Evidence map›Paper›PMID 33155546›Full record

ArticleeLife2020

Large domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters.

Xiaoyu Wang, Olga Boudker

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Multimodal dynamics control activity of a glial glutamate transporter.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. Structural basis of excitatory amino acid transporter 3 substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. 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
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Custom Design of a Humidifier Chamber forCrystal growth & design · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

2 authors at 2 institutions in 1 country.

Xiaoyu WangDepartment of Physiology and Biophysics, Weill Cornell Medicine, New York, United States.ORCID 0000-0002-8745-8238
Olga BoudkerDepartment of Physiology and Biophysics, Weill Cornell Medicine, New York, United States.ORCID 0000-0001-6965-0851
Cornell University · USHoward Hughes Medical Institute · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
The structural dynamics of a glutamate transporter homologueR37NS085318 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BOUDKER, OLGA · 2014 to 2020
$4.3M
Conformational Ensemble of Glutamate Transporters: Structure and IonicModulationR01NS064357 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BOUDKER, OLGA · 2009 to 2018
$3.8M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NCRR NIH HHS P41 RR001209NIGMS NIH HHS P41 GM103310NIH HHS S10 OD019994NINDS NIH HHS R01 NS064357NINDS NIH HHS R37 NS085318
6 · The paper itself

Abstract

Glutamate transporters are essential players in glutamatergic neurotransmission in the brain, where they maintain extracellular glutamate below cytotoxic levels and allow for rounds of transmission. The structural bases of their function are well established, particularly within a model archaeal homolog, sodium, and aspartate symporter Glt

Indexed as

Amino Acid Transport System X-AGArchaeal ProteinsBiological TransportCryoelectron MicroscopyGlutamic AcidKineticsLipid BilayersModels, MolecularProtein DomainsPyrococcus horikoshiiSodiumAmino Acid Transport System X-AGArchaeal ProteinsGlutamic AcidLipid BilayersSodiumE. coliGltPhglutamate transportersion-coupled membrane transportersmembrane structuremolecular biophysicsstructural biology

Identifiers

PMID33155546
PMCPMC7682989
OpenAlexW3096388697

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.