Evidence map›Paper›PMID 12049643›Full record

ArticleThe Biochemical journal2002

TcGPXII, a glutathione-dependent Trypanosoma cruzi peroxidase with substrate specificity restricted to fatty acid and phospholipid hydroperoxides, is localized to the endoplasmic reticulum.

Shane R Wilkinson, Martin C Taylor, Said Touitha, Isabel L Mauricio, David J Meyer, John M Kelly

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 111 citations in OpenAlex.

  1. Mitochondrial CaAntioxidants & redox signaling · 2022
    Review
  2. Review
  3. Frontiers in cellular and infection microbiology · 2022
    Article
  4. Article
  5. Redox Balance Keepers and Possible Cell Functions Managed by Redox Homeostasis inFrontiers in cellular and infection microbiology · 2019
    Review
  6. Kinetics, subcellular localization, and contribution to parasite virulence of aProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  7. Article
  8. Article
  9. Article
  10. A ComparativeEvolutionary bioinformatics online · 2016
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Vitamin C biosynthesis in trypanosomes: a role for the glycosome.Proceedings of the National Academy of Sciences of the United States of America · 2005
    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.

Shane R WilkinsonDepartment of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK. shane.wilkinson@lshtm.ac.uk
Martin C Taylor
Said Touitha
Isabel L Mauricio
David J Meyer
John M Kelly
University of London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Until recently, it had been thought that trypanosomes lack glutathione peroxidase activity. Here we report the subcellular localization and biochemical properties of a second glutathione-dependent peroxidase from Trypanosoma cruzi (TcGPXII). TcGPXII is a single-copy gene which encodes a 16 kDa protein that appears to be specifically dependent on glutathione as the source of reducing equivalents. Recombinant TcGPXII was purified and shown to have peroxidase activity towards a narrow substrate range, restricted to hydroperoxides of fatty acids and phospholipids. Analysis of the pathway revealed that TcGPXII activity could be readily saturated by glutathione and that the peroxidase functioned by a Ping Pong mechanism. Enzyme reduction was shown to be the rate-limiting step in this pathway. Using immunofluorescence, TcGPXII was shown to co-localize with a homologue of immunoglobulin heavy-chain binding protein (BiP), a protein restricted to the endoplasmic reticulum and Golgi. As the smooth endoplasmic reticulum is the site of phospholipid and fatty acid biosynthesis, this suggests that TcGPXII may play a specific role in the T. cruzi oxidative defence system by protecting newly synthesized lipids from peroxidation.

Indexed as

Amino Acid SequenceAnimalsFatty AcidsGlutathioneGlutathione PeroxidaseHumansHydrogen PeroxideKineticsMolecular Sequence DataPhospholipidsPhylogenyRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificityTrypanosoma cruziFatty AcidsGlutathioneGlutathione PeroxidaseGPX2 protein, humanHydrogen PeroxidePhospholipidsRecombinant Proteins

Identifiers

PMID12049643
PMCPMC1222628
OpenAlexW1979213367

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.