Evidence map›Paper›PMID 9864233›Full record

ArticleInfection and immunity1999

Identification of fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry.

D K Wong, B Y Lee, M A Horwitz, B W Gibson

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 129 citations in OpenAlex.

  1. eLife · 2026
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  6. Induced Heteroresistance in Carbapenem-ResistantInternational journal of molecular sciences · 2023
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  8. New Insights into the Methylation ofPathogens (Basel, Switzerland) · 2021
    Article
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  10. Pediatric Tuberculosis: The Impact of "Omics" on Diagnostics Development.International journal of molecular sciences · 2020
    Review
  11. Protein Composition ofFrontiers in microbiology · 2018
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

D K WongDepartment of Chemistry and Pharmaceutical Chemistry, University of California, San Francisco p594143-0446, USA.
B Y Lee
M A Horwitz
B W Gibson
University of California, Los Angeles · USUniversity of California, San Francisco · US

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SZOKA, FRANCIS C. · 1985 to 2011
$24.1M
PHARMACEUTICAL SCIENCES AND PHARMACOGENOMICST32GM007175 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AHITUV, NADAV, KROETZ, DEANNA L · 1985 to 2021
$7.1M
NCRR NIH HHS P41 RR001614NCRR NIH HHS RR01614NIGMS NIH HHS GM07175NIGMS NIH HHS T32 GM007175
6 · The paper itself

Abstract

Iron plays a critical role in the pathophysiology of Mycobacterium tuberculosis. To gain a better understanding of iron regulation by this organism, we have used two-dimensional (2-D) gel electrophoresis, mass spectrometry, and database searching to study protein expression in M. tuberculosis under conditions of high and low iron concentration. Proteins in cellular extracts from M. tuberculosis Erdman strain grown under low-iron (1 microM) and high-iron (70 microM) conditions were separated by 2-D polyacrylamide gel electrophoresis, which allowed high-resolution separation of several hundred proteins, as visualized by Coomassie staining. The expression of at least 15 proteins was induced, and the expression of at least 12 proteins was decreased under low-iron conditions. In-gel trypsin digestion was performed on these differentially expressed proteins, and the digestion mixtures were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry to determine the molecular masses of the resulting tryptic peptides. Partial sequence data on some of the peptides were obtained by using after source decay and/or collision-induced dissociation. The fragmentation data were used to search computerized peptide mass and protein sequence databases for known proteins. Ten iron-regulated proteins were identified, including Fur and aconitase proteins, both of which are known to be regulated by iron in other bacterial systems. Our study shows that, where large protein sequence databases are available from genomic studies, the combined use of 2-D gel electrophoresis, mass spectrometry, and database searching to analyze proteins expressed under defined environmental conditions is a powerful tool for identifying expressed proteins and their physiologic relevance.

Indexed as

Aconitate HydrataseAmino Acid SequenceAntigens, BacterialBacterial ProteinsCrystallinsCulture Media, ConditionedElectrophoresis, Gel, Two-DimensionalHeat-Shock ProteinsIronMolecular Sequence DataMycobacterium tuberculosisOxidoreductasesPeptide Elongation Factor TuPeptidylprolyl IsomerasePhosphoenolpyruvate Carboxykinase (ATP)Recombinant Fusion ProteinsAconitate HydrataseAntigens, BacterialBacterial ProteinsCrystallinsCulture Media, Conditionedferric uptake regulating proteins, bacterialHeat-Shock ProteinsIronLSR2 protein, Mycobacterium lepraeOxidoreductasesPeptide Elongation Factor TuPeptidylprolyl IsomerasePhosphoenolpyruvate Carboxykinase (ATP)Recombinant Fusion ProteinsRepressor Proteins

Identifiers

PMID9864233
PMCPMC96314
OpenAlexW1903814430

What OpenQuestion holds

Textmetadata
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.