Evidence map›Paper›PMID 28556455›Full record

ReviewMolecular microbiology2017

The serine/threonine phosphatases of apicomplexan parasites.

Chunlin Yang, Gustavo Arrizabalaga

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Functional redundancy of three mitochondrial MgJournal of Zhejiang University. Science. B · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. SPARK regulates AGC kinases central to thebioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. mSphere · 2022
    Article
  18. Article
  19. Article
  20. Open biology · 2022
    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

2 authors at 1 institution in 1 country.

Chunlin YangDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA.
Gustavo ArrizabalagaDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN, USA.ORCID http://orcid.org/0000-0002-4445-0375
Indiana University School of Medicine

Funding

Dissecting the calcium dependent phosphorylation network of Toxoplasma gondiiR01AI123457 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A, TREECK, MORITZ · 2016 to 2020
$2.7M
Calcium signaling in the parasitophorous vacuole of Toxoplasma gondiiR21AI119516 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A · 2015 to 2016
$460k
Dissecting the role of Toxoplasma CDPK3 in parasite propagation and virulenceR21AI108393 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A · 2015 to 2016
$429k
Characterization of calcium signaling proteins in Toxoplasma gondiiR03AI101624 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI ARRIZABALAGA, GUSTAVO A · 2012 to 2013
$156k
NIAID NIH HHS R01 AI123457NIAID NIH HHS R03 AI101624NIAID NIH HHS R21 AI108393NIAID NIH HHS R21 AI119516
6 · The paper itself

Abstract

The balance between phosphorylation and de-phosphorylation, which is delicately regulated by protein kinases and phosphatases, is critical for nearly all biological processes. The Apicomplexa are a large phylum which contains various parasitic protists, including human pathogens, such as Plasmodium, Toxoplasma, Cryptosporidium and Babesia species. The diverse life cycles of these parasites are highly complex and, not surprisingly, many of their key steps are exquisitely regulated by phosphorylation. Interestingly, many of the kinases and phosphatases, as well as the substrates involved in these events are unique to the parasites and therefore phosphorylation constitutes a viable target for antiparasitic intervention. Most progress on this realm has come from studies in Toxoplasma and Plasmodium of their respective kinomes and phosphoproteomes. Nonetheless, given their likely importance, phosphatases have recently become the focus of research within the apicomplexan parasites. In this review, we concentrate on serine/threonine phosphatases in apicomplexan parasites, with the focus on comprehensively identifying and naming protein phosphatases in available apicomplexan genomes, and summarizing the progress of their functional analyses in recent years.

Indexed as

AnimalsApicomplexaConserved SequenceGenomeHumansParasitesPhosphoprotein PhosphatasesPhosphorylationPhosphotransferasesPhylogenyPlasmodiumToxoplasmaPhosphoprotein PhosphatasesPhosphotransferases

Identifiers

PMID28556455
PMCPMC5787372
OpenAlexW2657434786

What OpenQuestion holds

Textmetadata
LicenceTDM
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.