Evidence map›Paper›PMID 23720318›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Top-down proteomics reveals a unique protein S-thiolation switch in Salmonella Typhimurium in response to infection-like conditions.

Charles Ansong, Si Wu, Da Meng, Xiaowen Liu, Heather M Brewer, Brooke L Deatherage Kaiser, Ernesto S Nakayasu, John R Cort, Pavel Pevzner, Richard D Smith and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

116 citing papers in PubMed, 161 citations in OpenAlex.

  1. A Draft Map of E. coli Proteoforms.Analytical chemistry · 2026
    Article
  2. Proteoforms as the true units of physiological function.European journal of applied physiology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Microorganisms · 2024
    Article
  11. Article
  12. Article
  13. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  14. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

56 more citing papers are in PubMed but not listed here.

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

13 authors at 5 institutions in 1 country.

Charles AnsongBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA. Charles.ansong@pnnl.gov
Si Wu
Da Meng
Xiaowen Liu
Heather M Brewer
Brooke L Deatherage Kaiser
Ernesto S Nakayasu
John R Cort
Pavel Pevzner
Richard D Smith
Fred Heffron
Joshua N Adkins
Ljiljana Pasa-Tolic
Pacific Northwest National Laboratory · USEnvironmental Molecular Sciences Laboratory · USIndiana University School of MedicineOregon Health & Science University · USUniversity of California, San Diego · US

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI BELOV, MIKHAIL · 2003 to 2011
$25.1M
Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
Consortia for High-Throughput-Enabled Structural Biology Partnerships (U01)U01GM094623 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI ADKINS, JOSHUA N. · 2010 to 2014
$5.2M
SURFACE CHEMISTRY OF MYCOBACTERIAR01AI008401 · NIAID · NATIONAL JEWISH HEALTH · PI GOREN, MAYER B. · 1989 to 1989
–
SURFACE CHEMISTRY OF MYCOBACTERIAR22AI008401 · NIAID · NATIONAL JEWISH HEALTH · PI GOREN, MAYER B. · 1985 to 1989
–
NCRR NIH HHS 5P41RR018522-10NCRR NIH HHS P41 RR018522NIAID NIH HHS Y01 AI008401NIAID NIH HHS Y1-AI-8401NIGMS NIH HHS 8 P41 GM103493-10NIGMS NIH HHS GM094623NIGMS NIH HHS P41 GM103493NIGMS NIH HHS U01 GM094623
6 · The paper itself

Abstract

Characterization of the mature protein complement in cells is crucial for a better understanding of cellular processes on a systems-wide scale. Toward this end, we used single-dimension ultra-high-pressure liquid chromatography mass spectrometry to investigate the comprehensive "intact" proteome of the Gram-negative bacterial pathogen Salmonella Typhimurium. Top-down proteomics analysis revealed 563 unique proteins including 1,665 proteoforms generated by posttranslational modifications (PTMs), representing the largest microbial top-down dataset reported to date. We confirmed many previously recognized aspects of Salmonella biology and bacterial PTMs, and our analysis also revealed several additional biological insights. Of particular interest was differential utilization of the protein S-thiolation forms S-glutathionylation and S-cysteinylation in response to infection-like conditions versus basal conditions. This finding of a S-glutathionylation-to-S-cysteinylation switch in a condition-specific manner was corroborated by bottom-up proteomics data and further by changes in corresponding biosynthetic pathways under infection-like conditions and during actual infection of host cells. This differential utilization highlights underlying metabolic mechanisms that modulate changes in cellular signaling, and represents a report of S-cysteinylation in Gram-negative bacteria. Additionally, the functional relevance of these PTMs was supported by protein structure and gene deletion analyses. The demonstrated utility of our simple proteome-wide intact protein level measurement strategy for gaining biological insight should promote broader adoption and applications of top-down proteomics approaches.

Indexed as

Bacterial ProteinsChromatography, LiquidCysteineDimerizationHumansMass SpectrometryProtein Processing, Post-TranslationalProtein Structure, SecondaryProtein Structure, TertiaryProteomicsSalmonella InfectionsSalmonella typhimuriumSulfurBacterial ProteinsCysteineSulfur

Identifiers

PMID23720318
PMCPMC3690903
OpenAlexW2138455910

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.