A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux. - Wikidata - wikimedia - TriplyDB

A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

http://www.wikidata.org/entity/Q40803792

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Proteomic and functional evidence for a P2X7 receptor signalling complex Cellular interplay between neurons and glia: toward a comprehensive mechanism for excitotoxic neuronal loss in neurodegeneration Dynamin-dependent NMDAR endocytosis during LTD and its dependence on synaptic state The Emergence of NMDA Receptor Metabotropic Function: Insights from Imaging Non-ionotropic signaling by the NMDA receptor: controversy and opportunity A Metabotropic-Like Flux-Independent NMDA Receptor Regulates Ca2+ Exit from Endoplasmic Reticulum and Mitochondrial Membrane Potential in Cultured Astrocytes Regulation of synaptic inhibition by phospho-dependent binding of the AP2 complex to a YECL motif in the GABAA receptor 2 subunit NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex Glutamate receptor ion channels: structure, regulation, and function Direct interaction of myosin regulatory light chain with the NMDA receptor Gain control of N-methyl-D-aspartate receptor activity by receptor-like protein tyrosine phosphatase alpha High-resolution localization of clathrin assembly protein AP180 in the presynaptic terminals of mammalian neurons Activation of 5-HT2A/C receptors counteracts 5-HT1A regulation of n-methyl-D-aspartate receptor channels in pyramidal neurons of prefrontal cortex NR2B tyrosine phosphorylation modulates fear learning as well as amygdaloid synaptic plasticity N-methyl-D-aspartate receptor subunits are non-myosin targets of myosin regulatory light chain Stability of surface NMDA receptors controls synaptic and behavioral adaptations to amphetamine.Calpain product of WT-CRMP2 reduces the amount of surface NR2B NMDA receptor subunit.Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calcium.mTORC1 Is a Local, Postsynaptic Voltage Sensor Regulated by Positive and Negative Feedback Pathways.Postsynaptic density-95 (PSD-95) and calcineurin control the sensitivity of N-methyl-D-aspartate receptors to calpain cleavage in cortical neurons.Role of the fourth membrane domain of the NR2B subunit in the assembly of the NMDA receptor Telling tails.Inhibition of NR2B phosphorylation restores alterations in NMDA receptor expression and improves functional recovery following traumatic brain injury in mice The NMDA receptor as a target for cognitive enhancement The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2.ER to synapse trafficking of NMDA receptors NMDA-receptor activation but not ion flux is required for amyloid-beta induced synaptic depression.Acute mechanisms underlying antibody effects in anti-N-methyl-D-aspartate receptor encephalitis Activity-induced synaptic delivery of the GluN2A-containing NMDA receptor is dependent on endoplasmic reticulum chaperone Bip and involved in fear memory Endocytosis and synaptic removal of NR3A-containing NMDA receptors by PACSIN1/syndapin1.Molecular pharmacology of human NMDA receptors Non-Ionotropic NMDA Receptor Signaling Drives Activity-Induced Dendritic Spine Shrinkage.Regulation of NMDA receptors by phosphorylation.Postsynaptic, not presynaptic NMDA receptors are required for spike-timing-dependent LTD induction Key amino acid residues within the third membrane domains of NR1 and NR2 subunits contribute to the regulation of the surface delivery of N-methyl-D-aspartate receptors.Chronic opioid potentiates presynaptic but impairs postsynaptic N-methyl-D-aspartic acid receptor activity in spinal cords: implications for opioid hyperalgesia and tolerance.Regulated internalization of NMDA receptors drives PKD1-mediated suppression of the activity of residual cell-surface NMDA receptors.Conformational signaling required for synaptic plasticity by the NMDA receptor complex Agonist binding to the NMDA receptor drives movement of its cytoplasmic domain without ion flow.Calcium flux-independent NMDA receptor activity is required for Aβ oligomer-induced synaptic loss

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P2860

A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

http://www.wikidata.org/entity/Q40803792

description

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2001年学术文章

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2001年学术文章

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2001年學術文章

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2001年學術文章

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name

A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

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A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

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prefLabel

A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

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Nature Neuroscience

P1476

A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux.

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P2093

Heinemann SF

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Krupp JJ

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Vissel B

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Westbrook GL

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P2860

Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain

PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A

Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor

The effect of transient global ischemia on the interaction of Src and Fyn with the N-methyl-D-aspartate receptor and postsynaptic densities: possible involvement of Src homology 2 domains

AMPA receptor-mediated regulation of a Gi-protein in cortical neurons

Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit

The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn

Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension

Recognition and specificity in protein tyrosine kinase-mediated signalling.

Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis.

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10.1038/88404

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1021352516

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11369939

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