Evidence map›Paper›PMID 25945702›Full record

ReviewActa crystallographica. Section F, Structural biology communications2015

Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?

Esa Pekka Kumpula, Inari Kursula

Open access · hybridAbstract readReview
In one paragraph

Review in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.3field-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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Recombinant actin-depolymerizing factor of the apicomplexanFrontiers in cellular and infection microbiology · 2022
    Article
  5. Article
  6. Unusual dynamics of the divergent malaria parasiteProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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 2 institutions in 3 countries.

Esa Pekka KumpulaFaculty of Biochemistry and Molecular Medicine, University of Oulu, PO Box 3000, 90014 Oulu, Finland.
Inari KursulaFaculty of Biochemistry and Molecular Medicine, University of Oulu, PO Box 3000, 90014 Oulu, Finland.
Helmholtz Centre for Infection Research · DEUniversity of Oulu · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apicomplexan parasites are the causative agents of notorious human and animal diseases that give rise to considerable human suffering and economic losses worldwide. The most prominent parasites of this phylum are the malaria-causing Plasmodium species, which are widespread in tropical and subtropical regions, and Toxoplasma gondii, which infects one third of the world's population. These parasites share a common form of gliding motility which relies on an actin-myosin motor. The components of this motor and the actin-regulatory proteins in Apicomplexa have unique features compared with all other eukaryotes. This, together with the crucial roles of these proteins, makes them attractive targets for structure-based drug design. In recent years, several structures of glideosome components, in particular of actins and actin regulators from apicomplexan parasites, have been determined, which will hopefully soon allow the creation of a complete molecular picture of the parasite actin-myosin motor and its regulatory machinery. Here, current knowledge of the function of this motor is reviewed from a structural perspective.

Indexed as

ComprehensionActinsAnimalsApicomplexaDrug Delivery SystemsHumansMalariaProtein Structure, SecondaryProtein Structure, TertiaryToxoplasmaActinsactin polymerizationcytoskeletondrug designgliding motilitymalariaparasitologyregulation

Identifiers

PMID25945702
PMCPMC4427158
OpenAlexW2063663939

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.