Evidence map›Paper›PMID 18420584›Full record

ArticleThe Journal of biological chemistry2008

Translation regulation by eukaryotic initiation factor-2 kinases in the development of latent cysts in Toxoplasma gondii.

Jana Narasimhan, Bradley R Joyce, Arunasalam Naguleswaran, Aaron T Smith, Meredith R Livingston, Stacy E Dixon, Isabelle Coppens, Ronald C Wek, William J Sullivan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
3.6field-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

77 citing papers in PubMed, 123 citations in OpenAlex.

  1. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. mSphere · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. The determinants regulatingFrontiers in microbiology · 2022
    Review
  17. Review
  18. Review
  19. Article
  20. Article

17 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

9 authors at 3 institutions in 1 country.

Jana NarasimhanDepartment of Pharmacology and Toxicology and Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
Bradley R Joyce
Arunasalam Naguleswaran
Aaron T Smith
Meredith R Livingston
Stacy E Dixon
Isabelle Coppens
Ronald C Wek
William J Sullivan
Indiana University – Purdue University Indianapolis · USIndiana University School of MedicineJohns Hopkins University · US

Funding

Metabolic stress responses andeIF2 kinase GCN2R01GM049164 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WEK, RONALD C · 1998 to 2019
$6.3M
Translational Control by elF2 Kinase during ER StressR01GM064350 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WEK, RONALD C · 2001 to 2008
$2.0M
NIGMS NIH HHS R01 GM049164NIGMS NIH HHS R01 GM064350NIGMS NIH HHS R01GM49164NIGMS NIH HHS R01GM64350
6 · The paper itself

Abstract

A key problem in the treatment of numerous pathogenic eukaryotes centers on their development into latent forms during stress. For example, the opportunistic protist Toxoplasma gondii converts to latent cysts (bradyzoites) responsible for recrudescence of disease. We report that Toxoplasma eukaryotic initiation factor-2alpha (TgIF2alpha) is phosphorylated during stress and establish that protozoan parasites utilize translation control to modulate gene expression during development. Importantly, TgIF2alpha remains phosphorylated in bradyzoites, explaining how these cells maintain their quiescent state. Furthermore, we have characterized novel eIF2 kinases; one in the endoplasmic reticulum and a likely regulator of the unfolded protein response (TgIF2K-A) and another that is a probable responder to cytoplasmic stresses (TgIF2K-B). Significantly, our data suggest that 1) the regulation of protein translation through eIF2 kinases is associated with development, 2) eIF2alpha phosphorylation is employed by cells to maintain a latent state, and 3) endoplasmic reticulum and cytoplasmic stress responses evolved in eukaryotic cells before the early diverging Apicomplexa. Given its importance to pathogenesis, eIF2 kinase-mediated stress responses may provide opportunities for novel therapeutics.

Indexed as

Gene Expression Regulation, EnzymologicProtein BiosynthesisAnimalsCentrifugation, Density GradientCloning, MolecularCytoplasmeIF-2 KinaseEndoplasmic ReticulumEukaryotic Initiation Factor-2Microscopy, FluorescenceModels, BiologicalOxidative StressPhosphorylationToxoplasmaTunicamycineIF-2 KinaseEukaryotic Initiation Factor-2Tunicamycin

Identifiers

PMID18420584
PMCPMC2423249
OpenAlexW2074708187

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.