Evidence map›Paper›PMID 25764948›Full record

ReviewJournal of structural biology2015

The apicomplexan glideosome and adhesins - Structures and function.

Lauren E Boucher, Jürgen Bosch

Open access · greenAbstract readReview
In one paragraph

Review in Journal of structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
8.6field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
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  6. Review
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  8. Elevated NADNature communications · 2025
    Article
  9. Article
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  11. Review
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  13. Review
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  15. Article
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  17. Unravelling the sexual developmental biology ofFrontiers in cellular and infection microbiology · 2023
    Article
  18. Article
  19. Article
  20. Comparison of high throughput RNA sequences betweenFrontiers in cellular and infection microbiology · 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.

Lauren E BoucherDepartment of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, 615 N Wolfe St, Baltimore, MD 21205, USA; Johns Hopkins Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, 615 N Wolfe St, Baltimore, MD 21205, USA. Electronic address: lboucher@jhu.edu.
Jürgen BoschDepartment of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, 615 N Wolfe St, Baltimore, MD 21205, USA; Johns Hopkins Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, 615 N Wolfe St, Baltimore, MD 21205, USA. Electronic address: jbosch@jhu.edu.
Johns Hopkins University · US

Funding

The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
NIGMS NIH HHS T32 GM080189NIGMS NIH HHS T32GM080189
6 · The paper itself

Abstract

The apicomplexan family of pathogens, which includes Plasmodium spp. and Toxoplasma gondii, are primarily obligate intracellular parasites and invade multiple cell types. These parasites express extracellular membrane protein receptors, adhesins, to form specific pathogen-host cell interaction complexes. Various adhesins are used to invade a variety of cell types. The receptors are linked to an actomyosin motor, which is part of a complex comprised of many proteins known as the invasion machinery or glideosome. To date, reviews on invasion have focused primarily on the molecular pathways and signals of invasion, with little or no structural information presented. Over 75 structures of parasite receptors and glideosome proteins have been deposited with the Protein Data Bank. These structures include adhesins, motor proteins, bridging proteins, inner membrane complex and cytoskeletal proteins, as well as co-crystal structures with peptides and antibodies. These structures provide information regarding key interactions necessary for target receptor engagement, machinery complex formation, how force is transmitted, and the basis of inhibitory antibodies. Additionally, these structures can provide starting points for the development of antibodies and inhibitory molecules targeting protein-protein interactions, with the aim to inhibit invasion. This review provides an overview of the parasite adhesin protein families, the glideosome components, glideosome architecture, and discuss recent work regarding alternative models.

Indexed as

Models, MolecularActomyosinApicomplexaDatabases, ProteinHost-Pathogen InteractionsMembrane ProteinsMultiprotein ComplexesProtein BindingProtein ConformationProtein Interaction MappingProtein Structure, TertiaryActomyosinMembrane ProteinsMultiprotein ComplexesAdhesinsApicomplexaCryptosporidiumGlideosomeInvasion machineryMalariaPlasmodiumToxoplasma

Identifiers

PMID25764948
PMCPMC4417069
OpenAlexW2091802170

What OpenQuestion holds

Textmetadata
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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.