Evidence map›Paper›PMID 19579231›Full record

ArticleProteomics2009

Phosphoproteomic analysis of the human pathogen Trypanosoma cruzi at the epimastigote stage.

Ernesto S Nakayasu, Matthew R Gaynor, Tiago J P Sobreira, Jeremy A Ross, Igor C Almeida

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. An Overview ofPathogens (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Cells · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

5 authors at 2 institutions in 2 countries.

Ernesto S NakayasuThe Border Biomedical Research Center, Department of Biological Sciences, University of Texas at El Paso, El Paso, TX 79968, USA.
Matthew R Gaynor
Tiago J P Sobreira
Jeremy A Ross
Igor C Almeida
The University of Texas at El Paso · USUniversidade de São Paulo · BR

Funding

TOXICOLOGY PROJECTG12RR008124 · NCRR · UNIVERSITY OF TEXAS EL PASO · PI WALSH, ELIZABETH J · 1992 to 2011
$20.8M
UTEP SCORE InstrumentationS06GM008012 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI GARZA, KRISTINE M · 1989 to 2010
$15.8M
NCRR NIH HHS 5G12RR008124NCRR NIH HHS G12 RR008124NIGMS NIH HHS 5S06GM08012-37NIGMS NIH HHS S06 GM008012
6 · The paper itself

Abstract

Trypanosoma cruzi is the etiologic agent of Chagas disease, which affects millions of people in Latin America and has become a public health concern in the United States and areas of Europe. The possibility that kinase inhibitors represent novel anti-parasitic agents is currently being explored. However, fundamental understanding of the cell-signaling networks requires the detailed analysis of the involved phosphorylated proteins. Here, we have performed a comprehensive MS-based phosphorylation mapping of phosphoproteins from T. cruzi epimastigote forms. Our LC-MS/MS, dual-stage fragmentation, and multistage activation analysis has identified 237 phosphopeptides from 119 distinct proteins. Furthermore, 220 phosphorylation sites were unambiguously mapped: 148 on serine, 57 on threonine, and 8 on tyrosine. In addition, immunoprecipitation and Western blotting analysis confirmed the presence of at least seven tyrosine-phosphorylated proteins in T. cruzi. The identified phosphoproteins were subjected to Gene Ontology, InterPro, and BLAST analysis, and categorized based on their role in cell structure, motility, transportation, metabolism, pathogenesis, DNA/RNA/protein turnover, and signaling. Taken together, our phosphoproteomic data provide new insights into the molecular mechanisms governed by protein kinases and phosphatases in T. cruzi. We discuss the potential roles of the identified phosphoproteins in parasite physiology and drug development.

Indexed as

Amino Acid MotifsAnimalsCytoskeletonDNA, ProtozoanFlagellaHumansPhosphoproteinsPhosphoserineProtein TransportProteomicsProtozoan ProteinsRNA, ProtozoanSignal TransductionTrypanosoma cruziDNA, ProtozoanPhosphoproteinsPhosphoserineProtozoan ProteinsRNA, Protozoan

Identifiers

PMID19579231
PMCPMC2752742
OpenAlexW1995627884

What OpenQuestion holds

Textmetadata
LicenceTDM
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.