Evidence map›Paper›PMID 23334289›Full record

ArticleNature structural & molecular biology2013

Conformational ensemble of the sodium-coupled aspartate transporter.

Elka R Georgieva, Peter P Borbat, Christopher Ginter, Jack H Freed, Olga Boudker

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
22.8field-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

82 citing papers in PubMed, 137 citations in OpenAlex.

  1. Review
  2. The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026
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  4. Conformational free energy landscape of a glutamate transporter and microscopic details of its transport mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Distinct roles of the NaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Review

22 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 1 institution in 1 country.

Elka R GeorgievaNational Biomedical Center for Advanced Electron Spin Resonance Technology, Cornell University, Ithaca, New York, USA.
Peter P Borbat
Christopher Ginter
Jack H Freed
Olga Boudker
Cornell University · US

Funding

X-BAND PULSE ESR SPECTROMETER FOR STUDY OF LOW-TEMPERATURE IMPURITY-HELIUM P41RR016292 · NCRR · CORNELL UNIVERSITY ITHACA · PI GEORGIEVA, ELKA R · 2001 to 2011
$14.3M
TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
ELECTRON SPIN RELAXATION IN MODEL MEMBRANESR01EB003150 · NIBIB · CORNELL UNIVERSITY ITHACA · PI FREED, JACK H · 2005 to 2016
$4.9M
Conformational Ensemble of Glutamate Transporters: Structure and IonicModulationR01NS064357 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BOUDKER, OLGA · 2009 to 2018
$3.8M
ELECTRON-SPIN RELAXATION IN MODEL MEMBRANESR01GM025862 · NIGMS · CORNELL UNIVERSITY ITHACA · PI FREED, JACK H · 1985 to 2002
$941k
NCRR NIH HHS P41 RR016292NCRR NIH HHS P41-RR016292NIBIB NIH HHS R010EB003150NIBIB NIH HHS R01 EB003150NIGMS NIH HHS P41 GM103521NIGMS NIH HHS P41GM103521NIGMS NIH HHS R01 GM025862NINDS NIH HHS NS064357NINDS NIH HHS NS064357-02S1NINDS NIH HHS R01 NS064357
6 · The paper itself

Abstract

Sodium and aspartate symporter from Pyrococcus horikoshii, Glt(Ph), is a homolog of the mammalian glutamate transporters, homotrimeric integral membrane proteins that control neurotransmitter levels in brain synapses. These transporters function by alternating between outward-facing and inward-facing states, in which the substrate binding site is oriented toward the extracellular space and the cytoplasm, respectively. Here we used double electron-electron resonance (DEER) spectroscopy to probe the structure and the state distribution of the subunits in the trimer in distinct hydrophobic environments of detergent micelles and lipid bilayers. Our experiments reveal a conformational ensemble of protomers that sample the outward-facing and inward-facing states with nearly equal probabilities, indicative of comparable energies, and independently of each other. On average, the distributions varied only modestly in detergent and in bilayers, but in several mutants unique conformations were stabilized by the latter.

Indexed as

Models, MolecularProtein ConformationAmino Acid Transport Systems, AcidicArchaeal ProteinsAspartic AcidLipid BilayersMicellesProtein SubunitsPyrococcus horikoshiiSodiumSpectrum AnalysisSpin LabelsAmino Acid Transport Systems, AcidicArchaeal ProteinsAspartic AcidLipid BilayersMicellesProtein SubunitsSodiumSpin Labels

Identifiers

PMID23334289
PMCPMC3565060
OpenAlexW2001362053

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.