Evidence map›Paper›PMID 19307175›Full record

ArticleThe Journal of biological chemistry2009

Dissection of mechanisms involved in the regulation of Plasmodium falciparum calcium-dependent protein kinase 4.

Ravikant Ranjan, Anwar Ahmed, Samudrala Gourinath, Pushkar Sharma

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Dissecting The role ofEmerging microbes & infections · 2022
    Article
  2. Article
  3. Review
  4. Review
  5. Proteins with calmodulin-like domains: structures and functional roles.Cellular and molecular life sciences : CMLS · 2019
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Allosteric activation of apicomplexan calcium-dependent protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Review
  12. Article
  13. Article
  14. An evolutionary perspective on the kinome of malaria parasites.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  15. Novel insights into the regulation of malarial calcium-dependent protein kinase 1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    Article
  16. Article
  17. Article
  18. Article
  19. The coming-out of malaria gametocytes.Journal of biomedicine & biotechnology · 2010
    Review
  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.

Ravikant RanjanEukaryotic Gene Expression Laboratory, National Institute of Immunology, New Delhi, India.
Anwar Ahmed
Samudrala Gourinath
Pushkar Sharma

Funding

Signaling in Plasmodium falciparum: Role of PfPLC and PfPKBR01AI075459 · NIAID · NATIONAL INSTITUTE OF IMMUNOLOGY · PI SHARMA, PUSHKAR · 2008 to 2011
$222k
NIAID NIH HHS R01AI075459Wellcome Trust
6 · The paper itself

Abstract

Recent studies have demonstrated that calcium-dependent protein kinases (CDPKs) are used by calcium to regulate a variety of biological processes in the malaria parasite Plasmodium. CDPK4 has emerged as an important enzyme for parasite development, because its gene disruption in rodent parasite Plasmodium berghei causes major defects in sexual differentiation of the parasite ( Billker, O., Dechamps, S., Tewari, R., Wenig, G., Franke-Fayard, B., and Brinkmann, V. (2004) Cell 117, 503-514 ). Despite these findings, it is not very clear how PfCDPK4 or any other PfCDPK is regulated by calcium at the molecular level. We report the biochemical characterization and elucidation of molecular mechanisms involved in the regulation of PfCDPK4. PfCDPK4 was detected on gametocyte periphery, and its activity in the parasite was regulated by phospholipase C. Even though the Junction Domain (JD) of PfCDPK4 shares moderate sequence homology with that of the plant CDPKs, it plays a pivotal role in PfCDPK4 regulation as previously reported for some plant CDPKs. The regions of the J-domain involved in interaction with both the kinase domain and the calmodulin-like domain were mapped. We propose a model for PfCDPK regulation by calcium, which may also prove useful for design of inhibitors against PfCDPK4 and other members of the PfCDPK family.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBiocatalysisCalciumCalcium-Calmodulin-Dependent Protein KinasesCloning, MolecularEnzyme ActivationLife Cycle StagesModels, BiologicalMolecular Sequence DataMutant ProteinsParasitesPhosphorylationPhosphothreoninePlasmodium falciparumCalciumCalcium-Calmodulin-Dependent Protein KinasesMutant ProteinsPhosphothreonineProtein KinasesRecombinant ProteinsType C Phospholipases

Identifiers

PMID19307175
PMCPMC2685707

What OpenQuestion holds

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Registered trials

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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.