Chemical shift assignments of the α-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841-865) from the NMDA receptor.

Aritra Bej, Johannes W Hell, James B Ames

Abstract read

In one paragraph

Article in Biomolecular NMR assignments, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

NMDA Receptor Regulation by Calmodulin and α-Actinin-1.Biomolecules · 2026
Review

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

3 authors.

Aritra BejDepartments of Chemistry, University of California, Davis, CA, 95616, USA.

Johannes W HellDepartments of Pharmacology, University of California, Davis, CA, 95616, USA.

James B AmesDepartments of Chemistry, University of California, Davis, CA, 95616, USA. jbames@ucdavis.edu.

Funding

MEMBRANE TARGETING CALCIUM SENSORS IN VISIONR01EY012347 · NEI · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI AMES, JAMES B · 1999 to 2023

$6.9M

NEI NIH HHS R01 EY012347NEI NIH HHS R01-EY012347

6 · The paper itself

Abstract

N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the brain are important for controlling neuronal excitability to promote synaptic plasticity. The cytoskeletal protein, α-actinin-1 (100 kDa, called ACTN1) binds to the cytosolic C0 domain of GluN1 (residues 841-865) that may play a role in the Ca

Indexed as

ActininProtein DomainsReceptors, N-Methyl-D-AspartateCytosolEF Hand MotifsHumansNuclear Magnetic Resonance, BiomolecularProtein BindingActininReceptors, N-Methyl-D-Aspartatea-actininC0 domainCalciumGluN1NMDA receptorNMR

Identifiers

PMID39207574

DOI10.1007/s12104-024-10194-2

PMCPMC11511685

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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.