Evidence map›Paper›PMID 26002073›Full record

ReviewTrends in pharmacological sciences2015

Designing selective inhibitors for calcium-dependent protein kinases in apicomplexans.

Raymond Hui, Majida El Bakkouri, L David Sibley

Abstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. In vitro evaluation of new 4-thiazolidinones on invasion and growth of Toxoplasma gondii.International journal for parasitology. Drugs and drug resistance · 2021
    Article
  7. ACS infectious diseases · 2021
    Review
  8. Calcium in the Backstage of Malaria Parasite Biology.Frontiers in cellular and infection microbiology · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Bumped kinase inhibitor 1369 is effective against Cystoisospora suis in vivo and in vitro.International journal for parasitology. Drugs and drug resistance · 2019
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Insights into the red algae and eukaryotic evolution from the genome ofProceedings of the National Academy of Sciences of the United States of America · 2017
    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

3 authors.

Raymond HuiStructural Genomics Consortium, University of Toronto, MaRS South Tower, 101 College St, Toronto, ON, M5G 1L7, Canada; Toronto General Hospital Research Institute, 610 University Avenue, Toronto, ON, M5G 2M9, Canada.
Majida El BakkouriStructural Genomics Consortium, University of Toronto, MaRS South Tower, 101 College St, Toronto, ON, M5G 1L7, Canada.
L David SibleyDepartment of Molecular Microbiology, 660 S. Euclid Ave., Washington University School of Medicine, St Louis, MO 63130, USA. Electronic address: sibley@wustl.edu.

Funding

PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
DESIGNING SELECTIVE INHIBITORS OF CALCIUM-DEPENDENT KINASES IN PARASITESR01AI094098 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2012 to 2015
$1.6M
NIAID NIH HHS AI094098NIAID NIH HHS R01 AI034036NIAID NIH HHS R01 AI094098
6 · The paper itself

Abstract

Apicomplexan parasites cause some of the most severe human diseases, including malaria (caused by Plasmodium), toxoplasmosis, and cryptosporidiosis. Treatments are limited by the lack of effective drugs and development of resistance to available agents. By exploiting novel features of protein kinases in these parasites, it may be possible to develop new treatments. We summarize here recent advances in identifying small molecule inhibitors against a novel family of plant-like, calcium-dependent kinases that are uniquely expanded in apicomplexan parasites. Analysis of the 3D structure, activation mechanism, and sensitivity to small molecules had identified several attractive chemical scaffolds that are potent and selective inhibitors of these parasite kinases. Further optimization of these leads may yield promising new drugs for treatment of these parasitic infections.

Indexed as

Drug DesignApicomplexaCalcium-Binding ProteinsHumansModels, MolecularMolecular StructurePhylogenyProtein Kinase InhibitorsProtein Serine-Threonine KinasesProtozoan InfectionsProtozoan ProteinsStructure-Activity RelationshipCalcium-Binding ProteinsProtein Kinase InhibitorsProtein Serine-Threonine KinasesProtozoan ProteinsATP-binding pocketchemotherapygatekeeperorthogonal inhibitorsparasitesserine-threonine protein kinases

Identifiers

PMID26002073
PMCPMC4485940

What OpenQuestion holds

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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.