Evidence map›Paper›PMID 41618743›Full record

ArticleFEBS open bio2026

Promiscuous stimulation of HSP70 ATPase activity by parasite-derived J-domains.

Julian Barth, Moritz Koch, Le-Han Rössner, Johanna Eichhorn, Denys Pogoryelov, Matthias P Mayer, Jude M Przyborski

Abstract read
In one paragraph

Article in FEBS open bio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

7 authors.

Julian BarthBiochemistry and Molecular Biology, Justus Liebig University, Giessen, Germany.
Moritz KochCenter for Molecular Biology (ZMBH), Heidelberg, Germany.
Le-Han RössnerInstitute of Botany, Justus Liebig University, Giessen, Germany.ORCID https://orcid.org/0009-0008-5759-9874
Johanna EichhornBiochemistry and Molecular Biology, Justus Liebig University, Giessen, Germany.
Denys PogoryelovBiochemistry and Molecular Biology, Justus Liebig University, Giessen, Germany.
Matthias P MayerCenter for Molecular Biology (ZMBH), Heidelberg, Germany.ORCID https://orcid.org/0000-0002-7859-3112
Jude M PrzyborskiBiochemistry and Molecular Biology, Justus Liebig University, Giessen, Germany.ORCID https://orcid.org/0000-0002-3494-7767

Funding

Loewe Center DRUID of Land Hesse
6 · The paper itself

Abstract

The malaria parasite P. falciparum exports a large number of proteins to the human host cell, including members of the J-domain protein (JDP) family. In other systems, JDPs stimulate the ATPase activity of HSP70 and direct client protein interactions. Three exported PfJDP are highly homologous yet appear to have divergent roles. We examined the ability of isolated J-domains from these proteins to stimulate the ATPase activity of PfHSP70-X and human HsHSP70 and HsHSC70. In vitro assays demonstrate that all domains stimulate the ATPase activity of each HSP70 tested. While overall stimulation was broadly comparable, differences were observed between individual PfJDP-HSP70 pairings. Our findings support a model in which the parasite systematically exports JDPs to exploit the host's chaperone power.

Indexed as

Adenosine TriphosphatasesHSP70 Heat-Shock ProteinsPlasmodium falciparumProtozoan ProteinsHumansProtein DomainsAdenosine TriphosphatasesHSP70 Heat-Shock ProteinsProtozoan ProteinsATPase activityHSP70J‐domain proteinmolecular chaperoneparasite–host interactionPlasmodium falciparum

Identifiers

PMID41618743
PMCPMC13327048

What OpenQuestion holds

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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.