Evidence map›Paper›PMID 30746819›Full record

ReviewProtein science : a publication of the Protein Society2019

Ribosome protection by ABC-F proteins-Molecular mechanism and potential drug design.

Rya Ero, Veerendra Kumar, Weixin Su, Yong-Gui Gao

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.7field-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

35 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Ribosomal protection as a linezolid resistance mechanism inAntimicrobial agents and chemotherapy · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Ribosomal protection as a linezolid resistance mechanism inbioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Vancomycin Resistance inMicroorganisms · 2022
    Review
  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

4 authors at 3 institutions in 1 country.

Rya EroSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Veerendra KumarA*STAR (Agency for Science, Technology and Research), Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673.
Weixin SuSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Yong-Gui GaoSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Nanyang Technological University · SGAgency for Science, Technology and Research · SGInstitute of Molecular and Cell Biology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the ATP-binding cassette F (ABC-F) proteins confer resistance to several classes of clinically important antibiotics through ribosome protection. Recent structures of two ABC-F proteins, Pseudomonas aeruginosa MsrE and Bacillus subtilis VmlR bound to ribosome have shed light onto the ribosome protection mechanism whereby drug resistance is mediated by the antibiotic resistance domain (ARD) connecting the two ATP binding domains. ARD of the E site bound MsrE and VmlR extends toward the drug binding region within the peptidyl transferase center (PTC) and leads to conformational changes in the P site tRNA acceptor stem, the PTC, and the drug binding site causing the release of corresponding drugs. The structural similarities and differences of the MsrE and VmlR structures likely highlight an universal ribosome protection mechanism employed by antibiotic resistance (ARE) ABC-F proteins. The variable ARD domains enable this family of proteins to adapt the protection mechanism for several classes of ribosome-targeting drugs. ARE ABC-F genes have been found in numerous pathogen genomes and multi-drug resistance conferring plasmids. Collectively they mediate resistance to a broader range of antimicrobial agents than any other group of resistance proteins and play a major role in clinically significant drug resistance in pathogenic bacteria. Here, we review the recent structural and biochemical findings on these emerging resistance proteins, offering an update of the molecular basis and implications for overcoming ABC-F conferred drug resistance.

Indexed as

Drug DesignDrug Resistance, BacterialAnimalsAnti-Bacterial AgentsATP-Binding Cassette TransportersBacteriaBacterial InfectionsBacterial ProteinsHumansModels, MolecularAnti-Bacterial AgentsATP-Binding Cassette TransportersBacterial ProteinsABC-Fand antibiotic designantibiotic resistancelincosamidesmacrolidesoxazolidinonesphenicolspleuromutilinsribosome protectionstreptogramins

Identifiers

PMID30746819
PMCPMC6423996
OpenAlexW2911786618

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.