Covalent modification of engineered cysteines in the nicotinic acetylcholine receptor agonist-binding domain inhibits receptor activation.
Visual identification of individual transfected cells for electrophysiology using antibody-coated beads.
An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding.
Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism.
A novel K+ channel with unique localizations in mammalian brain: molecular cloning and characterization.
