Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors. - Wikidata - awgldk - TriplyDB

Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.

Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.

http://www.wikidata.org/entity/Q40816191

about

Anti-NMDA-receptor encephalitis: case series and analysis of the effects of antibodies Glutamatergic autoencephalitides: an emerging field Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly.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 Amino terminal domains of the NMDA receptor are organized as local heterodimers A naturally occurring null variant of the NMDA type glutamate receptor NR3B subunit is a risk factor of schizophrenia.Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability and Mg2+ block.Stargazin is an AMPA receptor auxiliary subunit Molecular mechanisms involved in the side effects of fatty acid amide hydrolase inhibitors: a structural phenomics approach to proteome-wide cellular off-target deconvolution and disease association.Control of assembly and function of glutamate receptors by the amino-terminal domain.Subunit arrangement and function in NMDA receptors.ER to synapse trafficking of NMDA receptors Proteins interactions implicated in AMPA receptor trafficking: a clear destination and an improving route map.Transmembrane region of N-methyl-D-aspartate receptor (NMDAR) subunit is required for receptor subunit assembly.Comparison of diagnostic accuracy of microscopy and flow cytometry in evaluating N-methyl-D-aspartate receptor antibodies in serum using a live cell-based assay.Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.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.Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.Glutamate receptors and endoplasmic reticulum quality control: looking beneath the surface.Expression and characterization of soluble amino-terminal domain of NR2B subunit of N-methyl-D-aspartate receptor.Functioning of the dimeric GABA(B) receptor extracellular domain revealed by glycan wedge scanning.On the hypes and falls in neuroprotection: targeting the NMDA receptor.Assembly and forward trafficking of NMDA receptors (Review).Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.Binding of spermine and ifenprodil to a purified, soluble regulatory domain of the N-methyl-D-aspartate receptor Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-Methyl-D-aspartate receptors.Oligodendrocyte N-methyl-D-aspartate receptor signaling: insights into its functions.The σ-1 receptor interacts directly with GluN1 but not GluN2A in the GluN1/GluN2A NMDA receptor.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.Zinc inhibition of rat NR1/NR2A N-methyl-D-aspartate receptors.N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor.A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit.Subunit assembly of N-methyl-d-aspartate receptors analyzed by fluorescence resonance energy transfer.Roles of the N-terminal domain on the function and quaternary structure of the ionotropic glutamate receptor.Arginine 260 of the amino-terminal domain of NR1 subunit is critical for tissue-type plasminogen activator-mediated enhancement of N-methyl-D-aspartate receptor signaling.Export from the endoplasmic reticulum of assembled N-methyl-d-aspartic acid receptors is controlled by a motif in the c terminus of the NR2 subunit.

P2860

Q24642126-6BF196CE-D158-4A76-8A7D-D2143432C976 Q26992294-635BB6D4-E7AC-43A6-8405-D001AD97D135 Q27641433-A802E911-003E-457E-B6BD-7C485177DFAA Q27667242-3A1ED444-3516-45D5-AA04-292FDDA379AD Q27865201-DE0C2357-30D6-4473-BD40-2C972F144B75 Q28210064-FB1232D0-491A-4882-B349-6540C1344536 Q28290774-D1B9B9A2-5114-4DFB-A689-CA1F2C3AD2BF Q28571825-80BB1C65-5440-4B38-BCF2-ABF18E6EC54B Q30416311-678699B5-C609-4E5C-B6AC-87C28716CAF7 Q33722699-9CAB04AF-F812-4CDF-8B51-F569E4A9E282 Q33723617-0507F602-D0E5-487F-AC66-EAE9497C9F5A Q33917845-8AF1C094-F11D-4E0E-A22C-1C95B2B324FA Q34310112-5B73B59E-2BD5-47CF-87AA-7068C7D241F4 Q34466595-6869264E-A3C5-4505-B238-AC4E1AA8EA4A Q34579616-3071067F-B66B-4F6C-88A5-C9239986B3E4 Q35083764-FA6E5C12-D9E0-4783-8C04-3A20B0B65729 Q35145011-993D034B-E0EE-4EF1-9A83-DD63FC137E80 Q35224250-E9F630CB-3475-402E-8CCA-D935B3A7BD88 Q35608140-2C3F8600-EF21-4123-9B44-3F7EE0CC6CF5 Q36122277-250860B9-012D-4A83-A344-A5308F73741D Q36197690-1B366282-A0F8-43FB-B0AE-254142662831 Q36473601-B3BE1FF0-5101-4627-9397-0EC5781152AC Q36476996-6E5E8C2E-DE64-4B20-AFBA-44E3C6C0FFA7 Q36642706-96DA6ABC-869E-4774-89D1-8A47F69A93A7 Q36958209-29C5E9FC-D9C2-4EA7-A4B5-A7A330CFD9A4 Q37150922-1C7ED7AD-E4E3-4CB2-A869-53AF9F368138 Q37184815-A54C3800-3D26-4C75-B0E4-69687EB34D86 Q37212897-3DA510FC-F345-4AC5-9398-B52E9895E44B Q37311908-202B3194-7090-426F-9094-55C04B952460 Q37339060-09B328ED-7D59-4E79-851B-F2599C6B0817 Q38076363-542E611B-5EE6-441C-B7A5-8250464800D2 Q39063368-9E9F087D-281F-4763-92FB-4BFE2131489E Q39140430-767D97F4-1533-4F66-821B-32900772AC4B Q40042474-4B651A02-7016-4557-A1A3-4142DAA5DBE5 Q40112573-BC93EEA0-9277-4D09-8E0E-5C961910D296 Q40178880-F6993580-13DB-4778-9CC1-CCB458B3ADD1 Q40423808-F27FBAB7-07BE-4FE4-928F-F983AB56FD20 Q40444250-913F186B-4384-4BFA-8B81-DD7188B45BF9 Q40511087-DEBC7CF7-7796-4CCD-B475-CFEE42524AD9 Q40563945-EE25F864-2F61-4C19-8589-89677C1567E4

