Evidence map›Paper›PMID 26282925›Full record

ReviewCurrent opinion in structural biology2015

A structural biology perspective on NMDA receptor pharmacology and function.

Michael C Regan, Annabel Romero-Hernandez, Hiro Furukawa

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Receptor-Dependent and Independent Regulation of Voltage-Gated CaInternational journal of molecular sciences · 2021
    Review
  18. Review
  19. Article
  20. Rislenemdaz treatment in the lateral habenula improves despair-like behavior in mice.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2020
    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

3 authors.

Michael C ReganCold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, United States.
Annabel Romero-HernandezCold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, United States; Watson School of Biological Sciences, United States.
Hiro FurukawaCold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, United States; Watson School of Biological Sciences, United States. Electronic address: furukawa@cshl.edu.

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Structures and reagents of NMDA receptorsR01MH085926 · NIMH · COLD SPRING HARBOR LABORATORY · PI Hiroyasu Furukawa · 2010 to 2026
$8.9M
STRUCTURE AND FUNCTION OF HETERO-MULTIMERIC GLUTAMATE RECEPTORSR01GM105730 · NIGMS · COLD SPRING HARBOR LABORATORY · PI FURUKAWA, HIROYASU · 2014 to 2017
$2.0M
NCRR NIH HHS P41 RR012408NIGMS NIH HHS GM105730NIGMS NIH HHS R01 GM105730NIMH NIH HHS MH085926NIMH NIH HHS R01 MH085926
6 · The paper itself

Abstract

N-methyld-aspartate receptors (NMDARs) belong to the large family of ionotropic glutamate receptors (iGluRs), which are critically involved in basic brain functions as well as multiple neurological diseases and disorders. The NMDARs are large heterotetrameric membrane protein complexes. The extensive extracellular domains recognize neurotransmitter ligands and allosteric compounds and translate the binding information to regulate activity of the transmembrane ion channel. Here, we review recent advances in the structural biology of NMDARs with a focus on pharmacology and function. Structural analysis of the isolated extracellular domains in combination with the intact heterotetrameric NMDAR structure provides important insights into how this sophisticated ligand-gated ion channel may function.

Indexed as

Allosteric RegulationAnimalsIon ChannelsLearningLigandsMammalsMemoryProtein BindingProtein ConformationReceptors, N-Methyl-D-AspartateIon ChannelsLigandsReceptors, N-Methyl-D-Aspartate

Identifiers

PMID26282925
PMCPMC4641752

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.