Evidence map›Paper›PMID 29915058›Full record

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

Broadly conserved Na

Emel Ficici, Wenchang Zhou, Steven Castellano, José D Faraldo-Gómez

Abstract 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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. The structure of theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
  9. Article
  10. The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  11. Article
  12. 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
  13. Review
  14. Article
  15. 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
  16. Article
  17. Structural Basis of HStructure (London, England : 1993) · 2019
    Article
  18. Sodium and proton coupling in the conformational cycle of a MATE antiporter fromProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. 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

4 authors.

Emel FiciciTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Wenchang ZhouTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Steven CastellanoTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
José D Faraldo-GómezTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892 jose.faraldo@nih.gov.

Funding

Molecular Mechanisms in Membrane Bioenergetics, Transport and SignalingZIAHL006203 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FARALDO-GÓMEZ, JOSE · 2015 to 2023
$15.4M
6 · The paper itself

Abstract

Multidrug and toxic-compound extrusion (MATE) proteins comprise an important but largely uncharacterized family of secondary-active transporters. In both eukaryotes and prokaryotes, these transporters protect the cell by catalyzing the efflux of a broad range of cytotoxic compounds, including human-made antibiotics and anticancer drugs. MATEs are thus potential pharmacological targets against drug-resistant pathogenic bacteria and tumor cells. The activity of MATEs is powered by transmembrane electrochemical ion gradients, but their molecular mechanism and ion specificity are not understood, in part because high-quality structural information is limited. Here, we use computational methods to study PfMATE, from

Indexed as

Amino Acid MotifsArchaeal ProteinsBinding SitesCarrier ProteinsPyrococcus furiosusStructure-Activity RelationshipArchaeal ProteinsCarrier Proteinsmembrane proteinsmolecular dynamicsmultidrug resistanceon selectivitysecondary-active transporters

Identifiers

PMID29915058
PMCPMC6142261

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.