Evidence map›Paper›PMID 17012537›Full record

ArticleEukaryotic cell2006

The Tetrahymena thermophila phagosome proteome.

Mary Ellen Jacobs, Leroi V DeSouza, Haresha Samaranayake, Ronald E Pearlman, K W Michael Siu, Lawrence A Klobutcher

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2006. 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
4.9field-weighted citation impact, top 5% 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, 76 citations in OpenAlex.

  1. Review
  2. Article
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  5. Microbial warfare in the wild-the impact of protists on the evolution and virulence of bacterial pathogens.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    Review
  6. Article
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  9. Article
  10. Article
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  12. Review
  13. Identification ofFrontiers in cellular and infection microbiology · 2016
    Article
  14. Article
  15. Long-term exposure of bacterial and protozoan communities to TiOScience and technology of advanced materials · 2015
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

6 authors at 2 institutions in 2 countries.

Mary Ellen JacobsDepartment of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032, USA.
Leroi V DeSouza
Haresha Samaranayake
Ronald E Pearlman
K W Michael Siu
Lawrence A Klobutcher
UConn Health · USYork University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vertebrates, phagocytosis occurs mainly in specialized cells of the immune system and serves as a primary defense against invading pathogens, but it also plays a role in clearing apoptotic cells and in tissue remodeling during development. In contrast, unicellular eukaryotes, such as the ciliate Tetrahymena thermophila, employ phagocytosis to ingest and degrade other microorganisms to meet their nutritional needs. To learn more about the protein components of the multistep process of phagocytosis, we carried out an analysis of the Tetrahymena phagosome proteome. Tetrahymena cells were fed polystyrene beads, which allowed for the efficient purification of phagosomes. The protein composition of purified phagosomes was then analyzed by multidimensional separation coupled with tandem mass spectrometry. A total of 453 peptides were identified that resulted in the identification of 73 putative phagosome proteins. Twenty-eight of the proteins have been implicated in phagocytosis in other organisms, indicating that key aspects of phagocytosis were conserved during evolution. Other identified proteins have not previously been associated with phagocytosis, including some of unknown function. Live-cell confocal fluorescence imaging of Tetrahymena strains expressing green fluorescent protein-tagged versions of four of the identified phagosome proteins provided evidence that at least three of the proteins (including two with unknown functions) are associated with phagosomes, indicating that the bulk of the proteins identified in the analyses are indeed phagosome associated.

Indexed as

PhagocytosisAnimalsBase SequenceDNA, ProtozoanGenes, ProtozoanPhagosomesProteomeProtozoan ProteinsRecombinant Fusion ProteinsTandem Mass SpectrometryTetrahymena thermophilaDNA, ProtozoanProteomeProtozoan ProteinsRecombinant Fusion Proteins

Identifiers

PMID17012537
PMCPMC1694822
OpenAlexW2135052838

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.