Evidence map›Paper›PMID 10903134›Full record

ArticleThe Biochemical journal2000

Vacuolar proton pyrophosphatase activity and pyrophosphate (PPi) in Toxoplasma gondii as possible chemotherapeutic targets.

C O Rodrigues, D A Scott, B N Bailey, W De Souza, M Benchimol, B Moreno, J A Urbina, E Oldfield, S N Moreno

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. HParasitology research · 2024
    Review
  3. Review
  4. Article
  5. The Toxoplasma plant-like vacuolar compartment (PLVAC).The Journal of eukaryotic microbiology · 2022
    Review
  6. Article
  7. Article
  8. Multi-target heteroleptic palladium bisphosphonate complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  9. Asymmetry in catalysis byScience advances · 2019
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  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

9 authors at 1 institution in 1 country.

C O RodriguesLaboratory of Molecular Parasitology, Department of Pathobiology, College of Veterinary Medicine, University of Illinois at Urbana-Champaign, 2001 South Lincoln Avenue, Urbana, IL 61802, USA.
D A Scott
B N Bailey
W De Souza
M Benchimol
B Moreno
J A Urbina
E Oldfield
S N Moreno
University of Illinois Urbana-Champaign · US

Funding

ACIDOCALCISOMES AND TOXOPLASMA GONDIIR01AI043614 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI MORENO, SILVIA N · 1999 to 2003
$964k
NIAID NIH HHS AI43614
6 · The paper itself

Abstract

The addition of PP(i) promoted the acidification of a subcellular compartment in cell homogenates of Toxoplasma gondii tachyzoites, implying the presence of a proton-translocating pyrophosphatase. The proton gradient was collapsed by addition of the K(+)/H(+) antiporter nigericin, and was also inhibited by addition of the PP(i) analogue aminomethylenediphosphonate (AMDP). Both proton transport and PP(i) hydrolysis were dependent upon K(+), but Na(+) caused partial inhibition of these activities. PP(i) hydrolysis was sensitive in a dose-dependent manner to AMDP, imidodiphosphate, NaF and to the thiol reagent N-ethylmaleimide. This activity was unaffected by common inhibitors of phosphohydrolases, except that NaO(3)V (sodium orthovanadate) stimulated the activity by 87%. Immunofluorescence microscopy, using antisera raised against conserved peptide sequences of a plant vacuolar pyrophosphatase, suggested that the pyrophosphatase in T. gondii tachyzoites was located in the plasma membrane and intracellular vacuoles of the parasite. High-field (31)P-NMR spectroscopy showed that PP(i )was more abundant than ATP in tachyzoites. Bisphosphonates (PP(i) analogues), drugs that are used in the treatment of bone diseases, inhibited proton transport and PP(i) hydrolysis in tachyzoite homogenates, and also inhibited intracellular proliferation of tachyzoites in tissue culture cells.

Indexed as

AnimalsAntiprotozoal AgentsDiphosphatesEnzyme InhibitorsProtonsPyrophosphatasesSubcellular FractionsToxoplasmaVacuolesAntiprotozoal AgentsDiphosphatesEnzyme InhibitorsProtonsPyrophosphatases

Identifiers

PMID10903134
PMCPMC1221200
OpenAlexW2096818171

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.