Evidence map›Paper›PMID 36739573›Full record

ArticleBiomolecular NMR assignments2023

Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841-865) of the NMDA receptor.

Aritra Bej, James B Ames

Open access · hybridAbstract read
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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. 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 2 institutions 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 · USUniversity of California System · US

Funding

MEMBRANE TARGETING CALCIUM SENSORS IN VISIONR01EY012347 · NEI · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI AMES, JAMES B · 1999 to 2023
$6.9M
L-type Ca2+ Channel Regulation by Calmodulin and CaBP1R01GM130925 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI AMES, JAMES B · 2020 to 2023
$1.3M
NEI NIH HHS R01 EY012347NIGMS NIH HHS R01 GM130925
6 · The paper itself

Abstract

Neuroplasticity and synaptic transmission in the brain are regulated by N-methyl-D-aspartate receptors (NMDARs) that consist of hetero-tetrameric combinations of the glycine-binding GluN1 and glutamate-binding GluN2 subunits. Calmodulin (CaM) binds to the cytosolic C0 domain of GluN1 (residues 841-865) that may play a role in the Ca

Indexed as

CalmodulinReceptors, N-Methyl-D-AspartateHumansNuclear Magnetic Resonance, BiomolecularSignal TransductionCalmodulinReceptors, N-Methyl-D-AspartateC0 domainCalciumCaMGluN1NMDARNMR

Identifiers

PMID36739573
PMCPMC10232624
OpenAlexW4319262350

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.