Evidence map›Paper›PMID 23462205›Full record

ArticleMolecular & cellular proteomics : MCP2013

A chemical proteomics approach to profiling the ATP-binding proteome of Mycobacterium tuberculosis.

Lisa M Wolfe, Usha Veeraraghavan, Susan Idicula-Thomas, Stephan Schürer, Krister Wennerberg, Robert Reynolds, Gurdyal S Besra, Karen M Dobos

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. DecipheringmSystems · 2024
    Article
  4. Review
  5. Septum site placement inMicrobiology (Reading, England) · 2023
    Article
  6. Target Identification in Anti-Tuberculosis Drug Discovery.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. A Global Survey of ATPase Activity inMolecular & cellular proteomics : MCP · 2018
    Article
  15. Article
  16. Review
  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

8 authors at 6 institutions in 4 countries.

Lisa M WolfeDepartment of Microbiology, Colorado State University, Fort Collins, Colorado 80523, USA.
Usha Veeraraghavan
Susan Idicula-Thomas
Stephan Schürer
Krister Wennerberg
Robert Reynolds
Gurdyal S Besra
Karen M Dobos
Colorado State University · USUniversity of Birmingham · GBIndian Council of Medical Research · INUniversity of Alabama at Birmingham · USUniversity of Helsinki · FIUniversity of Miami · US

Funding

NIAID NIH HHS HHSN266200400091C
6 · The paper itself

Abstract

Tuberculosis, caused by Mycobacterium tuberculosis, remains one of the leading causes of death worldwide despite extensive research, directly observed therapy using multidrug regimens, and the widespread use of a vaccine. The majority of patients harbor the bacterium in a state of metabolic dormancy. New drugs with novel modes of action are needed to target essential metabolic pathways in M. tuberculosis; ATP-competitive enzyme inhibitors are one such class. Previous screening efforts for ATP-competitive enzyme inhibitors identified several classes of lead compounds that demonstrated potent anti-mycobacterial efficacy as well as tolerable levels of toxicity in cell culture. In this report, a probe-based chemoproteomic approach was used to selectively profile the M. tuberculosis ATP-binding proteome in normally growing and hypoxic M. tuberculosis. From these studies, 122 ATP-binding proteins were identified in either metabolic state, and roughly 60% of these are reported to be essential for survival in vitro. These data are available through ProteomeXchange with identifier PXD000141. Protein families vital to the survival of the tubercle bacillus during hypoxia emerged from our studies. Specifically, along with members of the DosR regulon, several proteins involved in energy metabolism (Icl/Rv0468 and Mdh/Rv1240) and lipid biosynthesis (UmaA/Rv0469, DesA1/Rv0824c, and DesA2/Rv1094) were found to be differentially abundant in hypoxic versus normal growing cultures. These pathways represent a subset of proteins that may be relevant therapeutic targets for development of novel ATP-competitive antibiotics.

Indexed as

Adenosine TriphosphateAntitubercular AgentsBacterial ProteinsBinding, CompetitiveCarrier ProteinsCulture MediaDNA-Binding ProteinsGene Expression Regulation, BacterialIsocitrate LyaseMycobacterium tuberculosisOxygenPeptidesProtein BindingProtein Interaction MappingProtein IsoformsProtein KinasesAdenosine TriphosphateAntitubercular AgentsATP-binding protein, bacteriaBacterial ProteinsCarrier ProteinsCulture MediaDNA-Binding ProteinsDosR protein, Mycobacterium tuberculosisicl protein, MycobacteriumIsocitrate LyaseOxygenPeptidesProtein IsoformsProtein KinasesProteome

Identifiers

PMID23462205
PMCPMC3675820
OpenAlexW2112077186

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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.