Evidence map›Paper›PMID 23090316›Full record

ArticleMolecular bioSystems2012

Measuring the dynamics of E. coli ribosome biogenesis using pulse-labeling and quantitative mass spectrometry.

Stephen S Chen, Edit Sperling, Josh M Silverman, Joseph H Davis, James R Williamson

Abstract read
In one paragraph

Article in Molecular bioSystems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.9field-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

45 citing papers in PubMed, 71 citations in OpenAlex.

  1. Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
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  7. Life sets off a cascade of machines.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Autonomous ribosome biogenesis in vitro.Nature communications · 2025
    Article
  9. Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
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  19. Ribosome Protein Composition Mediates Translation during theInternational journal of molecular sciences · 2023
    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

5 authors at 1 institution in 1 country.

Stephen S ChenDepartment of Molecular Biology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Edit Sperling
Josh M Silverman
Joseph H Davis
James R Williamson
Scripps Research Institute · US

Funding

Assembly of E. coli ribosomes in vitro and in cellsR37GM053757 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILLIAMSON, JAMES R · 2008 to 2017
$5.1M
NIGMS NIH HHS R37 GM053757NIGMS NIH HHS R37-GM053757
6 · The paper itself

Abstract

The ribosome is an essential organelle responsible for cellular protein synthesis. Until recently, the study of ribosome assembly has been largely limited to in vitro assays, with few attempts to reconcile these results with the more complex ribosome biogenesis process inside the living cell. Here, we characterize the ribosome synthesis and assembly pathway for each of the E. coli ribosomal protein (r-protein) in vivo using a stable isotope pulse-labeling timecourse. Isotope incorporation into assembled ribosomes was measured by quantitative mass spectrometry (qMS) and fit using steady-state flux models. Most r-proteins exhibit precursor pools ranging in size from 0% to 7% of completed ribosomes, and the sizes of these individual r-protein pools correlate well with the order of r-protein binding in vitro. Additionally, we observe anomalously large precursor pools for specific r-proteins with known extra-ribosomal functions, as well as three r-proteins that apparently turnover during steady-state growth. Taken together, this highly precise, time-dependent proteomic qMS approach should prove useful in future studies of ribosome biogenesis and could be easily extended to explore other complex biological processes in a cellular context.

Indexed as

Escherichia coliEscherichia coli ProteinsMass SpectrometryNitrogen IsotopesProteomicsRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNA, RibosomalEscherichia coli ProteinsNitrogen IsotopesRibosomal ProteinsRNA, Ribosomal

Identifiers

PMID23090316
PMCPMC3501348
OpenAlexW2115336799

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.