Evidence map›Paper›PMID 40091859›Full record

ArticleMolecular microbiology2025

A Soluble Expression Construct of the Isolated Catalytic Domain of Plasmodium falciparum ATP4 Exhibits ATPase Activity Independent of a γ-Phosphate Receiving Aspartate.

Timo Beyer, Jesko Caliebe, Lara Kähler, Eric Beitz

Abstract read
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In one paragraph

Article in Molecular microbiology, 2025. 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

4 authors.

Timo BeyerDepartment of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-University of Kiel, Kiel, Germany.
Jesko CaliebeDepartment of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-University of Kiel, Kiel, Germany.
Lara KählerDepartment of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-University of Kiel, Kiel, Germany.
Eric BeitzDepartment of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-University of Kiel, Kiel, Germany.ORCID 0000-0001-5912-6626

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sodium/proton-exchanging ATPase of Plasmodium falciparum malaria parasites, PfATP4, is an emerging drug target. Inhibition results in detrimental cell swelling due to cytosolic accumulation of sodium and alkalization. PfATP4 is a sodium-releasing type II P-type ATPase restricted to apicomplexan parasites. Experimental data on structure-function relationships of the isolated protein are absent. Here, we produced and purified the soluble catalytic domain of PfATP4 and evaluated kinetic properties by in vitro phosphate colorimetry. The protein exhibited Mg

Indexed as

Adenosine TriphosphatasesAspartic AcidPlasmodium falciparumProtozoan ProteinsAdenosine TriphosphateCatalytic DomainKineticsMagnesiumPhosphatesStructure-Activity RelationshipAdenosine TriphosphatasesAdenosine TriphosphateAspartic AcidMagnesiumPhosphatesProtozoan ProteinsATPasemalariaprotonsodiumstructure–function relationships

Identifiers

PMID40091859
PMCPMC12152296

What OpenQuestion holds

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Registered trials

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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.