Evidence map›Paper›PMID 27365450›Full record

ArticleScience (New York, N.Y.)2016

Elucidation of AMPA receptor-stargazin complexes by cryo-electron microscopy.

Edward C Twomey, Maria V Yelshanskaya, Robert A Grassucci, Joachim Frank, Alexander I Sobolevsky

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

97 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. GluDs are ionotropic dopamine receptors tuned by G-proteins.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Efficient and rapid isolation of native AMPA receptor complexes for cryo-EM.Protein science : a publication of the Protein Society · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Dynamic extracellular interactions with AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

37 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Edward C TwomeyDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. Integrated Program in Cellular, Molecular, and Biomedical Studies, Columbia University, 650 West 168th Street, New York, NY 10032, USA.
Maria V YelshanskayaDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA.
Robert A GrassucciDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. Howard Hughes Medical Institute, 650 West 168th Street, New York, NY 10032, USA.
Joachim FrankDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. Department of Biological Sciences, Columbia University, 650 West 168th Street, New York, NY 10032, USA. Howard Hughes Medical Institute, 650 West 168th Street, New York, NY 10032, USA. as4005@cumc.columbia.edu jf2192@cumc.columbia.edu.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. as4005@cumc.columbia.edu jf2192@cumc.columbia.edu.
Columbia University · USHoward Hughes Medical Institute · US

Funding

UPR--MEDICAL SCIENCES CAMPUS, MBRS PROGRAMS06GM008224 · NIGMS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI SILVA, WALTER I · 1989 to 2008
$28.0M
TRAINING IN CELLULAR, MOLECULAR AND BIOPHYSICAL STUDIEST32GM008224 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIEM, RONALD K. · 1987 to 2021
$9.9M
STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
TRAINING PROGRAM IN MOLECULAR BIOPHYSICST32GM008281 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PALMER, ARTHUR G · 1988 to 2017
$5.4M
Structure and Function of AMPA subtype ionotropic glutamate receptorsR01NS083660 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KURNIKOVA, MARIA G, SOBOLEVSKY, ALEXANDER · 2013 to 2022
$4.3M
Structural elucidation of ionotropic glutamate receptor states with cryoelectron microscopyF31NS093838 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI TWOMEY, EDWARD C · 2016 to 2017
$84k
Howard Hughes Medical InstituteNIGMS NIH HHS GM008281NIGMS NIH HHS R01 GM029169NIGMS NIH HHS S06 GM008224NIGMS NIH HHS T32 GM008224NIGMS NIH HHS T32 GM008281NINDS NIH HHS F31 NS093838NINDS NIH HHS R01 NS083660
6 · The paper itself

Abstract

AMPA-subtype ionotropic glutamate receptors (AMPARs) mediate fast excitatory neurotransmission and contribute to high cognitive processes such as learning and memory. In the brain, AMPAR trafficking, gating, and pharmacology is tightly controlled by transmembrane AMPAR regulatory proteins (TARPs). Here, we used cryo-electron microscopy to elucidate the structural basis of AMPAR regulation by one of these auxiliary proteins, TARP γ2, or stargazin (STZ). Our structures illuminate the variable interaction stoichiometry of the AMPAR-TARP complex, with one or two TARP molecules binding one tetrameric AMPAR. Analysis of the AMPAR-STZ binding interfaces suggests that electrostatic interactions between the extracellular domains of AMPAR and STZ play an important role in modulating AMPAR function through contact surfaces that are conserved across AMPARs and TARPs. We propose a model explaining how TARPs stabilize the activated state of AMPARs and how the interactions between AMPARs and their auxiliary proteins control fast excitatory synaptic transmission.

Indexed as

Synaptic TransmissionAnimalsBrainCalcium ChannelsCryoelectron MicroscopyHEK293 CellsHumansModels, MolecularProtein StabilityProtein Structure, SecondaryRatsReceptors, AMPACacng2 protein, mouseCalcium Channelsglutamate receptor ionotropic, AMPA 2Receptors, AMPA

Identifiers

PMID27365450
PMCPMC5125255
OpenAlexW2474758439

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.