Evidence map›Paper›PMID 37029330›Full record

ArticleBiomolecular NMR assignments2023

Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004-1024) from the NMDA receptor.

Aritra Bej, James B Ames

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2023. 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
0.4field-weighted citation impact, top 43% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Aritra BejDepartment of Chemistry, University of California, Davis, CA, 95616, USA.
James B AmesDepartment of Chemistry, University of California, Davis, CA, 95616, USA. jbames@ucdavis.edu.
University of California, Davis · US

Funding

MEMBRANE TARGETING CALCIUM SENSORS IN VISIONR01EY012347 · NEI · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI AMES, JAMES B · 1999 to 2023
$6.9M
ACQUISITION OF 500 MHZ NMR SPECTROMETERS10RR011973 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI LA MAR, GERD N · 1997 to 1997
–
NCRR NIH HHS S10 RR011973NEI 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 neuronal post-synaptic membrane are important for controlling neuroplasticity and synaptic transmission in the brain. Calmodulin (CaM) binds to the cytosolic C0 domains of both GluN1 (residues 841-865) and GluN2 (residues 1004-1024) that may play a role in the Ca

Indexed as

CalmodulinReceptors, N-Methyl-D-AspartateNeuronsNuclear Magnetic Resonance, BiomolecularProtein SubunitsCalmodulinProtein SubunitsReceptors, N-Methyl-D-AspartateC0 domainCalciumCaMGluN2NMDARNMR

Identifiers

PMID37029330
PMCPMC12554381
OpenAlexW4362703856

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.