Evidence map›Paper›PMID 20305001›Full record

ArticleEukaryotic cell2010

A Plasmodium falciparum transcriptional cyclin-dependent kinase-related kinase with a crucial role in parasite proliferation associates with histone deacetylase activity.

Jean Halbert, Lawrence Ayong, Leila Equinet, Karine Le Roch, Mary Hardy, Dean Goldring, Luc Reininger, Norman Waters, Debopam Chakrabarti, Christian Doerig

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Trial
  2. Integrative genomics ofbioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Chemical interrogation of the malaria kinome.Chembiochem : a European journal of chemical biology · 2014
    Article
  13. Cell division in apicomplexan parasites.Nature reviews. Microbiology · 2014
    Review
  14. Article
  15. An evolutionary perspective on the kinome of malaria parasites.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  16. Review
  17. Article
  18. Article
  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

10 authors at 5 institutions in 4 countries.

Jean HalbertINSERM-EPFL Joint Laboratory, Global Health Institute, Ecole Polytechnique Fédérale de Lausanne, GHI-SV-EPFL,Lausanne, Switzerland.
Lawrence Ayong
Leila Equinet
Karine Le Roch
Mary Hardy
Dean Goldring
Luc Reininger
Norman Waters
Debopam Chakrabarti
Christian Doerig
University of Central Florida · USÉcole Polytechnique Fédérale de Lausanne · CHWellcome Centre for Molecular Parasitology · GBUniversity of KwaZulu-Natal · ZAWellcome Trust · GB

Funding

Chemical Genetics of Plasmodium KinasesR01AI073795 · NIAID · UNIVERSITY OF CENTRAL FLORIDA · PI CHAKRABARTI, DEBOPAM · 2008 to 2010
$1.1M
NIAID NIH HHS AI 73795NIAID NIH HHS R01 AI073795
6 · The paper itself

Abstract

Cyclin-dependent protein kinases (CDKs) are key regulators of the eukaryotic cell cycle and of the eukaryotic transcription machinery. Here we report the characterization of Pfcrk-3 (Plasmodium falciparum CDK-related kinase 3; PlasmoDB identifier PFD0740w), an unusually large CDK-related protein whose kinase domain displays maximal homology to those CDKs which, in other eukaryotes, are involved in the control of transcription. The closest enzyme in Saccharomyces cerevisiae is BUR1 (bypass upstream activating sequence requirement 1), known to control gene expression through interaction with chromatin modification enzymes. Consistent with this, immunofluorescence data show that Pfcrk-3 colocalizes with histones. We show that recombinant Pfcrk-3 associates with histone H1 kinase activity in parasite extracts and that this association is detectable even if the catalytic domain of Pfcrk-3 is rendered inactive by site-directed mutagenesis, indicating that Pfcrk-3 is part of a complex that includes other protein kinases. Immunoprecipitates obtained from extracts of transgenic parasites expressing hemagglutinin (HA)-tagged Pfcrk-3 by using an anti-HA antibody displayed both protein kinase and histone deacetylase activities. Reverse genetics data show that the pfcrk-3 locus can be targeted only if the genetic modification does not cause a loss of function. Taken together, our data strongly suggest that Pfcrk-3 fulfils a crucial role in the intraerythrocytic development of P. falciparum, presumably through chromatin modification-dependent regulation of gene expression.

Indexed as

Cyclin-Dependent KinasesHistone DeacetylasesHumansModels, GeneticPhylogenyPlasmodium falciparumProtozoan ProteinsRNA, MessengerTransfectionCyclin-Dependent KinasesHistone DeacetylasesProtozoan ProteinsRNA, Messenger

Identifiers

PMID20305001
PMCPMC2901647
OpenAlexW2131733508

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.