Evidence map›Paper›PMID 24626316›Full record

ArticlePloS one2014

Proteomic identification of S-nitrosylated proteins in the parasite Entamoeba histolytica by resin-assisted capture: insights into the regulation of the Gal/GalNAc lectin by nitric oxide.

Rivka Hertz, Shani Ben Lulu, Preeti Shahi, Meirav Trebicz-Geffen, Moran Benhar, Serge Ankri

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Impact of Reactive Sulfur Species onAntioxidants (Basel, Switzerland) · 2024
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  4. Insights into the Mechanisms ofAntioxidants (Basel, Switzerland) · 2022
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  5. Microorganisms · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Identification of S-Nitrosylated (SNO) Proteins inFrontiers in cellular and infection microbiology · 2017
    Article
  12. Article
  13. Article
  14. 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

6 authors at 1 institution in 1 country.

Rivka HertzDepartment of Molecular Microbiology, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Shani Ben LuluDepartment of Biochemistry, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Preeti ShahiDepartment of Molecular Microbiology, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Meirav Trebicz-GeffenDepartment of Molecular Microbiology, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Moran BenharDepartment of Biochemistry, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Serge AnkriDepartment of Molecular Microbiology, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
Rappaport Family Institute for Research in the Medical Sciences · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Entamoeba histolytica is a gastrointestinal protozoan parasite that causes amebiasis, a disease which has a worldwide distribution with substantial morbidity and mortality. Nitrosative stress, which is generated by innate immune cells, is one of the various environmental challenges that E. histolytica encounters during its life cycle. Although the effects of nitric oxide (NO) on the regulation of gene expression in this parasite have been previously investigated, our knowledge on S-nitrosylated proteins in E.histolytica is lacking. In order to fill this knowledge gap, we performed a large-scale detection of S-nitrosylated (SNO) proteins in E.histolytica trophozoites that were treated with the NO donor, S-nitrosocysteine by resin-assisted capture (RAC). We found that proteins involved in glycolysis, gluconeogenesis, translation, protein transport, and adherence to target cells such as the heavy subunit of Gal/GalNac lectin are among the S-nitrosylated proteins that were enriched by SNO-RAC. We also found that the S-nitrosylated cysteine residues in the carbohydrate recognition domain (CRD) of Gal/GalNAc lectin impairs its function and contributes to the inhibition of E.histolytica adherence to host cells. Collectively, these results advance our understanding of the mechanism of reduced E.histolytica adherence to mammalian cells by NO and emphasize the importance of NO as a regulator of key physiological functions in E.histolytica.

Indexed as

CarbohydratesCell AdhesionChromatography, AffinityCysteineEntamoeba histolyticaEntamoebiasisGlycolysisHeLa CellsHumansLectinsNitric OxideNitrogenProtein TransportProteomeProteomicsProtozoan ProteinsCarbohydratesCysteineLectinsNitric OxideNitrogenProteomeProtozoan ProteinsS-nitrosocysteineS-Nitrosothiols

Identifiers

PMID24626316
PMCPMC3953491
OpenAlexW2072890882

What OpenQuestion holds

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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.