Evidence map›Paper›PMID 25941168›Full record

ReviewTrends in biochemical sciences2015

Emerging structural insights into the function of ionotropic glutamate receptors.

Erkan Karakas, Michael C Regan, Hiro Furukawa

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. On the molecular nature of large-pore channels.Journal of molecular biology · 2021
    Review
  19. Article
  20. 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.

Erkan KarakasCold Spring Harbor Laboratory, W.M. Keck Structural Biology Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.
Michael C ReganCold Spring Harbor Laboratory, W.M. Keck Structural Biology Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.
Hiro FurukawaCold Spring Harbor Laboratory, W.M. Keck Structural Biology Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA. Electronic address: furukawa@cshl.edu.

Funding

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
NIGMS NIH HHS GM105730NIGMS NIH HHS R01 GM105730NIMH NIH HHS MH085926NIMH NIH HHS R01 MH085926
6 · The paper itself

Abstract

Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that mediate excitatory neurotransmission crucial for brain development and function, including learning and memory formation. Recently a wealth of structural studies on iGluRs including AMPA receptors (AMPARs), kainate receptors, and NMDA receptors (NMDARs) became available. These studies showed structures of non-NMDARs including AMPAR and kainate receptor in various functional states, thereby providing the first visual sense of how non-NMDAR iGluRs may function in the context of homotetramers. Furthermore, they provided the first view of heterotetrameric NMDAR ion channels, and this illuminated the similarities with and differences from non-NMDARs, thus raising a mechanistic distinction between the two groups of iGluRs. We review mechanistic insights into iGluR functions gained through structural studies of multiple groups.

Indexed as

BrainHumansKainic Acid ReceptorsLigand-Gated Ion ChannelsProtein ConformationReceptors, AMPAReceptors, Ionotropic GlutamateReceptors, N-Methyl-D-AspartateStructure-Activity RelationshipSynaptic TransmissionKainic Acid ReceptorsLigand-Gated Ion ChannelsReceptors, AMPAReceptors, Ionotropic GlutamateReceptors, N-Methyl-D-Aspartateionotropic glutamate receptorspharmacologystructural biology

Identifiers

PMID25941168
PMCPMC4464829

What OpenQuestion holds

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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.