Evidence map›Paper›PMID 30500536›Full record

ArticleCell2018

Mechanisms for Zinc and Proton Inhibition of the GluN1/GluN2A NMDA Receptor.

Farzad Jalali-Yazdi, Sandipan Chowdhury, Craig Yoshioka, Eric Gouaux

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.1field-weighted citation impact, top 2% of its field
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

70 citing papers in PubMed, 125 citations in OpenAlex.

  1. Trial
  2. Imaging and recording of synaptic zinc in the brain by covalent chemistry-based semisynthetic biosensors.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Dimeric gold nanoparticles enable multiplexed labeling in cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025
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10 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Farzad Jalali-YazdiVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Sandipan ChowdhuryVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Craig YoshiokaVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Eric GouauxVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA; Department of Biomedical Engineering, Oregon Health and Science University, Portland, OR 97239, USA; Howard Hughes Medical Institute, Oregon Health and Science University, Portland, OR 97239, USA. Electronic address: gouauxe@ohsu.edu.
Oregon Health & Science University · USVollum Institute · US

Funding

3D STRUCTURE/FUNCTION OF LIGAND GATED ION CHANNELSR01NS038631 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI GOUAUX, JAMES E · 1999 to 2024
$6.7M
Elucidating the Structural Mechanism of NMDA Receptor Modulation by Cryo-Electron MicroscopyF32MH115595 · NIMH · OREGON HEALTH & SCIENCE UNIVERSITY · PI JALALI-YAZDI, FARZAD · 2017 to 2020
$192k
Howard Hughes Medical InstituteNIMH NIH HHS F32 MH115595NINDS NIH HHS R01 NS038631
6 · The paper itself

Abstract

N-methyl-D-aspartate receptors (NMDARs) play essential roles in memory formation, neuronal plasticity, and brain development, with their dysfunction linked to a range of disorders from ischemia to schizophrenia. Zinc and pH are physiological allosteric modulators of NMDARs, with GluN2A-containing receptors inhibited by nanomolar concentrations of divalent zinc and by excursions to low pH. Despite the widespread importance of zinc and proton modulation of NMDARs, the molecular mechanism by which these ions modulate receptor activity has proven elusive. Here, we use cryoelectron microscopy to elucidate the structure of the GluN1/GluN2A NMDAR in a large ensemble of conformations under a range of physiologically relevant zinc and proton concentrations. We show how zinc binding to the amino terminal domain elicits structural changes that are transduced though the ligand-binding domain and result in constriction of the ion channel gate.

Indexed as

ProtonsAllosteric RegulationAnimalsCryoelectron MicroscopyHydrogen-Ion ConcentrationMultiprotein ComplexesProtein DomainsRatsReceptors, N-Methyl-D-AspartateSf9 CellsSpodopteraZincMultiprotein ComplexesProtonsReceptors, N-Methyl-D-AspartateZincallosteric modulationglutamate receptorligand-gated ion channelneurotransmitter receptorproton-inhibitionstructural biologysynapsezinc-inhibition

Identifiers

PMID30500536
PMCPMC6333211
OpenAlexW2884221774

What OpenQuestion holds

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Registered trials

None linked

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.