N-Glycosylation is not a prerequisite for glutamate receptor function but Is essential for lectin modulation.
about
Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domainGlutamate receptor ion channels: structure, regulation, and functionLigand binding to the amino-terminal domain of the mGluR4 subtype of metabotropic glutamate receptorDeglycosylation altered the gating properties of rNav1.3: glycosylation/deglycosylation homeostasis probably complicates the functional regulation of voltage-gated sodium channelTethered ligands reveal glutamate receptor desensitization depends on subunit occupancy.Pharmacology of AMPA/kainate receptor ligands and their therapeutic potential in neurological and psychiatric disorders.Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha.AMPA receptors commandeer an ancient cargo exporter for use as an auxiliary subunit for signaling.Molecular physiology of kainate receptors.Abnormal N-linked glycosylation of cortical AMPA receptor subunits in schizophrenia.Isolation of novel prototype galectins from the marine ball sponge Cinachyrella sp. guided by their modulatory activity on mammalian glutamate-gated ion channels.Glycosylation contributes to variability in expression of murine cytomegalovirus m157 and enhances stability of interaction with the NK-cell receptor Ly49H.Molecular determinants controlling NMDA receptor synaptic incorporation.Evolutionarily conserved pattern of AMPA receptor subunit glycosylation in Mammalian frontal cortex.The molecular pharmacology and cell biology of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptorsTwo N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-d-aspartate (NMDA) Receptors from the Endoplasmic Reticulum.The NMDA receptor functions independently and as an LRP1 co-receptor to promote Schwann cell survival and migration.Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.Kainate receptors.Subtype selective kainic acid receptor agonists: discovery and approaches to rational design.The glutamate receptor subunit delta2 is capable of gating its intrinsic ion channel as revealed by ligand binding domain transplantationHNK-1 glyco-epitope regulates the stability of the glutamate receptor subunit GluR2 on the neuronal cell surface.Computationally Discovered Potentiating Role of Glycans on NMDA Receptors.The role of protein N-glycosylation in neural transmissionN-glycan content modulates kainate receptor functional properties.Assembly of AMPA receptors: mechanisms and regulation.Mouse galectin-1 inhibits the toxicity of glutamate by modifying NR1 NMDA receptor expression.ConBr, a lectin from Canavalia brasiliensis seeds, protects against quinolinic acid-induced seizures in mice.Biochemical and electrophysiological characterization of N-glycans on NMDA receptor subunits.Concanavalin-A reports agonist-induced conformational changes in the intact GluR6 kainate receptor.Allosteric regulation and spatial distribution of kainate receptors bound to ancillary proteins.Kainate-binding proteins are rendered functional ion channels upon transplantation of two short pore-flanking domains from a kainate receptor.TARP γ-8 glycosylation regulates the surface expression of AMPA receptors.N-glycosylation in regulation of the nervous system.Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit.Positive allosteric modulators of AMPA receptors reduce proton-induced receptor desensitization in rat hippocampal neurons.The delta subfamily of glutamate receptors: characterization of receptor chimeras and mutants.Functional analysis of Caenorhabditis elegans glutamate receptor subunits by domain transplantation.Putative NMDA receptors in Hydra: a biochemical and functional study.Different structural requirements for functional ion pore transplantation suggest different gating mechanisms of NMDA and kainate receptors.
P2860
Q28211830-D5AAF724-DB3D-4146-81EE-84E3536AF118Q28290774-FC8C4475-C3E3-4862-AD14-8788E113CF43Q28373018-5630D4CC-36B4-47C9-8859-0769C9E8C3F4Q28566539-BBA978C5-7EA7-40A8-9032-0F2A6E3E80A6Q33698262-9D050959-266F-407E-B768-59EE7809DAAFQ33863397-D2B91075-1BED-462E-9F63-484A6A6D9AA5Q33863637-3156134B-4616-41C0-AF0E-4334537FEAE3Q34146300-EB467B06-6379-4A75-AAAC-9B38B14B5794Q34294046-4EBB26FB-01C5-482B-A48C-CC2D9FF1A2DEQ34331035-474A8EF7-E94D-45B9-BBF8-4D44D1387CF9Q34501503-7516B61D-06E2-47A2-85F6-ABCED99A6E47Q34759678-3741474C-9054-4AB6-83A2-EC956113C3C2Q34974511-773BE87C-7D1C-41C4-9D95-B993245B0B5FQ35142747-DABD858A-4A43-4E5F-817C-1536D9548314Q35858251-363D20B3-B48D-453F-A821-3364B98ED090Q35883792-4AD47A96-F1CE-4176-9371-FA59783EA8F5Q36125572-6C58C8AC-2D6E-4C62-A69B-ED3C816B73BAQ36197690-38F3FB30-34A0-40CE-8108-D2EC5C816A01Q36539074-15EA72F6-B340-41C3-9F8C-9F92C4D2A20CQ37214843-794C1C86-F6F3-461A-832D-16983371A1DAQ37238823-67CD7CE5-5F71-4563-B977-54353957DD5CQ37431694-5D0CAAF8-07D3-4E8E-8D31-C562CC23F568Q37738255-FECAC049-AB99-4C6B-B19A-889C9A270CC9Q38197055-0F4610EA-A7C3-42AC-A862-6CA0DA2B16CEQ38287732-CB4D4C73-C4E0-4AF4-A0B0-BC5698759493Q38306577-D8A33170-E358-46ED-B153-C1A5F930B8CFQ38306712-2848ECD6-E186-4937-A088-4F4867001831Q38331580-631084B4-B695-458C-8D85-90A107A3DB8DQ39741746-6971E1B6-53A4-44CC-AE5E-A63A9FB0840BQ40324619-7947D7F7-2956-4EDC-A2F5-B22E614630C1Q40673372-F74F88FA-0AB5-40BF-88E8-E5F1BBE2F0E7Q40699149-EF3DC651-957F-4D1A-825F-08934DC0B46DQ41705140-97DA24E2-E7D2-41CE-BFC6-2E0F74A643A9Q41842547-3F106EE9-4D6F-4AB5-92EC-6E372A25480BQ42060242-8A2E697A-2C40-46A3-8FAF-ADA4265C5511Q43607871-94927A7E-E645-47CC-A1FD-8A690D69F416Q43849872-E9B02378-1DAF-4AEA-98C5-09E817F85185Q44557679-C250E4E4-46C2-4760-B497-CBE514E773BCQ45153228-C48A78EB-AAF2-4FCB-9751-DB0E3CB23BB5Q46424194-A13EC090-BF9B-4E15-9778-C9926543C6E5
P2860
N-Glycosylation is not a prerequisite for glutamate receptor function but Is essential for lectin modulation.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
N-Glycosylation is not a prere ...... sential for lectin modulation.
@en
N-Glycosylation is not a prere ...... sential for lectin modulation.
@nl
type
label
N-Glycosylation is not a prere ...... sential for lectin modulation.
@en
N-Glycosylation is not a prere ...... sential for lectin modulation.
@nl
prefLabel
N-Glycosylation is not a prere ...... sential for lectin modulation.
@en
N-Glycosylation is not a prere ...... sential for lectin modulation.
@nl
P2093
P356
P1476
N-Glycosylation is not a prere ...... sential for lectin modulation.
@en
P2093
P304
P356
10.1124/MOL.52.5.861
P577
1997-11-01T00:00:00Z