Evidence map›Paper›PMID 41898490›Full record

ArticleInternational journal of molecular sciences2026

Identification of a New Phosphorylated Host Interactor of the Epstein-Barr Virus (EBV) Kinase BGLF4 Suggests Key Points for EBV-Specific Antiviral Drug Targeting.

Melanie Kögler, Christina Wangen, Alena Hammerschmitt, Debora Obergfäll, Friedrich Hahn, Manfred Marschall

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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. 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.

Melanie KöglerHarald zur Hausen Institute of Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Schlossgarten 4, 91054 Erlangen, Germany.
Christina WangenHarald zur Hausen Institute of Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Schlossgarten 4, 91054 Erlangen, Germany.
Alena HammerschmittHarald zur Hausen Institute of Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Schlossgarten 4, 91054 Erlangen, Germany.
Debora ObergfällHarald zur Hausen Institute of Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Schlossgarten 4, 91054 Erlangen, Germany.ORCID 0009-0009-8984-0340
Friedrich HahnHarald zur Hausen Institute of Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Schlossgarten 4, 91054 Erlangen, Germany.ORCID 0000-0003-3011-8416
Manfred MarschallHarald zur Hausen Institute of Virology, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Schlossgarten 4, 91054 Erlangen, Germany.

Funding

Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) 401821119-Research Training Group GRK2504.1-2/A1Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) MA 1289/11-3Volkswagen-Stiftung AZ-9B783-M.M./S.B.T.Wilhelm Sander-Stiftung M.M./H.S. AZ2022.073.1
6 · The paper itself

Abstract

Epstein-Barr virus (EBV) is a human pathogenic and oncogenic herpesvirus, with worldwide importance, at times associated with serious to life-threatening symptoms, especially in immunocompromised hosts. The available preventive options against EBV disease are limited to medically elaborate and cost-intensive measures of cell-based immunotherapy. The development of novel options of anti-EBV drug targeting is currently a matter of intense international efforts. A putative target of the antiviral therapy approach is the EBV-encoded protein kinase BGLF4, which fulfills a multifaceted role in productive viral replication. So far, viral BGLF4 interactor proteins and phosphorylated substrates have occasionally been reported, but in particular cellular interactors await further characterization concerning both, their relevance for BGLF4 functionality and their accessibility to antiviral drugs. In this study, we have analyzed host cell-BGLF4 interaction, BGLF4 kinase properties, and BGLF4-directed small molecules. The main results are as follows:

Indexed as

Antiviral AgentsEpstein-Barr Virus InfectionsHerpesvirus 4, HumanHost-Pathogen InteractionsProtein Serine-Threonine KinasesViral ProteinsCell LineHumansPhosphorylationProtein BindingVirus ReplicationAntiviral AgentsBGLF4 protein, Epstein-Barr virusProtein Serine-Threonine KinasesViral ProteinsEpstein–Barr virus (EBV)host pyruvate dehydrogenase (PDH)kinase inhibitors with antiviral potentialmass spectrometry-based identification of BGLF4–PDH interactionnovel options of anti-EBV drug targetingPDH phosphorylation by in vitro BGLF4 activityviral kinase BGLF4

Identifiers

PMID41898490
PMCPMC13026206

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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.