Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors - Test2 - elhamkhani - TriplyDB

Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors

Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors

http://www.wikidata.org/entity/Q28776368

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Histidine 140 plays a key role in the inhibitory modulation of the P2X4 nucleotide receptor by copper but not zinc A structural biology perspective on NMDA receptor pharmacology and function Novel NMDA receptor modulators: an update Functional insights from glutamate receptor ion channel structures Molecular bases of NMDA receptor subtype-dependent properties Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors Zinc Potentiates GluK3 Glutamate Receptor Function by Stabilizing the Ligand Binding Domain Dimer Interface From molecular phylogeny towards differentiating pharmacology for NMDA receptor subtypes Three rare diseases in one Sib pair: RAI1, PCK1, GRIN2B mutations associated with Smith–Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain Glutamate receptor ion channels: structure, regulation, and function Mapping the high-affinity binding domain of 5-substituted benzimidazoles to the proximal N-terminus of the GluN2B subunit of the NMDA receptor The serine protease plasmin cleaves the amino-terminal domain of the NR2A subunit to relieve zinc inhibition of the N-methyl-D-aspartate receptors Structural insights into phenylethanolamines high-affinity binding site in NR2B from binding and molecular modeling studies.Zinc alleviates pain through high-affinity binding to the NMDA receptor NR2A subunit Endogenous zinc in neurological diseases.Structural determinants of D-cycloserine efficacy at the NR1/NR2C NMDA receptors The Emerging Role for Zinc in Depression and Psychosis.pH-dependent inhibition of kainate receptors by zinc.Stoichiometry of N-methyl-D-aspartate receptors within the suprachiasmatic nucleus.Molecular determinants of proton modulation of glycine receptors.Control of assembly and function of glutamate receptors by the amino-terminal domain.The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.Hypoxia limits inhibitory effects of Zn2+ on spreading depolarizations.A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc.Different sites of alcohol action in the NMDA receptor GluN2A and GluN2B subunits.The neurobiology of zinc in health and disease.Molecular Mechanism of Disease-Associated Mutations in the Pre-M1 Helix of NMDA Receptors and Potential Rescue Pharmacology.A de novo loss-of-function GRIN2A mutation associated with childhood focal epilepsy and acquired epileptic aphasia.Expression and characterization of soluble amino-terminal domain of NR2B subunit of N-methyl-D-aspartate receptor.Constitutive activation of the N-methyl-D-aspartate receptor via cleft-spanning disulfide bonds.Intersubunit interactions at putative sites of ethanol action in the M3 and M4 domains of the NMDA receptor GluN1 and GluN2B subunits.Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.The Free Zinc Concentration in the Synaptic Cleft of Artificial Glycinergic Synapses Rises to At least 1 μM Non-agonist-binding subunit interfaces confer distinct functional signatures to the alternate stoichiometries of the alpha4beta2 nicotinic receptor: an alpha4-alpha4 interface is required for Zn2+ potentiation.Control of NMDA receptor function by the NR2 subunit amino-terminal domain Allosteric modulators of NR2B-containing NMDA receptors: molecular mechanisms and therapeutic potential Heavy Resistance Training and Supplementation With the Alleged Testosterone Booster Nmda has No Effect on Body Composition, Muscle Performance, and Serum Hormones Associated With the Hypothalamo-Pituitary-Gonadal Axis in Resistance-Trained Males.Molecular basis of NMDA receptor functional diversity.

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P2860

Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors

http://www.wikidata.org/entity/Q28776368

description

2000 nî lūn-bûn

@nan

2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Molecular determinants of coor ...... D-aspartate NR1/NR2A receptors

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Molecular determinants of coor ...... D-aspartate NR1/NR2A receptors

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Molecular determinants of coor ...... D-aspartate NR1/NR2A receptors

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Molecular determinants of coor ...... D-aspartate NR1/NR2A receptors

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Molecular determinants of coor ...... D-aspartate NR1/NR2A receptors

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Proceedings of the National Academy of Sciences of the United States of America

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Molecular determinants of coor ...... D-aspartate NR1/NR2A receptors

@en

P2093

C M Low

http://www.w3.org/2001/XMLSchema#string

F Zheng

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P Lyuboslavsky

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S F Traynelis

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P2860

Structure of a glutamate-receptor ligand-binding core in complex with kainate

The glutamate receptor ion channels

Developmental and regional expression in the rat brain and functional properties of four NMDA receptors

Proton inhibition of N-methyl-D-aspartate receptors in cerebellar neurons.

Control of proton sensitivity of the NMDA receptor by RNA splicing and polyamines.

Modulation of inhibitory and excitatory amino acid receptor ion channels by zinc.

Zn2+: an endogenous modulator of ligand- and voltage-gated ion channels.

A practical guide to the preparation of Ca2+ buffers.

Identification of an inhibitory Zn2+ binding site on the human glycine receptor alpha1 subunit.

Tyrosine kinase potentiates NMDA receptor currents by reducing tonic zinc inhibition.

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scholarly article

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3382936

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10.1073/PNAS.180307497

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20

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97

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2000-09-26T00:00:00Z

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12336819

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10984504

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27148

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