhibiting subtype-specific features along the activation pathway that can determine their apparent sensitivity to stimuli.

A comprehensive allosteric model describes how inhibitors can activate rather than inhibit a target kinase by selectively driving formation of kinase dimers with one inhibited and one activated subunit.

Regulation of phosphoinositide 3 kinase (PI3Kγ) is essential in immune function, and stimuli that modulate the dynamics of the PI3Kγ helical domain can activate or inhibit kinase activity.

Rigorous biophysical studies reconcile several conflicting views on how cGAS is activated, and present a new unifying allosteric activation mechanism.

Whole endosome recording shows that chloride interacts with vesicular glutamate transporters as both allosteric activator and permeant ion, and although the mode of permeation differs, chloride and glutamate use a related conduction pathway.

Epigenetic modifications to DNA can regulate E3 ubiquitin ligase activity in human cells.

Functional analysis reveals a distinct mode of action of the allosteric modulators in the GABA_B receptor in a pocket that is formed only in the active state and identifies a region in the GABA_B2 subunit important for allosteric agonism.

Phosphorylation of Aurora A does not trigger a population shift to the active state as previously thought, but instead switches the kinase on by tuning the structure and dynamics of a dynamically sampled subpopulation.

The full-length structures of the mammalian nitric oxide receptor reveal the molecular activation steps and a binding site for the prototype of FDA-approved stimulators.

In mGlu heterodimers, an oriented asymmetrical activation revealed complex allosteric interaction between subunits.