Evidence map›Paper›PMID 9307028›Full record

ArticleThe Biochemical journal1997

Removal of hydrogen peroxide by the 29 kDa protein of Entamoeba histolytica.

I Bruchhaus, S Richter, E Tannich

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.6field-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

30 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Evaluation of the PEJournal of immunology research · 2021
    Article
  4. Article
  5. Article
  6. Flavonoids as a Natural Treatment AgainstFrontiers in cellular and infection microbiology · 2018
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. The cell surface proteome of Entamoeba histolytica.Molecular & cellular proteomics : MCP · 2014
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Peroxiredoxins in parasites.Antioxidants & redox signaling · 2012
    Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

I BruchhausBernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany.
S Richter
E Tannich
Bernhard Nocht Institute for Tropical Medicine · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 29 kDa protein of Entamoeba histolytica (Eh29), as well as a truncated variant of this protein, which lacks a cysteine-rich N-terminal region of 40 amino acid residues (Eh29mut), were recombinantly expressed in Escherichia coli and purified to homogeneity. Both recombinant proteins (recEh29, recEh29mut) were found to have hydrogen peroxide (H2O2)-removing activity, but recEh29 was twice as active as recEh29mut. For the consumption of exogenous H2O2, activity was dependent on the presence of reducing equivalents, such as dithiothreitol (DTT), indicating that Eh29 constitutes a thiol-dependent peroxidase. DTT was not required to remove H2O2 by recEh29 or recEh29mut when H2O2 was generated enzymically by the E. histolytica NADPH:flavin oxidoreductase. This enzyme produces H2O2 under aerobic conditions and simultaneously serves as a hydrogen donor for Eh29. Peroxidase activity of the recombinant proteins was further supported by complementation of an E. coli strain that lacks the entire alkyl hydroperoxide reductase locus. The high sensitivity of these bacteria against cumene hydroperoxide was significantly reduced by the introduction of the genes encoding recEh29 or recEh29mut. Using antisera raised against the recombinant proteins, native Eh29 was localized within the cytoplasm of the amoebae. In addition, the antisera reacted with proteins of E. histolytica lysates with apparent molecular masses of 35 kDa and 160-300 kDa. All of them exhibited thiol-peroxidase activity.

Indexed as

AnimalsEntamoeba histolyticaEscherichia coliHydrogen PeroxideProtozoan ProteinsRecombinant ProteinsHydrogen PeroxideProtozoan ProteinsRecombinant Proteins

Identifiers

PMID9307028
PMCPMC1218733
OpenAlexW42959172

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.