Evidence map›Paper›PMID 19469554›Full record

ArticleJournal of proteome research2009

Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes.

George Y Soung, Jennifer L Miller, Hasan Koc, Emine C Koc

Abstract read
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Molecular characterization and expression analysis ofSaudi journal of biological sciences · 2021
    Article
  5. Mirror-Image 5S Ribonucleoprotein Complexes.Angewandte Chemie (International ed. in English) · 2020
    Article
  6. Frontiers in genetics · 2020
    Article
  7. Genome Wide Phosphoproteome Analysis ofFrontiers in microbiology · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Bacterial tyrosine kinases: evolution, biological function and structural insights.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

George Y SoungDepartment of Biochemistry & Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Jennifer L Miller
Hasan Koc
Emine C Koc
Pennsylvania State University · US

Funding

Structural Studies of Mammalian Mitochondrial RibosomesR01GM071034 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI KOC, EMINE C · 2005 to 2009
$1.3M
Profiling Biochemical Contents of Single MitochondriaR01EB005197 · NIBIB · UNIVERSITY OF WASHINGTON · PI CHIU, DANIEL T · 2006 to 2009
$1.3M
NIBIB NIH HHS EB005197-01NIBIB NIH HHS R01 EB005197NIGMS NIH HHS R01 GM071034NIGMS NIH HHS R01 GM071034-01A1
6 · The paper itself

Abstract

Phosphorylation of bacterial ribosomal proteins has been known for decades; however, there is still very limited information available on specific locations of the phosphorylation sites in ribosomal proteins and the role they might play in protein synthesis. In this study, we have mapped the specific phosphorylation sites in 24 Escherichia coli ribosomal proteins by tandem mass spectrometry. Detection of phosphorylation was achieved by either phosphorylation specific visualization techniques, ProQ staining, and antibodies for phospho-Ser, Thr, and Tyr; or by mass spectrometry equipped with a capability to detect addition and loss of the phosphate moiety. Enrichment by immobilized metal affinity and/or strong cation exchange chromatography was used to improve the success of detection of the low abundance phosphopeptides. We found the small subunit (30S) proteins S3, S4, S5, S7, S11, S12, S13, S18, and S21 and the large subunit (50S) proteins L1, L2, L3, L5, L6, L7/L12, L13, L14, L16, L18, L19, L21, L22, L28, and L31 to be phosphorylated at one or more residues. Potential roles for each specific site in ribosome function were deduced through careful evaluation of the given phosphorylation sites in 3D-crystal structure models of ribosomes and the previous mutational studies of E. coli ribosomal proteins.

Indexed as

Amino Acid SequenceBacterial ProteinsElectrophoresis, Gel, Two-DimensionalEscherichia coliImmunoblottingMass SpectrometryMetalsModels, MolecularMolecular ConformationMolecular Sequence DataPhosphatesPhosphopeptidesPhosphorylationProteomicsRibosomesSequence Homology, Amino AcidBacterial ProteinsMetalsPhosphatesPhosphopeptides

Identifiers

PMID19469554
PMCPMC2760691
OpenAlexW2053137607

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.