Evidence map›Paper›PMID 38551344›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2024

Structural analysis of resistance-nodulation cell division transporters.

Philip A Klenotic, Edward W Yu

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Structural and functional analysis of theProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Regulation, structure, and activity of theAntimicrobial agents and chemotherapy · 2025
    Review
  11. Review
  12. 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 1 institution in 1 country.

Philip A KlenoticDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.ORCID 0000-0001-8429-0145
Edward W YuDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.ORCID 0000-0001-5912-1227
University School · US

Funding

GONOCOCCI: GENETICS OF RESISTANCE TO PMN PROTEINSR01AI021150 · NIAID · EMORY UNIVERSITY · PI SHAFER, WILLIAM MAURICE · 1985 to 2025
$5.5M
Emerging antibiotic resistance in Gram-negative pathogensR01AI145069 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI YU, EDWARD W · 2019 to 2023
$3.3M
Emerging multidrug resistance mechanisms in CampylobacterR01AI140669 · NIAID · IOWA STATE UNIVERSITY · PI YU, EDWARD W, ZHANG, QIJING · 2020 to 2024
$3.2M
De Novo Synthesis, and Functional and Structural Characterization of Novel Aminoglycoside Analogues to Bypass Resistance Mechanisms and Optimize SelectivityR01AI154860 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI KIRBY, JAMES E, O'DOHERTY, GEORGE A · 2020 to 2023
$3.1M
HHS | NIH | Office of Extramural Research (OER) R01AI021150HHS | NIH | Office of Extramural Research (OER) R01AI140669HHS | NIH | Office of Extramural Research (OER) R01AI145069HHS | NIH | Office of Extramural Research (OER) R01AI154860HHS | NIH | Office of Extramural Research (OER) R01AI1572080NIAID NIH HHS R01 AI021150NIAID NIH HHS R01 AI140669NIAID NIH HHS R01 AI145069NIAID NIH HHS R01 AI154860
6 · The paper itself

Abstract

SUMMARYInfectious bacteria have both intrinsic and acquired mechanisms to combat harmful biocides that enter the cell. Through adaptive pressures, many of these pathogens have become resistant to many, if not all, of the current antibiotics used today to treat these often deadly infections. One prominent mechanism is the upregulation of efflux systems, especially the resistance-nodulation-cell division class of exporters. These tripartite systems consist of an inner membrane transporter coupled with a periplasmic adaptor protein and an outer membrane channel to efficiently transport a diverse array of substrates from inside the cell to the extracellular space. Detailed mechanistic insight into how these inner membrane transporters recognize and shuttle their substrates can ultimately inform both new antibiotic and efflux pump inhibitor design. This review examines the structural basis of substrate recognition of these pumps and the molecular mechanisms underlying multidrug extrusion, which in turn mediate antimicrobial resistance in bacterial pathogens.

Indexed as

Anti-Bacterial AgentsMembrane Transport ProteinsBacteriaBacterial ProteinsBiological TransportCell DivisionDrug Resistance, BacterialDrug Resistance, Multiple, BacterialModels, MolecularAnti-Bacterial AgentsBacterial ProteinsMembrane Transport Proteinscryo-EMefflux pumpsRND transportersX-ray

Identifiers

PMID38551344
PMCPMC11332337
OpenAlexW4393318042

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.