Evidence map›Paper›PMID 39154344›Full record

ArticleCell reports2024

Subtype-specific conformational landscape of NMDA receptor gating.

Julia Bleier, Philipe Ribeiro Furtado de Mendonca, Chris H Habrian, Cherise Stanley, Vojtech Vyklicky, Ehud Y Isacoff

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Design of (Journal of medicinal chemistry · 2025
    Article
  4. Article
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Julia BleierHelen Wills Neuroscience Institute, University of California, Berkeley, Berkeley, CA 94720, USA.
Philipe Ribeiro Furtado de MendoncaDepartment of Molecular & Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Chris H HabrianBiophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, USA.
Cherise StanleyDepartment of Molecular & Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Vojtech VyklickyDepartment of Molecular & Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Ehud Y IsacoffHelen Wills Neuroscience Institute, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Molecular & Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA; Weill Neurohub, University of California, Berkeley, Berkeley, CA 94720, USA; Molecular Biology & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: ehud@berkeley.edu.

Funding

STRUCTURAL REARRANGEMENTS IN CHANNEL GATINGR01NS035549 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 1996 to 2013
$4.1M
Conformational mechanisms of mGluR gating and regulationR01NS119826 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 2021 to 2024
$1.6M
Voltage Gating MechanismsR01GM117051 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM117051NINDS NIH HHS R01 NS035549NINDS NIH HHS R01 NS119826
6 · The paper itself

Abstract

N-methyl-D-aspartate receptors are ionotropic glutamate receptors that mediate synaptic transmission and plasticity. Variable GluN2 subunits in diheterotetrameric receptors with identical GluN1 subunits set very different functional properties. To understand this diversity, we use single-molecule fluorescence resonance energy transfer (smFRET) to measure the conformations of the ligand binding domain and modulatory amino-terminal domain of the common GluN1 subunit in receptors with different GluN2 subunits. Our results demonstrate a strong influence of the GluN2 subunits on GluN1 rearrangements, both in non-agonized and partially agonized activation intermediates, which have been elusive to structural analysis, and in the fully liganded state. Chimeric analysis reveals structural determinants that contribute to these subtype differences. Our study provides a framework for understanding the conformational landscape that supports highly divergent levels of activity, desensitization, and agonist potency in receptors with different GluN2s and could open avenues for the development of subtype-specific modulators.

Indexed as

Receptors, N-Methyl-D-AspartateAnimalsFluorescence Resonance Energy TransferHEK293 CellsHumansIon Channel GatingProtein ConformationProtein DomainsProtein SubunitsProtein SubunitsReceptors, N-Methyl-D-AspartateallosteryCP: NeuroscienceFRETGluN1GluN2Grin1Grin2NMDA receptorssingle-molecule FRET

Identifiers

PMID39154344
PMCPMC11446236

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.