Evidence map›Paper›PMID 18690695›Full record

ArticleAnalytical chemistry2008

Protein dynamics in iron-starved Mycobacterium tuberculosis revealed by turnover and abundance measurement using hybrid-linear ion trap-Fourier transform mass spectrometry.

Prahlad K Rao, G Marcela Rodriguez, Issar Smith, Qingbo Li

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 10% 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, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Metalloregulation of Gram-positive pathogen physiology.Current opinion in microbiology · 2012
    Review
  9. Latent tuberculosis: what the host "sees"?Immunologic research · 2011
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Acid stress response of a mycobacterial proteome: insight from a gene ontology analysis.International journal of clinical and experimental medicine · 2009
    Article
  15. A systems biology approach to study the phagosomal proteome modulated by mycobacterial infections.International journal of clinical and experimental medicine · 2009
    Article
  16. Protein turnover in mycobacterial proteomics.Molecules (Basel, Switzerland) · 2009
    Review
  17. Article
  18. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Prahlad K RaoCenter for Pharmaceutical Biotechnology, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois 60607, USA.
G Marcela Rodriguez
Issar Smith
Qingbo Li
University of Illinois Chicago · US

Funding

M TUBERCULOSIS SURVIVAL AND GROWTH IN VIVOR01AI044856 · NIAID · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI RODRIGUEZ, GLORIA MARCELA, SMITH, ISSAR · 1999 to 2014
$6.8M
NIAID NIH HHS R01 AI044856
6 · The paper itself

Abstract

To study the proteome response of Mycobacterium tuberculosis H37Rv to a change in iron level, iron-starved late-log-phase cells were diluted in fresh low- and high-iron media containing [ (15)N]-labeled asparagine as the sole nitrogen source for labeling the proteins synthesized upon dilution. We determined the relative protein abundance and protein turnover in M. tuberculosis H37Rv under these two conditions. For measurements, we used a high-resolution hybrid-linear ion trap-Fourier transform mass spectrometer coupled with nanoliquid chromatography separation. While relative protein abundance analysis shows that only 5 proteins were upregulated by high iron, 24 proteins had elevated protein turnover for the cells in the high-iron medium. This suggests that protein turnover is a sensitive parameter to assess the proteome dynamics. Cluster analysis was used to explore the interconnection of protein abundance and turnover, revealing coordination of the cellular processes of protein synthesis, degradation, and secretion that determine the abundance and allocation of a protein in the cytosol and the extracellular matrix of the cells. Further potential utility of the approach is discussed.

Indexed as

Fourier AnalysisIron DeficienciesAsparagineBacterial ProteinsCluster AnalysisCytosolExtracellular MatrixIronMass SpectrometryMycobacterium tuberculosisProteomeStaining and LabelingAsparagineBacterial ProteinsIronProteome

Identifiers

PMID18690695
PMCPMC2768315
OpenAlexW2081298443

What OpenQuestion holds

Textmetadata
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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.