Evidence map›Paper›PMID 41418773›Full record

ArticleCell reports. Medicine2026

Oxidized MIF is an Alzheimer's disease drug target relaying external risk factors to tau pathology.

Andreas Müller-Schiffmann, Felix Torres, Anatoliy Kitaygorodskyy, Anand Ramani, Argyro Alatza, Sarah K Tschirner, Julien Orts, Arthur Haltrich, Ingrid Prikulis, Shaofeng Yu and 11 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports. Medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

21 authors.

Andreas Müller-SchiffmannDepartment Neuropathology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Felix TorresLaboratory of Physical Chemistry, ETH Zürich, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.
Anatoliy KitaygorodskyyProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Anand RamaniInstitute of Human Genetics, University Hospital, Friedrich-Schiller-Universität Jena, 07740 Jena, Germany.
Argyro AlatzaDepartment of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 1PJ, UK.
Sarah K TschirnerDepartment Neuropathology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Julien OrtsLaboratory of Physical Chemistry, ETH Zürich, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland; Department of Pharmaceutical Sciences, University of Vienna, 1090 Vienna, Austria.
Arthur HaltrichDepartment Neuropathology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Ingrid PrikulisDepartment Neuropathology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Shaofeng YuProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Debendranath DeyProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Suguna MalleshProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Dharma PrasadProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Dennis SolasProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Verian BaderDepartment Neuropathology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Annemieke RozemullerDepartment Pathology, VUMC Amsterdam, 1081HV Amsterdam, the Netherlands.
Selina WrayDepartment of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 1PJ, UK.
Jay GopalakrishnanInstitute of Human Genetics, University Hospital, Friedrich-Schiller-Universität Jena, 07740 Jena, Germany.
Roland RiekLaboratory of Physical Chemistry, ETH Zürich, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.
Vishwanath R LingappaProsetta Biosciences Inc, 670 5th Street, San Francisco, CA 94107, USA.
Carsten KorthDepartment Neuropathology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany. Electronic address: ckorth@hhu.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During deep co-evolution of viruses and host cells, viruses have selected specific host cellular proteins redirected from physiological functions to viral needs, thereby disturbing cellular proteostasis and increasing the risk of triggering protein misfolding diseases (PMDs). Identifying virus-specific, repurposed host proteins also allows the study of fundamental cellular events in "sporadic" PMDs, independent of the virus. Here, we identify a small molecule with very strong activity against neurotropic herpes simplex virus 1 (HSV-1), modulating an allosteric site of macrophage migration inhibitory factor (MIF). The compound efficiently reduces both HSV-1-mediated and non-mediated tau phosphorylation or aggregation in vitro and in vivo. The lead compound, as well as conformation-sensitive antibodies, specifically interacts with an oxidized conformer of MIF (oxMIF) enriched in postmortem brain homogenates of patients with Alzheimer's disease (AD). OxMIF thus participates in a host-viral interface connecting HSV-1 infection, and possibly other external stressors, with tau cellular pathology characteristic for PMDs, including AD.

Indexed as

Alzheimer DiseaseIntramolecular OxidoreductasesMacrophage Migration-Inhibitory Factorstau ProteinsAnimalsBrainHerpesvirus 1, HumanHumansMiceOxidation-ReductionPhosphorylationRisk FactorsIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsMIF protein, humantau ProteinsAlzheimer’s diseaseherpes virusmacrophage migration inhibitory factorneurodegenerationoxMIFprotein aggregationproteostasisrisk factortautauopathy

Identifiers

PMID41418773
PMCPMC12866179

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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.