Evidence map›Paper›PMID 23563139›Full record

ArticleNature structural & molecular biology2013

Binding thermodynamics of a glutamate transporter homolog.

Nicolas Reyes, SeCheol Oh, 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 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

60 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. 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
  3. Article
  4. Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Distinct roles of the NaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Linking function to global and local dynamics in an elevator-type transporter.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Rational design of ASCT2 inhibitors using an integrated experimental-computational approach.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021
    Review
  18. Kinetic mechanism of NaCommunications biology · 2021
    Article
  19. Review
  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 at 1 institution in 2 countries.

Nicolas ReyesDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA. nicolas.reyes@pasteur.fr
SeCheol Oh
Olga Boudker
Cornell University · US

Funding

Conformational Ensemble of Glutamate Transporters: Structure and IonicModulationR01NS064357 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BOUDKER, OLGA · 2009 to 2018
$3.8M
Isothermal Titration CalorimeterS10RR026970 · NCRR · WEILL MEDICAL COLL OF CORNELL UNIV · PI BOUDKER, OLGA · 2011 to 2011
$266k
NCRR NIH HHS S10 RR026970NINDS NIH HHS R01 NS064357
6 · The paper itself

Abstract

Glutamate transporters catalyze concentrative uptake of the neurotransmitter into glial cells and neurons. Their transport cycle involves binding and release of the substrate on the extra- and intracellular sides of the plasma membranes and translocation of the substrate-binding site across the lipid bilayers. The energy of the ionic gradients, mainly sodium, fuels the cycle. Here, we used a cross-linking approach to trap a glutamate transporter homolog from Pyrococcus horikoshii in key conformational states with the substrate-binding site facing either the extracellular or the intracellular side of the membrane to study binding thermodynamics. We show that the chemical potential of sodium ions in solution is exclusively coupled to substrate binding and release, not to substrate translocation. Despite the transporter's structural symmetry, the binding mechanisms are distinct on the opposite sides of the membrane and more complex than the current models suggest.

Indexed as

ThermodynamicsBinding SitesGlutamate Plasma Membrane Transport ProteinsIonsModels, MolecularNeurotransmitter AgentsProtein BindingProtein ConformationPyrococcus horikoshiiSodiumGlutamate Plasma Membrane Transport ProteinsIonsNeurotransmitter AgentsSodium

Identifiers

PMID23563139
PMCPMC3711778
OpenAlexW1975331284

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.