Evidence map›Paper›PMID 18654865›Full record

ReviewMolecular neurobiology2008

Shuffling the deck anew: how NR3 tweaks NMDA receptor function.

Nora A Cavara, Michael Hollmann

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Calcium-Handling Defects and Neurodegenerative Disease.Cold Spring Harbor perspectives in biology · 2020
    Review
  6. Frontiers in physiology · 2020
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Inflammatory sensitization of nociceptors depends on activation of NMDA receptors in DRG satellite cells.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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.

Nora A CavaraInternational Graduate School of Neuroscience (IGSN), Ruhr University Bochum, Bochum, Germany.
Michael Hollmann
Ruhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N-methyl-D -aspartate (NMDA) receptors are the most complex members in the family of ionotropic glutamate receptors. They are involved in long-term potentiation and underlie higher cognitive functions like memory formation and learning. On the other hand, overstimulation of NMDA receptors (NMDARs), leading to a massive influx of Ca(2+) ions into the cell, is linked to neurodegenerative disorders such as for example Huntington's disease and epilepsy. NMDARs are generally considered to be heteromeric tetramers and are conventionally thought to assemble from NR1 splice variants and NR2 subunits, which determine crucial channel properties. With the recent discovery of the functionally different NR3 subunits, many of the known features of NMDARs are being reassessed: The presence of NR3 in NMDARs decreases Mg(2+) sensitivity and Ca(2+) permeability and reduces agonist-induced current responses. Between altering those essential key characteristics of conventional NMDARs and forming a new class of excitatory glycine receptors when coassembling with NR1, the NR3 subunits give rise to a functionally entirely new array of "NMDA" receptors. Understanding the multifaceted influence of NR3 is imperative to further the understanding of the complex role of NMDARs in neurotransmission and higher brain functions.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsElectrophysiologyHumansLigandsMolecular Sequence DataProtein IsoformsProtein Structure, SecondaryProtein SubunitsReceptors, N-Methyl-D-AspartateLigandsNR3A NMDA receptorProtein IsoformsProtein SubunitsReceptors, N-Methyl-D-Aspartate

Identifiers

PMID18654865
OpenAlexW2026967783

What OpenQuestion holds

Textmetadata
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.