Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking - Wikidata - awgldk - TriplyDB

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

http://www.wikidata.org/entity/Q42697198

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Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking Palmitoylation-dependent regulation of glutamate receptors and their PDZ domain-containing partners The physiology of protein S-acylation The perilipin homologue, lipid storage droplet 2, regulates sleep homeostasis and prevents learning impairments following sleep loss Dynamic Regulation of N-Methyl-d-aspartate (NMDA) and α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by Posttranslational Modifications Common mechanisms of excitatory and inhibitory imbalance in schizophrenia and autism spectrum disorders Glutamate receptor ion channels: structure, regulation, and function Novel epigallocatechin-3-gallate (EGCG) derivative as a new therapeutic strategy for reducing neuropathic pain after chronic constriction nerve injury in mice Effect of C-Terminal S-Palmitoylation on D2 Dopamine Receptor Trafficking and Stability Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels SorCS2-mediated NR2A trafficking regulates motor deficits in Huntington's disease Sudden death due to paralysis and synaptic and behavioral deficits when Hip14/Zdhhc17 is deleted in adult mice.DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95) protein and plays a role in learning and memory.Long-lasting adaptations of the NR2B-containing NMDA receptors in the dorsomedial striatum play a crucial role in alcohol consumption and relapse.Ion channel regulation by protein S-acylation.Protein Lipidation As a Regulator of Apoptotic Calcium Release: Relevance to Cancer.In vivo composition of NMDA receptor signaling complexes differs between membrane subdomains and is modulated by PSD-95 and PSD-93 Ganglioside regulation of AMPA receptor trafficking.The NMDA receptor as a target for cognitive enhancement Palmitoylation and depalmitoylation dynamics at a glance.Reduced Alzheimer's disease ß-amyloid deposition in transgenic mice expressing S-palmitoylation-deficient APH1aL and nicastrin.Xanthohumol improved cognitive flexibility in young mice.The intracellular dynamic of protein palmitoylation Palmitoylation at two cysteine clusters on the C-terminus of GluN2A and GluN2B differentially control synaptic targeting of NMDA receptors.Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation Post-translational modification biology of glutamate receptors and drug addiction In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to Rab5-positive endosomes.Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins.Reversible palmitoylation regulates surface stability of AMPA receptors in the nucleus accumbens in response to cocaine in vivo.Fatty acid synthase as a factor required for exercise-induced cognitive enhancement and dentate gyrus cellular proliferation.Voluntary running in young adult mice reduces anxiety-like behavior and increases the accumulation of bioactive lipids in the cerebral cortex.Protein kinase C promotes N-methyl-D-aspartate (NMDA) receptor trafficking by indirectly triggering calcium/calmodulin-dependent protein kinase II (CaMKII) autophosphorylation.S-nitrosylation and S-palmitoylation reciprocally regulate synaptic targeting of PSD-95 Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein.Palmitoylation influences the function and pharmacology of sodium channels.Posttranslational regulation of AMPA receptor trafficking and function Human CLC-K Channels Require Palmitoylation of Their Accessory Subunit Barttin to Be Functional A highly conserved cytoplasmic cysteine residue in the α4 nicotinic acetylcholine receptor is palmitoylated and regulates protein expression.Regulated internalization of NMDA receptors drives PKD1-mediated suppression of the activity of residual cell-surface NMDA receptors.Myelination of rodent hippocampal neurons in culture.

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P2860

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

http://www.wikidata.org/entity/Q42697198

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2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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2009年论文

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2009年论文

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name

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

@en

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

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type

label

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

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Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

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prefLabel

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

@en

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

@nl

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J.NEURON.2009.08.017

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Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking

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Gareth M Thomas

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Richard L Huganir

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P2860

Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins

Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins

NMDA receptor function is regulated by the inhibitory scaffolding protein, RACK1

The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase

Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae.

The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion.

The glutamate receptor ion channels

Palmitoylation of the GluR6 kainate receptor

Identification of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor

5-Hydroxytryptamine 4(a) receptor expressed in Sf9 cells is palmitoylated in an agonist-dependent manner

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scholarly article

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10.1016/J.NEURON.2009.08.017

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Takashi Hayashi

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