Evidence map›Paper›PMID 25106450›Full record

ArticleJournal of proteome research2014

Correlation of phenotypic profiles using targeted proteomics identifies mycobacterial esx-1 substrates.

Matthew M Champion, Emily A Williams, Richard S Pinapati, Patricia A DiGiuseppe Champion

Abstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Tyloxapol inhibits ESX-1 secretion inJournal of bacteriology · 2026
    Article
  3. Article
  4. Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026
    Review
  5. Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Journal of bacteriology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Proteo-genetic analysis reveals clear hierarchy of ESX-1 secretion inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
  19. An In Vivo Model of SeparateInternational journal of molecular sciences · 2022
    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 1 institution in 1 country.

Matthew M ChampionDepartment of Chemistry and Biochemistry, ‡Department of Biological Sciences, §Eck Institute for Global Health, and ∥Center for Rare and Neglected Diseases, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Emily A Williams
Richard S Pinapati
Patricia A DiGiuseppe Champion
University of Notre Dame · US

Funding

Role of N-alpha acetylation in mycobacterial secretion and virulenceR01AI106872 · NIAID · UNIVERSITY OF NOTRE DAME · PI CHAMPION, PATRICIA A · 2013 to 2024
$4.2M
Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
Comprehensive Identification of the Genetic Requirements for ESX-1 SecretionR21AI092484 · NIAID · UNIVERSITY OF NOTRE DAME · PI CHAMPION, PATRICIA A · 2011 to 2012
$413k
NIAID NIH HHS R01 AI106872NIAID NIH HHS R21 AI092484NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

The Esx/WXG-100 (ESAT-6/Wss) exporters are multiprotein complexes that promote protein translocation across the cytoplasmic membrane in a diverse range of pathogenic and nonpathogenic bacterial species. The Esx-1 (ESAT-6 System-1) system mediates virulence factor translocation in mycobacterial pathogens, including the human pathogen Mycobacterium tuberculosis. Although several genes have been associated with Esx-1-mediated transport and virulence, the contribution of individual Esx-1 genes to export is largely undefined. A unique aspect of Esx-1 export is that several substrates require each other for export/stability. We exploited substrate "codependency" to identify Esx-1 substrates. We simultaneously quantified changes in the levels of 13 Esx-1 proteins from both secreted and cytosolic protein fractions generated from 16 Esx-1-deficient Mycobacterium marinum strains in a single experiment using MRM/SRM targeted mass spectrometry. This expansion of measurable Esx-1 proteins allowed us to define statistical rules for assigning novel substrates using phenotypic profiles of known Esx-1 substrates. Using this approach, we identified three additional Esx-1 substrates encoded by the esx-1 region. Our studies begin to address how disruption of specific genes affects several proteins in the Esx-1 complex. Overall, our findings illuminate relationships between Esx-1 proteins and create a framework for the identification of secreted substrates applicable to other protein exporters and pathways.

Indexed as

Antigens, BacterialBacterial ProteinsMass SpectrometryMycobacterium marinumPhenotypeProtein Interaction MappingProtein TransportProteomicsReproducibility of ResultsAntigens, BacterialBacterial ProteinsESAT-6 protein, Mycobacterium tuberculosisEsx-1EsxAMRM/SRMMycobacterium marinumRD1secretionsubstrate identificationtargeted proteomics

Identifiers

PMID25106450
PMCPMC4227905
OpenAlexW2333939089

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.