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Amino terminal domains of the NMDA receptor are organized as local heterodimers
scientific journal article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
title
Amino terminal domains of the NMDA receptor are organized as local heterodimers
(English)
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
author name string
Chia-Hsueh Lee
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
Eric Gouaux
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
language of work or name
English
0 references
publication date
22 April 2011
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
published in
PLOS One
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
volume
6
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
issue
4
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
page(s)
e19180
1 reference
stated in
PubMed
PubMed ID
21544205
retrieved
31 January 2017
copyright license
Creative Commons Attribution 4.0 International
start time
22 April 2011
1 reference
stated in
April 2022 Public Data File from Crossref
copyright status
copyrighted
0 references
cites work
Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
The N-terminal domain of GluR6-subtype glutamate receptor ion channels
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Crystal structure and association behaviour of the GluR2 amino-terminal domain
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Pharmacological characterization of recombinant NR1/NR2A NMDA receptors with truncated and deleted carboxy termini expressed in Xenopus laevis oocytes
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
A nomenclature for ligand-gated ion channels
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
The glutamate receptor ion channels
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Heteromeric NMDA receptors: molecular and functional distinction of subtypes
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
19 March 2017
Control of assembly and function of glutamate receptors by the amino-terminal domain.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Domain organization and function in GluK2 subtype kainate receptors.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Subunit arrangement in N-methyl-D-aspartate (NMDA) receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Control of NMDA receptor function by the NR2 subunit amino-terminal domain
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-Methyl-D-aspartate receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Mechanism of differential control of NMDA receptor activity by NR2 subunits
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Different roles of C-terminal cassettes in the trafficking of full-length NR1 subunits to the cell surface
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Binding of spermine and ifenprodil to a purified, soluble regulatory domain of the N-methyl-D-aspartate receptor
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
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
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
NMDA receptor subunits: function and pharmacology.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Subunit arrangement and function in NMDA receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Mechanism of partial agonist action at the NR1 subunit of NMDA receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Subunit assembly of N-methyl-d-aspartate receptors analyzed by fluorescence resonance energy transfer
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
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
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Three pairs of cysteine residues mediate both redox and zn2+ modulation of the nmda receptor.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Molecular cloning and characterization of the rat NMDA receptor
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
29 September 2017
Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
3 June 2018
Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3081335
retrieved
3 June 2018
Masking of the endoplasmic reticulum retention signals during assembly of the NMDA receptor.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0019180
retrieved
21 January 2018
Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21544205
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1371/JOURNAL.PONE.0019180
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3096884
ADS bibcode
2011PLoSO...619180L
0 references
OpenCitations bibliographic resource ID
3096884
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3096884
PMCID
3081335
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3096884
PubMed ID
21544205
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3096884
ResearchGate publication ID
51099862
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