Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain (Q28210064)

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14 December 2019

title

Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain (English)

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14 December 2019

2

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14 December 2019

David Mottershead

4

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14 December 2019

author name string

Arja Pasternack

1

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14 December 2019

Annukka Jouppila

3

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14 December 2019

Maria Lindfors

5

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14 December 2019

Michael Pasternack

6

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14 December 2019

Kari Keinänen

7

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14 December 2019

language of work or name

English

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publication date

21 October 2002

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Journal of Biological Chemistry

14 December 2019

published in

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14 December 2019

volume

277

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14 December 2019

issue

51

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14 December 2019

page(s)

49662-49667

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The structure and function of glutamate receptor ion channels

14 December 2019

cites work

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The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins

21 January 2018

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

21 January 2018

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Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins

21 January 2018

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

21 January 2018

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Molecular organization of a zinc binding n-terminal modulatory domain in a NMDA receptor subunit

21 January 2018

1 reference

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

21 January 2018

1 reference

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Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD.

21 January 2018

1 reference

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Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions

21 January 2018

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N-Terminal Domains in the NR2 Subunit Control Desensitization of NMDA Receptors

21 January 2018

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Four residues of the extracellular N-terminal domain of the NR2A subunit control high-affinity Zn2+ binding to NMDA receptors

21 January 2018

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

21 January 2018

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Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A.

21 January 2018

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Glycine-independent NMDA receptor desensitization: localization of structural determinants

21 January 2018

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Synaptic clustering of AMPA receptors by the extracellular immediate-early gene product Narp.

21 January 2018

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Flip and Flop: A Cell-Specific Functional Switch in Glutamate-Operated Channels of the CNS

21 January 2018

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Use of proteoliposomes to generate phage antibodies against native AMPA receptor

21 January 2018

1 reference

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Functional characterization of a potassium-selective prokaryotic glutamate receptor

21 January 2018

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Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state

21 January 2018

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

21 January 2018

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NMDA receptor channels: subunit-specific potentiation by reducing agents

21 January 2018

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A point mutation in the glutamate binding site blocks desensitization of AMPA receptors

21 January 2018

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Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core

21 January 2018

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Mechanism of glutamate receptor desensitization

21 January 2018

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

21 January 2018

1 reference

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Heteromeric AMPA receptors assemble with a preferred subunit stoichiometry and spatial arrangement

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208349200

Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208349200

Characterization of the ligand-binding domains of glutamate receptor (GluR)-B and GluR-D subunits expressed in Escherichia coli as periplasmic proteins.

21 January 2018

1 reference

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EphB receptors interact with NMDA receptors and regulate excitatory synapse formation

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M208349200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12393905%20AND%20SRC:MED&resulttype=core&format=json

14 December 2019

1 reference