Induction of dendritic spines by an extracellular domain of AMPA receptor subunit GluR2. (Q44540735)

4 December 2017

title

Induction of dendritic spines by an extracellular domain of AMPA receptor subunit GluR2. (English)

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4 December 2017

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3

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4 December 2017

Maria Passafaro

1

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4 December 2017

Terunaga Nakagawa

series ordinal

2

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4 December 2017

Morgan Sheng

series ordinal

4

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4 December 2017

language of work or name

English

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publication date

1 August 2003

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4 December 2017

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4 December 2017

volume

424

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4 December 2017

issue

6949

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4 December 2017

page(s)

677-681

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Dendritic spine geometry is critical for AMPA receptor expression in hippocampal CA1 pyramidal neurons

4 December 2017

cites work

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Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation

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LTP promotes formation of multiple spine synapses between a single axon terminal and a dendrite.

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

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Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons

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Differences in Ca2+ permeability of AMPA-type glutamate receptor channels in neocortical neurons caused by differential GluR-B subunit expression

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

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

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

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N-terminal domains in the NR2 subunit control desensitization of NMDA receptors

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Glycine-independent NMDA receptor desensitization: localization of structural determinants

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Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor.

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

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

21 January 2018

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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

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The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn

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EphB receptors interact with NMDA receptors and regulate excitatory synapse formation

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Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons

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Regulation of dendritic spine morphology and synaptic function by Shank and Homer

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Subunit-specific temporal and spatial patterns of AMPA receptor exocytosis in hippocampal neurons

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A system for stable expression of short interfering RNAs in mammalian cells

21 January 2018

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Differential dependence on GluR2 expression of three characteristic features of AMPA receptors

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein

1 reference

https://api.crossref.org/works/10.1038%2FNATURE01781

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NATURE01781

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Dimensions Publication ID

4 December 2017

1044600378

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