Evidence map›Paper›PMID 19946275›Full record

ArticleNature chemical biology2010

Aminoglycoside activity observed on single pre-translocation ribosome complexes.

Michael B Feldman, Daniel S Terry, Roger B Altman, Scott C Blanchard

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
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  10. Real-time measurements of aminoglycoside effects on protein synthesis in live cells.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. The genusRSC advances · 2020
    Review
  13. The structural basis for inhibition of ribosomal translocation by viomycin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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 2 institutions in 1 country.

Michael B FeldmanDepartment of Physiology and Biophysics, Weill Medical College of Cornell University, New York, New York, USA.
Daniel S Terry
Roger B Altman
Scott C Blanchard
Cornell University · USTri-Institutional PhD Program in Chemical Biology · US

Funding

Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
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
NIGMS NIH HHS R01 GM079238NIGMS NIH HHS T32 GM007739
6 · The paper itself

Abstract

Aminoglycoside-class antibiotics bind directly to ribosomal RNA, imparting pleiotropic effects on ribosome function. Despite in-depth structural investigations of aminoglycoside-RNA oligonucleotide and aminoglycoside-ribosome interactions, mechanisms explaining the unique ribosome inhibition profiles of chemically similar aminoglycosides remain elusive. Here, using single-molecule fluorescence resonance energy transfer (smFRET) methods, we show that high-affinity aminoglycoside binding to the conserved decoding site region of the functional pre-translocation ribosome complex specifically remodels the nature of intrinsic dynamic processes within the particle. The extents of these effects, which are distinct for each member of the aminoglycoside class, strongly correlate with their inhibition of EF-G-catalyzed translocation. Neomycin, a 4,5-linked aminoglycoside, binds with lower affinity to one or more secondary binding sites, mediating distinct structural and dynamic perturbations that further enhance translocation inhibition. These new insights help explain why closely related aminoglycosides elicit pleiotropic translation activities and demonstrate the potential utility of smFRET as a tool for dissecting the mechanisms of antibiotic action.

Indexed as

AminoglycosidesBinding SitesConserved SequenceCryoelectron MicroscopyFluorescence Resonance Energy TransferKanamycinKineticsModels, MolecularMutationNeomycinOligonucleotidesProtein BindingProtein TransportReproducibility of ResultsRibosomesRNAAminoglycosidesKanamycinNeomycinOligonucleotidesRNARNA, Transfer

Identifiers

PMID19946275
PMCPMC2914512
OpenAlexW2003187423

What OpenQuestion holds

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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.