DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels.

scientific article published on December 2002

DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1523/JNEUROSCI.22-23-10209.2002
P932PMC publication ID6758750
P698PubMed publication ID12451122

P2093author name stringThomas Kuner
Junryo Watanabe
Lonnie P Wollmuth
Christine Beck
Louis S Premkumar
P2860cites workIntracellular Mg2+ interacts with structural determinants of the narrow constriction contributed by the NR1-subunit in the NMDA receptor channel.Q41063217
Calcium permeability of glutamate-gated channels in the central nervous systemQ41103315
Calcium-dependent inactivation of recombinant N-methyl-D-aspartate receptors is NR2 subunit specific.Q41148644
The role of divalent cations in the N-methyl-D-aspartate responses of mouse central neurones in cultureQ41253548
Fractional calcium currents through recombinant GluR channels of the NMDA, AMPA and kainate receptor subtypesQ41339891
Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptorQ41603790
Structural basis for explaining open-channel blockade of the NMDA receptor.Q41664696
Different mechanisms of Ca2+ transport in NMDA and Ca2+-permeable AMPA glutamate receptor channels.Q41900225
Molecular rearrangements of the extracellular vestibule in NMDAR channels during gatingQ43846767
Fractional contribution of calcium to the cation current through glutamate receptor channelsQ48264301
NMDAR channel segments forming the extracellular vestibule inferred from the accessibility of substituted cysteinesQ48921111
Coupling of permeation and gating in an NMDA-channel pore mutantQ48968453
Identification of a high affinity divalent cation binding site near the entrance of the NMDA receptor channelQ49016266
Differential contribution of the NR1- and NR2A-subunits to the selectivity filter of recombinant NMDA receptor channelsQ49016668
Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines.Q50760890
The use of fura-2 for estimating Ca buffers and Ca fluxes.Q52324742
Substituted-cysteine accessibility methodQ77121562
Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+.Q27867707
The glutamate receptor ion channelsQ28137916
Voltage and concentration dependence of Ca(2+) permeability in recombinant glutamate receptor subtypesQ28344390
Calcium channel permeation: A field in fluxQ33648624
The changing landscape of ischaemic brain injury mechanisms.Q33678157
Dimensions of the narrow portion of a recombinant NMDA receptor channelQ34128656
Altered voltage dependence of fractional Ca2+ current in N-methyl-D-aspartate channel pore mutants with a decreased Ca2+ permeabilityQ34167555
Interactions between two divalent ion binding sites in N-methyl-D-aspartate receptor channelsQ35947358
Ionic permeability characteristics of the N-methyl-D-aspartate receptor channelQ36411434
Subconductance states of a mutant NMDA receptor channel kinetics, calcium, and voltage dependenceQ36417599
Calcium permeability of the N-methyl-D-aspartate receptor channel in hippocampal neurons in cultureQ36714319
P433issue23
P407language of work or nameEnglishQ1860
P304page(s)10209-10216
P577publication date2002-12-01
P1433published inJournal of NeuroscienceQ1709864
P1476titleDRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels
P478volume22

Reverse relations

cites work (P2860)
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Q44902321Block of AMPA receptor desensitization by a point mutation outside the ligand-binding domain.
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Q40655991Extracellular Vestibule Determinants of Ca2+ Influx in Ca2+‐Permeable AMPA Receptor Channels
Q90124343From bedside-to-bench: What disease-associated variants are teaching us about the NMDA receptor
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Q42256489High Ca(2+) permeability of a peptide-gated DEG/ENaC from Hydra
Q88241483Ion permeation in ionotropic glutamate receptors: Still dynamic after all these years
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