An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.
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Glutamate receptor poresMechanical coupling maintains the fidelity of NMDA receptor-mediated currentsGeneral rules for the arrangements and gating motions of pore-lining helices in homomeric ion channels.Reduced curvature of ligand-binding domain free-energy surface underlies partial agonism at NMDA receptors.Emerging structural insights into the function of ionotropic glutamate receptors.Block of NMDA receptor channels by endogenous neurosteroids: implications for the agonist induced conformational states of the channel vestibule.Conformational transitions in the glycine-bound GluN1 NMDA receptor LBD via single-molecule FRET.Phylogenetic analysis of ionotropic L-glutamate receptor genes in the Bilateria, with special notes on Aplysia californica.The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) ReceptorsComputationally Discovered Potentiating Role of Glycans on NMDA Receptors.Structure and gating of tetrameric glutamate receptors.Radial symmetry in a chimeric glutamate receptor pore.Gating Motions and Stationary Gating Properties of Ionotropic Glutamate Receptors: Computation Meets Electrophysiology.NMDA receptors: linking physiological output to biophysical operation.Probing the Structural Dynamics of the NMDA Receptor Activation by Coarse-Grained Modeling.Semiclosed Conformations of the Ligand-Binding Domains of NMDA Receptors during Stationary Gating.Single-molecule patch-clamp FRET microscopy studies of NMDA receptor ion channel dynamics in living cells: revealing the multiple conformational states associated with a channel at its electrical off state.Mechanism-Based Mathematical Model for Gating of Ionotropic Glutamate Receptors.Structural modeling for the open state of an NMDA receptor.The LILI Motif of M3-S2 Linkers Is a Component of the NMDA Receptor Channel Gate.Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca permeabilityA structurally derived model of subunit-dependent NMDA receptor function
P2860
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P2860
An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
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2013年论文
@zh-cn
name
An NMDA receptor gating mechan ...... ubunit-specific contributions.
@en
type
label
An NMDA receptor gating mechan ...... ubunit-specific contributions.
@en
prefLabel
An NMDA receptor gating mechan ...... ubunit-specific contributions.
@en
P2860
P1433
P1476
An NMDA receptor gating mechan ...... ubunit-specific contributions.
@en
P2093
Huan-Xiang Zhou
P2860
P304
P356
10.1016/J.BPJ.2013.04.013
P407
P577
2013-05-01T00:00:00Z