Evidence map›Paper›PMID 25775265›Full record

ArticleNature structural & molecular biology2015

High-resolution structure of the Escherichia coli ribosome.

Jonas Noeske, Michael R Wasserman, Daniel S Terry, Roger B Altman, Scott C Blanchard, Jamie H D Cate

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.

0numbers the graph read from it
0cells of the map it votes in
171citing papers in PubMed
–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

171 citing papers in PubMed.

  1. Article
  2. Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. RiboScreenBiomedicines · 2026
    Review
  10. Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

111 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

6 authors.

Jonas Noeske1] Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA. [2] Department of Chemistry, University of California, Berkeley, Berkeley, California, USA.
Michael R WassermanDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Daniel S TerryDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Roger B AltmanDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Scott C Blanchard1] Department of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA. [2] Tri-Institutional Training Program in Chemical Biology, Weill Cornell Medical College, Rockefeller University, Memorial Sloan Kettering Cancer Center, New York, New York, USA.
Jamie H D Cate1] Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA. [2] Department of Chemistry, University of California, Berkeley, Berkeley, California, USA.

Funding

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
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
NIGMS NIH HHS 2R01GM079238NIGMS NIH HHS R01 GM065050NIGMS NIH HHS R01 GM079238NIGMS NIH HHS R01 GM105404NIGMS NIH HHS R01GM105404NIGMS NIH HHS R01-GM65050
6 · The paper itself

Abstract

Protein synthesis by the ribosome is highly dependent on the ionic conditions in the cellular environment, but the roles of ribosome solvation have remained poorly understood. Moreover, the functions of modifications to ribosomal RNA and ribosomal proteins have also been unclear. Here we present the structure of the Escherichia coli 70S ribosome at 2.4-Å resolution. The structure reveals details of the ribosomal subunit interface that are conserved in all domains of life, and it suggests how solvation contributes to ribosome integrity and function as well as how the conformation of ribosomal protein uS12 aids in mRNA decoding. This structure helps to explain the phylogenetic conservation of key elements of the ribosome, including post-transcriptional and post-translational modifications, and should serve as a basis for future antibiotic development.

Indexed as

Models, MolecularBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsProtein BiosynthesisProtein Structure, TertiaryProtein SubunitsRibosomesRNA, MessengerEscherichia coli ProteinsProtein SubunitsRNA, Messenger

Identifiers

PMID25775265
PMCPMC4429131

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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.