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Voltage-dependent block by Mg2+ of NMDA responses in spinal cord neurones
Using voltage-clamp experiments on mouse spinal cord neurones, it is shown that the voltage-sensitivity of NMDA action is greatly reduced on the withdrawal of physiological concentrations (∼1 mM) of Mg2+ from the extracellular fluid, providing further evidence that Mg 2+ blocks inward current flow through ion channels linked to NMDA receptors. Expand
Mechanism of glutamate receptor desensitization
Using the GluR2 AMPA-sensitive glutamate receptor, it is shown that the ligand-binding cores form dimers and that stabilization of the intradimer interface by either mutations or allosteric modulators reduces desensitization. Expand
Permeation and block of N‐methyl‐D‐aspartic acid receptor channels by divalent cations in mouse cultured central neurones.
Manganese both permeates and blocks the NMDA receptor channel, implying an apparent increase in PCa/PNa on lowering [Na+]o and may result from interaction of permeant ions within the channel. Expand
Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-D-aspartate and quisqualate receptors
Dose-response curves for activation of excitatory amino acid receptors on mouse embryonic hippocampal neurons in culture were recorded for 15 excitatory amino acids, including the L-isomers ofExpand
Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A
Northern blot analysis of mRNA for dorsal root ganglia revealed a predominant expression of GluR5, indicating that modulation of desensitization by concanavalin A but not cyclothiazide in sensory neurons accurately predicts subunit expression for native glutamate receptors. Expand
The physiology of excitatory amino acids in the vertebrate central nervous system
Abbreviations 198
AMPA Receptor Flip/Flop Mutants Affecting Deactivation, Desensitization, and Modulation by Cyclothiazide, Aniracetam, and Thiocyanate
The experiments demonstrate for the first time the functional importance of residue 750 in regulating intrinsic channel-gating kinetics and emphasize the biological significance of alternative splicing in the M3–M4 extracellular loop. Expand
Structure and function of glutamate receptor ion channels.
This paper presents a mechanistic explanation for the activation of channel gating by agonists and partial agonists; the process of desensitization, and its block by allosteric modulators, is mostly explained; and the basis of receptor subtype selectivity is emerging with clarity as more and more structures are solved. Expand
Structural basis for partial agonist action at ionotropic glutamate receptors
Findings from crystallographic and electrophysiological studies of the mechanism of activation of an AMPA-subtype glutamate receptor ion channel are reported, showing that the GluR2 ligand-binding core can adopt a range of lig and-dependent conformational states, which in turn control the open probability of discrete subconductance states of the intact ion channel. Expand
NMDA-receptor activation increases cytoplasmic calcium concentration in cultured spinal cord neurones
It is directly demonstrated that excitatory amino acids acting at NMDA receptors on spinal cord neurones increase the intracellular Ca2+ activity, measured using the indicator dye arsenazo III, and that this is the result of Ca2- influx through NMDA receptor channels. Expand