Evidence map›Paper›PMID 30082384›Full record

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

Structure of the

Victor Ovchinnikov, Tracy A Stone, Charles M Deber, Martin Karplus

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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

32 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.bioRxiv : the preprint server for biology · 2026
    Article
  4. Phenotypic and Genomic Profiling ofAntibiotics (Basel, Switzerland) · 2026
    Article
  5. Review
  6. Article
  7. Design principles of the common Gly-X6-Gly membrane protein building block.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Human Gut Antibiotic Resistome and Progression of Diabetes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Asymmetric protonation of glutamate residues drives a preferred transport pathway in EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

4 authors at 3 institutions in 3 countries.

Victor OvchinnikovDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138; ovchinnv@georgetown.edu deber@sickkids.ca marci@tammy.harvard.edu.
Tracy A StoneDivision of Molecular Medicine, Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Charles M DeberDivision of Molecular Medicine, Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada; ovchinnv@georgetown.edu deber@sickkids.ca marci@tammy.harvard.edu.
Martin KarplusDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138; ovchinnv@georgetown.edu deber@sickkids.ca marci@tammy.harvard.edu.
Harvard University · USHospital for Sick Children · CAUniversity of Toronto · CA

Funding

Modeling atomic structure of the EmrE multidrug pump to design inhibitor peptidesR03AI111416 · NIAID · HARVARD UNIVERSITY · PI KARPLUS, MARTIN · 2014 to 2015
$169k
CIHR 376666NIAID NIH HHS R03 AI111416
6 · The paper itself

Abstract

Small multidrug resistance (SMR) pumps represent a minimal paradigm of proton-coupled membrane transport in bacteria, yet no high-resolution structure of an SMR protein is available. Here, atomic-resolution structures of the

Indexed as

AntiportersDrug Resistance, Multiple, BacterialEscherichia coli ProteinsMolecular Dynamics SimulationProtein MultimerizationCatalytic DomainEscherichia coliPeptidesProtein Structure, QuaternaryAntiportersEmrE protein, E coliEscherichia coli ProteinsPeptidesdrug resistancemembrane proteinsmolecular dynamicsstapled peptidesstructure refinement

Identifiers

PMID30082384
PMCPMC6112734
OpenAlexW2886754164

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.