DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels.
about
Glutamate receptor poresCrystal structure of a heterotetrameric NMDA receptor ion channelGlutamate receptor ion channels: structure, regulation, and functionSeparate intramolecular targets for protein kinase A control N-methyl-D-aspartate receptor gating and Ca2+ permeability.Extracellular Ca(2+) ions reduce NMDA receptor conductance and gating.Specific sites within the ligand-binding domain and ion channel linkers modulate NMDA receptor gatingArrangement of subunits in functional NMDA receptors.Emerging structural insights into the function of ionotropic glutamate receptors.Permeation properties of the hair cell mechanotransducer channel provide insight into its molecular structureBidirectional Effect of Pregnenolone Sulfate on GluN1/GluN2A N-Methyl-D-Aspartate Receptor Gating Depending on Extracellular Calcium and Intracellular MilieuSubunit-specific contribution of pore-forming domains to NMDA receptor channel structure and gating.An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.Modulation of NMDA channel gating by Ca(2+) and Cd(2+) binding to the external pore mouthStructure and gating of tetrameric glutamate receptors.Potentiation of Glycine-Gated NR1/NR3A NMDA Receptors Relieves Ca-Dependent Outward Rectification.Voltage-dependent gating of NR1/2B NMDA receptors.Role of aspartate 298 in mouse 5-HT3A receptor gating and modulation by extracellular Ca2+.Extracellular vestibule determinants of Ca2+ influx in Ca2+-permeable AMPA receptor channels.Qgrid: clustering tool for detecting charged and hydrophobic regions in proteins.Calcium-dependent decrease in the single-channel conductance of TRPV1.High Ca(2+) permeability of a peptide-gated DEG/ENaC from Hydra.Ionic flow enhances low-affinity binding: a revised mechanistic view into Mg2+ block of NMDA receptors.Early biophysics of the NMDA receptor channel.De novo mutations in GRIN1 cause extensive bilateral polymicrogyria.Resident Calmodulin Primes NMDA Receptors for Ca2+-Dependent Inactivation.
P2860
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P2860
DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
DRPEER: a motif in the extrace ...... tes in NMDA receptor channels.
@en
type
label
DRPEER: a motif in the extrace ...... tes in NMDA receptor channels.
@en
prefLabel
DRPEER: a motif in the extrace ...... tes in NMDA receptor channels.
@en
P2093
P1476
DRPEER: a motif in the extrace ...... ates in NMDA receptor channels
@en
P2093
Christine Beck
Junryo Watanabe
Lonnie P Wollmuth
Louis S Premkumar
Thomas Kuner
P304
10209-10216
P356
10.1523/JNEUROSCI.22-23-10209.2002
P407
P577
2002-12-01T00:00:00Z