Evidence map›Paper›PMID 20159970›Full record

ArticleThe Journal of biological chemistry2010

MYST family lysine acetyltransferase facilitates ataxia telangiectasia mutated (ATM) kinase-mediated DNA damage response in Toxoplasma gondii.

Nathalie Vonlaufen, Arunasalam Naguleswaran, Isabelle Coppens, William J Sullivan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Current and future therapies for small cell lung carcinoma.Journal of hematology & oncology · 2025
    Review
  2. Article
  3. Article
  4. Analysis of the role of acetylation inFrontiers in microbiology · 2024
    Article
  5. Article
  6. Emerging Therapeutic Targets AgainstFrontiers in cellular and infection microbiology · 2020
    Review
  7. Article
  8. Evaluation of ATM Kinase Inhibitor KU-55933 as Potential Anti-Frontiers in cellular and infection microbiology · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Histones: Controlling Tumor Signaling Circuitry.Journal of carcinogenesis & mutagenesis · 2013
    Article
  18. Toxoplasma histone acetylation remodelers as novel drug targets.Expert review of anti-infective therapy · 2012
    Review
  19. 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 3 institutions in 1 country.

Nathalie VonlaufenDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
Arunasalam Naguleswaran
Isabelle Coppens
William J Sullivan
Indiana University – Purdue University Indianapolis · USIndiana University School of MedicineJohns Hopkins University · US

Funding

MYST opportunities for Toxoplasma drug developmentR21AI083732 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI SULLIVAN, WILLIAM J · 2009 to 2010
$420k
NIAID NIH HHS R21 AI083732NIAID NIH HHS R21AI083732
6 · The paper itself

Abstract

The MYST family of lysine acetyltransferases (KATs) function in a wide variety of cellular operations, including gene regulation and the DNA damage response. Here we report the characterization of the second MYST family KAT in the protozoan parasite Toxoplasma gondii (TgMYST-B). Toxoplasma causes birth defects and is an opportunistic pathogen in the immunocompromised, the latter due to its ability to convert into a latent cyst (bradyzoite). We demonstrate that TgMYST-B can gain access to the parasite nucleus and acetylate histones. Overexpression of recombinant, tagged TgMYST-B reduces growth rate in vitro and confers protection from a DNA-alkylating agent. Expression of mutant TgMYST-B produced no growth defect and failed to protect against DNA damage. We demonstrate that cells overexpressing TgMYST-B have increased levels of ataxia telangiectasia mutated (ATM) kinase and phosphorylated H2AX and that TgMYST-B localizes to the ATM kinase gene. Pharmacological inhibitors of ATM kinase or KATs reverse the slow growth phenotype seen in parasites overexpressing TgMYST-B. These studies are the first to show that a MYST KAT contributes to ATM kinase gene expression, further illuminating the mechanism of how ATM kinase is up-regulated to respond to DNA damage.

Indexed as

DNA DamageAcetylationAmino Acid SequenceAnimalsAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsChromatinDNA-Binding ProteinsDNA RepairEpigenesis, GeneticHeLa CellsHistone AcetyltransferasesHistonesHumansMolecular Sequence DataPhylogenyAtaxia Telangiectasia Mutated ProteinsATM protein, humanCell Cycle ProteinsChromatinDNA-Binding ProteinsHistone AcetyltransferasesHistonesProtein Serine-Threonine KinasesRecombinant ProteinsTumor Suppressor Proteins

Identifiers

PMID20159970
PMCPMC2856992
OpenAlexW2064219281

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.