Evidence map›Paper›PMID 23509141›Full record

ArticleInfection and immunity2013

Cysteine protease-binding protein family 6 mediates the trafficking of amylases to phagosomes in the enteric protozoan Entamoeba histolytica.

Atsushi Furukawa, Kumiko Nakada-Tsukui, Tomoyoshi Nozaki

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  8. The American journal of tropical medicine and hygiene · 2018
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. The cell surface proteome of Entamoeba histolytica.Molecular & cellular proteomics : MCP · 2014
    Article
  15. Article
  16. Regulation of virulence of Entamoeba histolytica.Annual review of microbiology · 2014
    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

3 authors at 2 institutions in 1 country.

Atsushi FurukawaDepartment of Parasitology, National Institute of Infectious Diseases, Toyama, Tokyo, Japan.
Kumiko Nakada-Tsukui
Tomoyoshi Nozaki
National Institute of Infectious Diseases · JPGunma University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phagocytosis plays a pivotal role in nutrient acquisition and evasion from the host defense systems in Entamoeba histolytica, the intestinal protozoan parasite that causes amoebiasis. We previously reported that E. histolytica possesses a unique class of a hydrolase receptor family, designated the cysteine protease-binding protein family (CPBF), that is involved in trafficking of hydrolases to lysosomes and phagosomes, and we have also reported that CPBF1 and CPBF8 bind to cysteine proteases or β-hexosaminidase α-subunit and lysozymes, respectively. In this study, we showed by immunoprecipitation that CPBF6, one of the most highly expressed CPBF proteins, specifically binds to α-amylase and γ-amylase. We also found that CPBF6 is localized in lysosomes, based on immunofluorescence imaging. Immunoblot and proteome analyses of the isolated phagosomes showed that CPBF6 mediates transport of amylases to phagosomes. We also demonstrated that the carboxyl-terminal cytosolic region of CPBF6 is engaged in the regulation of the trafficking of CPBF6 to phagosomes. Our proteome analysis of phagosomes also revealed new potential phagosomal proteins.

Indexed as

alpha-AmylasesAmylasesCysteine ProteasesEntamoeba histolyticaGene Expression ProfilingGlucan 1,4-alpha-GlucosidaseLysosomesPhagocytosisPhagosomesProteomeReceptors, Cell Surfacealpha-AmylasesAmylasesCysteine ProteasesGlucan 1,4-alpha-GlucosidaseProteomeReceptors, Cell Surface

Identifiers

PMID23509141
PMCPMC3648001
OpenAlexW2097976777

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.