P2860

Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.

http://www.wikidata.org/entity/Q40816191

description

2001 nî lūn-bûn

@nan

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

2001年论文

@zh

2001年论文

@zh-cn

name

Identification of molecular de ...... -methyl-D-aspartate receptors.

@en

type

label

Identification of molecular de ...... -methyl-D-aspartate receptors.

@en

prefLabel

Identification of molecular de ...... -methyl-D-aspartate receptors.

@en

P1433

Q40816191-CD789F52-C66C-4025-A643-C7FFB6C07063

P1476

Q40816191-0E100800-04F7-405C-B044-659CB9C4081A

P2093

Q40816191-4D506FC4-C9CF-4EFE-A35A-248DC780A366

Q40816191-62AB1915-8410-4AE8-9361-D33937C3C1B5

Q40816191-79EC5419-C81E-4C47-8C73-E34625B34E00

Q40816191-81855EBB-3F91-4739-876D-86F8235AC0EF

Q40816191-972A9417-C0D6-477D-A51E-D4069A4F12B9

Q40816191-C059D934-B70D-4632-ACEA-CC8D96C5A0EF

Q40816191-F6A09C0E-7A07-4B4A-A4CC-866D201AAE51

P2860

Q40816191-0229C505-0D6F-4E45-B1E1-27A8D4F92878

Q40816191-1120599A-173F-4C1D-9135-CE70B601EE12

Q40816191-13C01B64-1CF9-401C-AF72-CA3ACCF5EC87

Q40816191-158A1750-F4EB-4501-AA83-30579F037556

Q40816191-17BC1E25-1285-494D-A798-44CF2B967AD8

Q40816191-375F4E79-3ABD-44AD-9C13-8B8A7787E4F2

Q40816191-4598F1D4-BA66-47B9-9978-BDB0DA191120

Q40816191-486AEAF9-3690-492F-95FD-DE5E15A2B82F

Q40816191-4D76E85C-8161-477F-9CAE-35915E665FE0

Q40816191-536C86DC-7CBE-43D9-9166-46A73ED1E461

P304

Q40816191-E69025E5-706B-4A93-A808-CF8264862E38

P31

Q40816191-0E5C6EC9-6FE8-4766-8BD6-CC7136D0A0ED

P356

Q40816191-198E9C94-123E-4483-964A-9CED6E9E3306

P407

Q40816191-4428C71F-F007-49ED-A62B-6E13F6754B39

P433

Q40816191-7CE6C45E-6645-4A36-9352-8D1DA3E0AB64

P478

Q40816191-80B246BE-7CEF-4359-A102-2A2AEA1D93B1

P577

Q40816191-265FB9AC-1E3B-47BC-A714-5788D7DB2717

P698

Q40816191-92B11CDF-30C2-4EE0-8024-1D0282127D6D

P356

P1433

Journal of Biological Chemistry

P1476

Identification of molecular de ...... -methyl-D-aspartate receptors.

@en

P2093

Grimwood S

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

Le Bourdelles B

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

McIlhinney RA

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

Meddows E

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

Sandhu S

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

Wafford K

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

Whiting P

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

P2860

Biochemical evidence for the co-association of three N-methyl-D-aspartate (NMDA) R2 subunits in recombinant NMDA receptors

P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels.

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

Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains

Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins

Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

Three-dimensional models of non-NMDA glutamate receptors

Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen.

Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha.

P304

18795-18803

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

P31

scholarly article

P356

10.1074/JBC.M101382200

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

P407

P433

22

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

P478

276

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

P577

2001-03-06T00:00:00Z

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

P698

11279200

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