title: Deeper Insights into the Allosteric Modulation of Ionotropic Glutamate Receptors.
abstract: Two articles in this issue of Neuron (Yelshanskaya et al., 2016; Yi et al., 2016) explore the structural basis of allosteric inhibition in ionotropic glutamate receptors, providing key insights into how iGluRs function in the brain as well as how they might be pharmacologically modulated in neurological disorders and disease.
authors.affiliation: W.M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, One Bungtown Road, Cold Spring Harbor, NY 11724, USA.
authors.forename: Michael C
authors.initials: MC
authors.lastname: Regan
authors.affiliation: W.M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, One Bungtown Road, Cold Spring Harbor, NY 11724, USA. Electronic address: furukawa@cshl.edu.
authors.forename: Hiro
authors.initials: H
authors.lastname: Furukawa
mesh_terms: D001921:Brain; D006801:Humans; D009474:Neurons; D017470:Receptors, Glutamate; D058468:Receptors, Ionotropic Glutamate / Q000737:chemistry*
chemical_list: D017470:Receptors, Glutamate; D058468:Receptors, Ionotropic Glutamate