Evidence map›Paper›PMID 21609840›Full record

ArticleChemistry & biology2011

Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases.

Aleksandra Mikolajka, Hanqing Liu, Yuanwei Chen, Agata L Starosta, Viter Márquez, Marina Ivanova, Barry S Cooperman, Daniel N Wilson

Abstract read
In one paragraph

Article in Chemistry & biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Structures of the orthosomycin antibiotics avilamycin and evernimicin in complex with the bacterial 70S ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Cryo-EM structure of the tetracycline resistance protein TetM in complex with a translating ribosome at 3.9-Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. The bacterial translation stress response.FEMS microbiology reviews · 2014
    Review
  17. Bioactive oligosaccharide natural products.Natural product reports · 2014
    Review
  18. Review
  19. Article
  20. Structural basis for potent inhibitory activity of the antibiotic tigecycline during protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

8 authors at 3 institutions in 2 countries.

Aleksandra MikolajkaGene Center and Department of Biochemistry, University of Munich, Germany.
Hanqing Liu
Yuanwei Chen
Agata L Starosta
Viter Márquez
Marina Ivanova
Barry S Cooperman
Daniel N Wilson
Ludwig-Maximilians-Universität München · DEUniversity of Pennsylvania · USCenter for Integrated Protein Science Munich · DE

Funding

Dynamics of Ribosomal Protein SynthesisR01GM071014 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI COOPERMAN, BARRY S. · 2004 to 2011
$2.5M
NIGMS NIH HHS R01 GM071014
6 · The paper itself

Abstract

The ribosome is a major target in the bacterial cell for antibiotics. Here, we dissect the effects that the thiopeptide antibiotics thiostrepton (ThS) and micrococcin (MiC) as well as the orthosomycin antibiotic evernimicin (Evn) have on translational GTPases. We demonstrate that, like ThS, MiC is a translocation inhibitor, and that the activation by MiC of the ribosome-dependent GTPase activity of EF-G is dependent on the presence of the ribosomal proteins L7/L12 as well as the G' subdomain of EF-G. In contrast, Evn does not inhibit translocation but is a potent inhibitor of back-translocation as well as IF2-dependent 70S-initiation complex formation. Collectively, these results shed insight not only into fundamental aspects of translation but also into the unappreciated specificities of these classes of translational inhibitors.

Indexed as

AminoglycosidesAnti-Bacterial AgentsBacteriocinsBinding SitesPeptide Elongation Factor GPeptidesProkaryotic Initiation Factor-2Protein Structure, TertiaryThiostreptonTranslocation, GeneticAminoglycosidesAnti-Bacterial AgentsBacteriocinsevernimicinmicrococcinPeptide Elongation Factor GPeptidesProkaryotic Initiation Factor-2Thiostrepton

Identifiers

PMID21609840
PMCPMC3102230
OpenAlexW2085054490

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.