about
RNA based antagonist of NMDA receptorsDynamic membrane protein topological switching upon changes in phospholipid environment.Stargazin promotes closure of the AMPA receptor ligand-binding domainSubtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc.Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism.Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.Stargazin Modulation of AMPA Receptors.Proton-mediated conformational changes in an acid-sensing ion channel.The delta2 glutamate-like receptor undergoes similar conformational changes as other ionotropic glutamate receptors.Transmembrane AMPA receptor regulatory protein regulation of competitive antagonism: a problem of interpretation.Na+/Cl- dipole couples agonist binding to kainate receptor activation.Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation.Deactivation kinetics of acid-sensing ion channel 1a are strongly pH-sensitive.The structure-energy landscape of NMDA receptor gating.Acid-sensing ion channels are tuned to follow high-frequency stimuli.Dynamic Lipid-dependent Modulation of Protein Topology by Post-translational Phosphorylation.The α2δ-1-NMDA Receptor Complex Is Critically Involved in Neuropathic Pain Development and Gabapentin Therapeutic Actions.Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRETCrossTalk opposing view: TARPs modulate AMPA receptor conformations before the gating transitionsConformational spread and dynamics in allostery of NMDA receptorsβ11-12 linker isomerization governs acid-sensing ion channel desensitization and recoveryMechanism of modulation of AMPA receptors by TARP-γ8Coupling structure with function in acid-sensing ion channels: Challenges in pursuit of proton sensors
P50
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P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
David M Maclean
@en
David M Maclean
@nl
type
label
David M Maclean
@en
David M Maclean
@nl
prefLabel
David M Maclean
@en
David M Maclean
@nl
P31
P496
0000-0001-8294-6075