Evidence map›Paper›PMID 30773146›Full record

ReviewParasitology2019

Protein

Giulia Bandini, Andreia Albuquerque-Wendt, Jan Hegermann, John Samuelson, Françoise H Routier

Open access · hybridAbstract readReview
In one paragraph

Review in Parasitology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Role ofJournal of personalized medicine · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. ProteinMolecules (Basel, Switzerland) · 2021
    Review
  17. Review
  18. Review
  19. Article
  20. The Journal of biological chemistry · 2020
    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

5 authors at 2 institutions in 2 countries.

Giulia BandiniDepartment of Molecular and Cell Biology, Boston University, Goldman School of Dental Medicine, 72 East Concord Street, Boston, MA 02118, USA.ORCID 0000-0002-8885-3643
Andreia Albuquerque-WendtDepartment of Clinical Biochemistry OE4340, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.
Jan HegermannHannover Medical School, Electron Microscopy Facility OE8840, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.
John SamuelsonDepartment of Molecular and Cell Biology, Boston University, Goldman School of Dental Medicine, 72 East Concord Street, Boston, MA 02118, USA.
Françoise H RoutierDepartment of Clinical Biochemistry OE4340, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.ORCID 0000-0002-7163-0590
Medizinische Hochschule Hannover · DEBoston University · US

Funding

Structure and Development of Oocyst and Sporocyst WallsR01AI110638 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SAMUELSON, JOHN C. · 2015 to 2019
$1.8M
NIAID NIH HHS R01 AI110638
6 · The paper itself

Abstract

Apicomplexan parasites are amongst the most prevalent and morbidity-causing pathogens worldwide. They are responsible for severe diseases in humans and livestock and are thus of great public health and economic importance. Until the sequencing of apicomplexan genomes at the beginning of this century, the occurrence of N- and O-glycoproteins in these parasites was much debated. The synthesis of rudimentary and divergent N-glycans due to lineage-specific gene loss is now well established and has been recently reviewed. Here, we will focus on recent studies that clarified classical O-glycosylation pathways and described new nucleocytosolic glycosylations in Toxoplasma gondii, the causative agents of toxoplasmosis. We will also review the glycosylation of proteins containing thrombospondin type 1 repeats by O-fucosylation and C-mannosylation, newly discovered in Toxoplasma and the malaria parasite Plasmodium falciparum. The functional significance of these post-translational modifications has only started to emerge, but the evidence points towards roles for these protein glycosylation pathways in tissue cyst wall rigidity and persistence in the host, oxygen sensing, and stability of proteins involved in host invasion.

Indexed as

Metabolic Networks and PathwaysGlycoproteinsGlycosylationHost-Parasite InteractionsHumansMucinsPlasmodium falciparumProtein Processing, Post-TranslationalProtozoan ProteinsThrombospondin 1ToxoplasmaGlycoproteinsMucinsProtozoan ProteinsThrombospondin 1ApicomplexaC-mannosylationMucin type O-glycosylationnucleocytosolic O-glycosylationO-fucosylationPlasmodium falciparumthrombospondin type 1 repeatToxoplasma gondii

Identifiers

PMID30773146
PMCPMC6939170
OpenAlexW2916469090

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.