Evidence map›Paper›PMID 25829490›Full record

ArticleThe Journal of biological chemistry2015

Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.

Rita E Sirrieh, David M MacLean, Vasanthi Jayaraman

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
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  12. Article
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  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017
    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.

Rita E SirriehFrom the Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center, Houston, Texas 77030.
David M MacLeanFrom the Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center, Houston, Texas 77030.
Vasanthi JayaramanFrom the Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center, Houston, Texas 77030 vasanthi.jayaraman@uth.tmc.edu.

Funding

HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
Structure and Function of NMDA ReceptorsR01GM094246 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2011 to 2016
$2.0M
TARP modulation of AMPA receptorsR01GM113212 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2015 to 2017
$897k
NIGMS NIH HHS 2T32GM008280NIGMS NIH HHS R01GM094245NIGMS NIH HHS R01 GM094246NIGMS NIH HHS R01 GM113212NIGMS NIH HHS R01GM113212NIGMS NIH HHS T32 GM008280
6 · The paper itself

Abstract

The N-methyl-d-aspartate (NMDA) subtype of the ionotropic glutamate receptors is the primary mediator of calcium-permeable excitatory neurotransmission in the central nervous system. Subunit composition and binding of allosteric modulators to the amino-terminal domain determine the open probability of the channel. By using luminescence resonance energy transfer with functional receptors expressed in CHO cells, we show that the cleft of the amino-terminal domain of the GluN2B subunit, which has a lower channel open probability, is on average more closed than the GluN2A subunit, which has a higher open probability. Furthermore, the GluN1 amino-terminal domain adopts a more open conformation when coassembled with GluN2A than with GluN2B. Binding of spermine, an allosteric potentiator, opens the amino-terminal domain cleft of both the GluN2B subunit and the adjacent GluN1 subunit. These studies provide direct structural evidence that the inherent conformations of the amino-terminal domains vary based on the subunit and match the reported open probabilities for the receptor.

Indexed as

Allosteric RegulationAnimalsCHO CellsCricetinaeCricetulusIon Channel GatingProtein BindingProtein Structure, TertiaryRatsReceptors, N-Methyl-D-AspartateSpermineNR1 NMDA receptorNR2B NMDA receptorReceptors, N-Methyl-D-AspartateSpermineconformational changefluorescencefluorescence resonance energy transfer (FRET)glutamate receptorligand-binding protein

Identifiers

PMID25829490
PMCPMC4432297

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.