Evidence map›Paper›PMID 39419910›Full record

ReviewParasitology research2024

H

Karina Araujo-Ruiz, Ricardo Mondragón-Flores

Abstract readReview
In one paragraph

Review in Parasitology research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Karina Araujo-RuizDepartamento de Bioquímica, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Av. IPN 2508 Col. Zacatenco, Ciudad de México, 07360, México.
Ricardo Mondragón-FloresDepartamento de Bioquímica, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Av. IPN 2508 Col. Zacatenco, Ciudad de México, 07360, México. rmflores@cinvestav.mx.

Funding

Consejo Nacional de Ciencia y Tecnología , México 51486 FORDECYT-PRONACES
6 · The paper itself

Abstract

Integral membrane pyrophosphatases (mPPases) hydrolyze pyrophosphate. This enzymatic mechanism is coupled with the pumping of H + and/or Na + across membranes, which can be either K + -dependent or K + -independent. Inorganic proton-translocating pyrophosphatases (H + -PPases) can transport protons across cell membranes and are reported in various organisms such as plants, bacteria, and protozoan parasites. The evolutionary implications of these enzymes are of great interest for proposing approaches related to the treatment of parasitic of phytopathogenic diseases. This work presents a literature review on pyrophosphate, pyrophosphatases, their inhibitors and emphasizes H + -PPases found in various medically significant protozoan parasites such as Toxoplasma gondii, the causative agent of toxoplasmosis, and Plasmodium falciparum, the causative agent of malaria, as well as protozoan species that primarily affect animals, such as Eimeria maxima and Besnoitia besnoiti.

Indexed as

EukaryotaAnimalsDiphosphatesInorganic PyrophosphataseDiphosphatesInorganic PyrophosphataseH + -PPasemPPaseParasitesProtozoanPyrophosphatase

Identifiers

PMID39419910
PMCPMC11486809

What OpenQuestion holds

Textmetadata
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.