Evidence map›Paper›PMID 24136294›Full record

ArticleMolecular & cellular proteomics : MCP2014

The cell surface proteome of Entamoeba histolytica.

Laura Biller, Jenny Matthiesen, Vera Kühne, Hannelore Lotter, Ghassan Handal, Tomoyoshi Nozaki, Yumiko Saito-Nakano, Michael Schümann, Thomas Roeder, Egbert Tannich and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.6field-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

45 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  8. Article
  9. Review
  10. Review
  11. Article
  12. Membranes · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Taxon-Specific Proteins of the PathogenicFrontiers in cellular and infection microbiology · 2021
    Review
  18. Article
  19. Review
  20. Review
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

12 authors at 4 institutions in 2 countries.

Laura BillerBernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany;
Jenny Matthiesen
Vera Kühne
Hannelore Lotter
Ghassan Handal
Tomoyoshi Nozaki
Yumiko Saito-Nakano
Michael Schümann
Thomas Roeder
Egbert Tannich
Eberhard Krause
Iris Bruchhaus
Bernhard Nocht Institute for Tropical Medicine · DELeibniz Association · DENational Institute of Infectious Diseases · JPKiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Surface molecules are of major importance for host-parasite interactions. During Entamoeba histolytica infections, these interactions are predicted to be of prime importance for tissue invasion, induction of colitis and liver abscess formation. To date, however, little is known about the molecules involved in these processes, with only about 20 proteins or protein families found exposed on the E. histolytica surface. We have therefore analyzed the complete surface proteome of E. histolytica. Using cell surface biotinylation and mass spectrometry, 693 putative surface-associated proteins were identified. In silico analysis predicted that ∼26% of these proteins are membrane-associated, as they contain transmembrane domains and/or signal sequences, as well as sites of palmitoylation, myristoylation, or prenylation. An additional 25% of the identified proteins likely represent nonclassical secreted proteins. Surprisingly, no membrane-association sites could be predicted for the remaining 49% of the identified proteins. To verify surface localization, 23 proteins were randomly selected and analyzed by immunofluorescence microscopy. Of these 23 proteins, 20 (87%) showed definite surface localization. These findings indicate that a far greater number of E. histolytica proteins than previously supposed are surface-associated, a phenomenon that may be based on the high membrane turnover of E. histolytica.

Indexed as

Mass SpectrometryColitisEntamoeba histolyticaHost-Parasite InteractionsHumansLipoylationMembrane ProteinsPrenylationProteomeMembrane ProteinsProteome

Identifiers

PMID24136294
PMCPMC3879609
OpenAlexW2125791516

What OpenQuestion holds

Textmetadata
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.