Amino terminal domains of the NMDA receptor are organized as local heterodimers (Q28571825)

31 January 2017

title

Amino terminal domains of the NMDA receptor are organized as local heterodimers (English)

1 reference

31 January 2017

Chia-Hsueh Lee

1

1 reference

31 January 2017

Eric Gouaux

series ordinal

2

1 reference

31 January 2017

language of work or name

English

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publication date

22 April 2011

1 reference

31 January 2017

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31 January 2017

volume

6

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31 January 2017

issue

4

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31 January 2017

page(s)

e19180

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Creative Commons Attribution 4.0 International

31 January 2017

copyright license

start time

22 April 2011

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

0 references

cites work

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Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit

19 March 2017

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Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors

19 March 2017

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19 March 2017

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Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly

19 March 2017

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19 March 2017

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Control of assembly and function of glutamate receptors by the amino-terminal domain.

19 March 2017

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Domain organization and function in GluK2 subtype kainate receptors.

29 September 2017

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29 September 2017

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An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-Methyl-D-aspartate receptors

29 September 2017

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Mechanism of differential control of NMDA receptor activity by NR2 subunits

29 September 2017

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Different roles of C-terminal cassettes in the trafficking of full-length NR1 subunits to the cell surface

29 September 2017

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Binding of spermine and ifenprodil to a purified, soluble regulatory domain of the N-methyl-D-aspartate receptor

29 September 2017

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N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor

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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

29 September 2017

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29 September 2017

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Subunit arrangement and function in NMDA receptors

29 September 2017

1 reference

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Mechanism of partial agonist action at the NR1 subunit of NMDA receptors

29 September 2017

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Subunit assembly of N-methyl-d-aspartate receptors analyzed by fluorescence resonance energy transfer

29 September 2017

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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

29 September 2017

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Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors

29 September 2017

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29 September 2017

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

29 September 2017

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Three pairs of cysteine residues mediate both redox and zn2+ modulation of the nmda receptor.

29 September 2017

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Molecular cloning and characterization of the rat NMDA receptor

29 September 2017

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Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit

29 September 2017

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Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies

3 June 2018

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Masking of the endoplasmic reticulum retention signals during assembly of the NMDA receptor.

3 June 2018

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Crossref

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0019180

Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain

21 January 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/21544205

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PONE.0019180

1 reference

ADS bibcode

2011PLoSO...619180L

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