Evidence map›Paper›PMID 18694966›Full record

ArticleInfection and immunity2008

Role of protein kinase A in Trypanosoma cruzi.

Yi Bao, Louis M Weiss, Vicki L Braunstein, Huan Huang

Abstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Pathogens (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Iron Uptake ControlsAntioxidants (Basel, Switzerland) · 2023
    Article
  5. The ElusivePathogens (Basel, Switzerland) · 2023
    Review
  6. Cells · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Yi BaoDepartment of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Louis M Weiss
Vicki L Braunstein
Huan Huang
Albert Einstein College of Medicine · US

Funding

T. cruzi: pathogenesis modulation by eicosanoidsR01AI076248 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI TANOWITZ, HERBERT BERNARD · 2008 to 2012
$2.3M
Differentiation in T.cruzi:an emerging AIDS pathogenR01AI058893 · NIAID · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI HUANG, HUAN · 2005 to 2009
$1.8M
NIAID NIH HHS AI05739NIAID NIH HHS AI058893NIAID NIH HHS AI076248NIAID NIH HHS R01 AI058893NIAID NIH HHS R01 AI076248
6 · The paper itself

Abstract

Protein kinase A (PKA) is an important mediator of many signal transduction pathways that occur in eukaryotic cells, and it has been implicated as a regulator of stage differentiation in Trypanosoma cruzi. To evaluate the importance of the PKA catalytic subunit of T. cruzi (TcPKAc), a gene encoding a PKA inhibitor (PKI) containing a specific PKA pseudosubstrate, R-R-N-A, was subcloned into a pTREX vector and introduced into epimastigotes by electroporation. Expression of PKI has a lethal effect in this parasite. Similarly, a pharmacological inhibitor, H89, killed epimastigotes at a concentration of 10 muM. To understand the biology of PKA, identification of the particular substrates of this enzyme is essential. Using a yeast two-hybrid system, 38 candidates interacting with TcPKAc were identified. Eighteen of these were hypothetical proteins with unknown functions, while the others had putative or known functions. The entire open reading frames of eight genes presumably important in regulating T. cruzi growth, adaptation, and differentiation, including a type III PI3 kinase (Vps34), a putative PI3 kinase, a putative mitogen-activated extracellular signal-regulated kinase, a cyclic AMP (cAMP)-specific phosphodiesterase (PDEC2), a hexokinase, a putative ATPase, a DNA excision repair protein, and an aquaporin were confirmed to interact with TcPKAc in the yeast Saccharomyces cerevisiae under the highest stringency selection conditions, and PKA phosphorylated the recombinant proteins of these genes. Taken together, these findings demonstrate the importance of cAMP-PKA signaling in this organism.

Indexed as

AnimalsCell SurvivalCyclic AMP-Dependent Protein KinasesPhosphorylationProtein BindingProtein Kinase InhibitorsProtozoan ProteinsTrypanosoma cruziTwo-Hybrid System TechniquesCyclic AMP-Dependent Protein KinasesProtein Kinase InhibitorsProtozoan Proteins

Identifiers

PMID18694966
PMCPMC2546855
OpenAlexW2032141731

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.