Evidence map›Paper›PMID 22902368›Full record

ArticleNature structural & molecular biology2012

Allosteric control of the ribosome by small-molecule antibiotics.

Leyi Wang, Arto Pulk, Michael R Wasserman, Michael B Feldman, Roger B Altman, Jamie H Doudna Cate, Scott C Blanchard

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

86 citing papers in PubMed, 134 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Mechanism of read-through enhancement by aminoglycosides and mefloquine.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Cryo-EM structure ofEmerging microbes & infections · 2022
    Article
  15. Review
  16. Identifying targets to prevent aminoglycoside ototoxicity.Molecular and cellular neurosciences · 2022
    Review
  17. Review
  18. Review
  19. Article
  20. Engineering ofMolecules (Basel, Switzerland) · 2021
    Article

26 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

7 authors at 4 institutions in 1 country.

Leyi WangDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Arto Pulk
Michael R Wasserman
Michael B Feldman
Roger B Altman
Jamie H Doudna Cate
Scott C Blanchard
Cornell University · USLawrence Berkeley National Laboratory · USMemorial Sloan Kettering Cancer Center · USUniversity of California, Berkeley · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
The Role of the Ribosome in the Accuracy of TranslationR01GM065050 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CATE, JAMIE H · 2001 to 2022
$7.4M
Imaging Protein Synthesis on the Ribosome using Single-Molecule FRETR01GM079238 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLANCHARD, SCOTT C · 2006 to 2023
$7.0M
smFRET Investigation of Aminoglycoside-induced OtotoxicityF31DC012026 · NIDCD · WEILL MEDICAL COLL OF CORNELL UNIV · PI WASSERMAN, MICHAEL R · 2011 to 2013
$126k
NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NIDCD NIH HHS 5F31DC012026-02NIDCD NIH HHS F31 DC012026NIGMS NIH HHS 1R01GM65050NIGMS NIH HHS 2R01GM079238NIGMS NIH HHS GM07739NIGMS NIH HHS R01 GM065050NIGMS NIH HHS R01 GM079238NIGMS NIH HHS T32 GM007739
6 · The paper itself

Abstract

Protein synthesis is targeted by numerous, chemically distinct antibiotics that bind and inhibit key functional centers of the ribosome. Using single-molecule imaging and X-ray crystallography, we show that the aminoglycoside neomycin blocks aminoacyl-transfer RNA (aa-tRNA) selection and translocation as well as ribosome recycling by binding to helix 69 (H69) of 23S ribosomal RNA within the large subunit of the Escherichia coli ribosome. There, neomycin prevents the remodeling of intersubunit bridges that normally accompanies the process of subunit rotation to stabilize a partially rotated ribosome configuration in which peptidyl (P)-site tRNA is constrained in a previously unidentified hybrid position. Direct measurements show that this neomycin-stabilized intermediate is incompatible with the translation factor binding that is required for distinct protein synthesis reactions. These findings reveal the functional importance of reversible intersubunit rotation to the translation mechanism and shed new light on the allosteric control of ribosome functions by small-molecule antibiotics.

Indexed as

Anti-Bacterial AgentsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsModels, MolecularNeomycinProtein BiosynthesisRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNA, BacterialRNA, RibosomalRNA, Transfer, Amino AcylAnti-Bacterial AgentsEscherichia coli ProteinsNeomycinRNA, BacterialRNA, RibosomalRNA, Transfer, Amino Acyl

Identifiers

PMID22902368
PMCPMC3645490
OpenAlexW2016241395

What OpenQuestion holds

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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.