Evidence map›Paper›PMID 23033476›Full record

ArticleMolecular & cellular proteomics : MCP2012

Dynamics of ribosomal protein S1 on a bacterial ribosome with cross-linking and mass spectrometry.

Matthew A Lauber, Juri Rappsilber, James P Reilly

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Translation initiation site of mRNA is selected through dynamic interaction with the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. A translational riboswitch coordinates nascent transcription-translation coupling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. ETD-Cleavable Linker for Confident Cross-linked Peptide Identifications.Journal of the American Society for Mass Spectrometry · 2019
    Article
  13. Review
  14. Review
  15. Article
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  19. Mass spectrometric identification of phenol-soluble modulins in the ATCC® 43300 standard strain of methicillin-resistant Staphylococcus aureus harboring two distinct phenotypes.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2017
    Article
  20. 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

3 authors at 2 institutions in 3 countries.

Matthew A LauberDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Juri Rappsilber
James P Reilly
Indiana University Bloomington · USTechnische Universität Berlin · DE

Funding

Wellcome Trust 077707Wellcome Trust 084229Wellcome Trust 091020Wellcome Trust 092076
6 · The paper itself

Abstract

Ribosomal protein S1 has been shown to be a significant effector of prokaryotic translation. The protein is in fact capable of efficiently initiating translation, regardless of the presence of a Shine-Dalgarno sequence in mRNA. Structural insights into this process have remained elusive, as S1 is recalcitrant to traditional techniques of structural analysis, such as x-ray crystallography. Through the application of protein cross-linking and high resolution mass spectrometry, we have detailed the ribosomal binding site of S1 and have observed evidence of its dynamics. Our results support a previous hypothesis that S1 acts as the mRNA catching arm of the prokaryotic ribosome. We also demonstrate that in solution the major domains of the 30S subunit are remarkably flexible, capable of moving 30-50Å with respect to one another.

Indexed as

Peptide Chain Initiation, TranslationalBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsMass SpectrometryNucleic Acid ConformationProtein BiosynthesisRibosomal ProteinsRibosome Subunits, Small, BacterialRNA, MessengerEscherichia coli ProteinsRibosomal Proteinsribosomal protein S1, E coliRNA, Messenger

Identifiers

PMID23033476
PMCPMC3518124
OpenAlexW2153707027

What OpenQuestion holds

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LicenceCC BY-NC
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.