Evidence map›Paper›PMID 29570352›Full record

ReviewAnnual review of biochemistry2018

Ribosome-Targeting Antibiotics: Modes of Action, Mechanisms of Resistance, and Implications for Drug Design.

Jinzhong Lin, Dejian Zhou, Thomas A Steitz, Yury S Polikanov, Matthieu G Gagnon

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
205citing papers in PubMed, 1 pooled it
–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

205 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Antimicrobial photodynamic therapy reprograms resistance by inducing sensitization in methicillin-resistant Staphylococcus aureus.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
    Article
  10. Article
  11. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

145 more citing papers are in PubMed but not listed here.

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.

Jinzhong LinState Key Laboratory of Genetic Engineering, School of Life Sciences, Zhongshan Hospital, Fudan University, Shanghai 200438, China; email: linjinzhong@fudan.edu.cn.
Dejian ZhouState Key Laboratory of Genetic Engineering, School of Life Sciences, Zhongshan Hospital, Fudan University, Shanghai 200438, China; email: linjinzhong@fudan.edu.cn.
Thomas A SteitzDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA; email: thomas.steitz@yale.edu.
Yury S PolikanovDepartment of Biological Sciences, and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, Illinois 60607, USA; email: yuryp@uic.edu.
Matthieu G GagnonDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA; email: thomas.steitz@yale.edu.

Funding

X-RAY ANALYSIS OF PROTEIN STRUCTURE AND FUNCTIONP01GM022778 · NIGMS · YALE UNIVERSITY · PI BREAKER, RONALD R · 1985 to 2019
$26.1M
NIGMS NIH HHS P01 GM022778
6 · The paper itself

Abstract

Genetic information is translated into proteins by the ribosome. Structural studies of the ribosome and of its complexes with factors and inhibitors have provided invaluable information on the mechanism of protein synthesis. Ribosome inhibitors are among the most successful antimicrobial drugs and constitute more than half of all medicines used to treat infections. However, bacterial infections are becoming increasingly difficult to treat because the microbes have developed resistance to the most effective antibiotics, creating a major public health care threat. This has spurred a renewed interest in structure-function studies of protein synthesis inhibitors, and in few cases, compounds have been developed into potent therapeutic agents against drug-resistant pathogens. In this review, we describe the modes of action of many ribosome-targeting antibiotics, highlight the major resistance mechanisms developed by pathogenic bacteria, and discuss recent advances in structure-assisted design of new molecules.

Indexed as

AnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBinding SitesDrug DesignDrug Resistance, MicrobialHumansModels, BiologicalModels, MolecularProtein BiosynthesisProtein Synthesis InhibitorsRibosomesStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic PeptidesProtein Synthesis Inhibitorsantibiotic resistanceantibioticsdrug designmechanisms of inhibitionprotein synthesisribosome

Identifiers

PMID29570352
PMCPMC9176271

What OpenQuestion holds

Textmetadata
LicenceTDM
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.