Evidence map›Paper›PMID 12496098›Full record

ArticleBiophysical journal2002

Staggering of subunits in NMDAR channels.

Alexander I Sobolevsky, LeeAnn Rooney, Lonnie P Wollmuth

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

26 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Properties of TriheteromericMolecular pharmacology · 2018
    Article
  6. Article
  7. Review
  8. NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  9. Binding of ArgTX-636 in the NMDA receptor ion channel.Journal of molecular biology · 2015
    Article
  10. Glutamate receptor pores.The Journal of physiology · 2015
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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 at 1 institution in 1 country.

Alexander I SobolevskyDepartment of Neurobiology and Behavior, State University of New York at Stony Brook, Stony Brook, NY 11794-5230, USA. asobolevsky@notes2.cc.sunysb.edu
LeeAnn Rooney
Lonnie P Wollmuth
Stony Brook University · US

Funding

CALCIUM TRANSPORT IN GLUTAMATE RECEPTOR CHANNELSR01NS039102 · NINDS · STATE UNIVERSITY NEW YORK STONY BROOK · PI WOLLMUTH, LONNIE P · 1999 to 2002
$797k
NINDS NIH HHS R01 NS 39102
6 · The paper itself

Abstract

Functional N-methyl-D-aspartate receptors (NMDARs) are heteromultimers formed by NR1 and NR2 subunits. The M3 segment, as contributed by NR1, forms the core of the extracellular vestibule, including binding sites for channel blockers, and represents a critical molecular link between ligand binding and channel opening. Taking advantage of the substituted cysteine accessibility method along with channel block and multivalent coordination, we studied the contribution of the M3 segment in NR2C to the extracellular vestibule. We find that the M3 segment in NR2C, like that in NR1, contributes to the core of the extracellular vestibule. However, the M3 segments from the two subunits are staggered relative to each other in the vertical axis of the channel. Compared to NR1, homologous positions in NR2C, including those in the highly conserved SYTANLAAF motif, are located about four amino acids more externally. The staggering of subunits may represent a key structural feature underlying the distinct functional properties of NMDARs.

Indexed as

AminacrineAmino Acid SequenceAnimalsCationsCell MembraneCells, CulturedCysteineExtracellular SpaceFemaleGlutamic AcidIon Channel GatingIon ChannelsMacromolecular SubstancesMembrane PotentialsMesylatesMolecular Sequence DataAminacrineCationsCysteineGlutamic AcidIon ChannelsMacromolecular SubstancesMesylatesmethanethiosulfonateNR1 NMDA receptorNR2C NMDA receptorProtein SubunitsReceptors, N-Methyl-D-AspartateSilver

Identifiers

PMID12496098
PMCPMC1302406
OpenAlexW2057900344

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.