Evidence map›Paper›PMID 29915043›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Sodium and proton coupling in the conformational cycle of a MATE antiporter from

Derek P Claxton, Kevin L Jagessar, P Ryan Steed, Richard A Stein, Hassane S Mchaourab

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  9. Article
  10. Article
  11. Sequence and structural determinants of ligand-dependent alternating access of a MATE transporter.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Inward-facing conformation of a multidrug resistance MATE family transporter.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Structural Basis of HStructure (London, England : 1993) · 2019
    Article
  17. Broadly conserved NaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. 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

5 authors at 1 institution in 1 country.

Derek P ClaxtonDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.ORCID 0000-0002-1374-7176
Kevin L JagessarDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.
P Ryan SteedDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.
Richard A SteinDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.
Hassane S MchaourabDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232 hassane.mchaourab@vanderbilt.edu.
Vanderbilt University · US

Funding

Structural Dynamics of Multi-drug TransportersR01GM077659 · NIGMS · VANDERBILT UNIVERSITY · PI MCHAOURAB, HASSANE S · 2006 to 2023
$5.0M
NIGMS NIH HHS R01 GM077659
6 · The paper itself

Abstract

Secondary active transporters belonging to the multidrug and toxic compound extrusion (MATE) family harness the potential energy of electrochemical ion gradients to export a broad spectrum of cytotoxic compounds, thus contributing to multidrug resistance. The current mechanistic understanding of ion-coupled substrate transport has been informed by a limited set of MATE transporter crystal structures from multiple organisms that capture a 12-transmembrane helix topology adopting similar outward-facing conformations. Although these structures mapped conserved residues important for function, the mechanistic role of these residues in shaping the conformational cycle has not been investigated. Here, we use double-electron electron resonance (DEER) spectroscopy to explore ligand-dependent conformational changes of NorM from

Indexed as

ProtonsAntiportersBacterial ProteinsDoxorubicinProtein DomainsSodiumVibrio choleraeAntiportersBacterial ProteinsDoxorubicinNorM protein, bacteriaProtonsSodiumDEEREPRMATENorMtransport mechanism

Identifiers

PMID29915043
PMCPMC6142240
OpenAlexW2809234913

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.