Evidence map›Paper›PMID 42712752›Full record

ArticleRSC chemical biology2026

14-3-3/Tau molecular glues modulate

Maxime C M van den Oetelaar, Leandre Ravatt, Francisco Maqueda Zelaya, Ansgar Oberheide, Tom R van de Wijngaart, Floor M A van Boxtel, Marloes A M Pennings, Carlo J A Verhoef, Thijs W van Veldhuisen, Peter J Cossar and 3 more

Abstract read
In one paragraph

Article in RSC chemical biology, 2026. 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

13 authors.

Maxime C M van den OetelaarLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0002-1224-4171
Leandre RavattGerman Center for Neurodegenerative Diseases (DZNE) Department Charité University Medicine, Charitéplatz 1 10117 Berlin Germany susanne.wegmann@dzne.de.
Francisco Maqueda ZelayaLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0002-9962-159X
Ansgar OberheideLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0003-3664-5428
Tom R van de WijngaartLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0009-0008-8968-909X
Floor M A van BoxtelLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0009-0005-2519-1960
Marloes A M PenningsLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0002-3366-0238
Carlo J A VerhoefLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0001-5720-1602
Thijs W van VeldhuisenLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0003-2304-0294
Peter J CossarLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0002-8260-5710
Christian OttmannLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0001-7315-0315
Susanne WegmannGerman Center for Neurodegenerative Diseases (DZNE) Department Charité University Medicine, Charitéplatz 1 10117 Berlin Germany susanne.wegmann@dzne.de.ORCID https://orcid.org/0000-0002-5388-2479
Luc BrunsveldLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology Groene Loper 3 5612 AE Eindhoven The Netherlands c.ottmann@tue.nl l.brunsveld@tue.nl.ORCID https://orcid.org/0000-0001-5675-511X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intrinsically disordered protein Tau is highly phosphorylated under pathological conditions, which, among others, results in Tau liquid-liquid phase separation (LLPS), followed by aggregation. The hub protein 14-3-3 regulates Tau protein solubility and prevents LLPS by binding with phosphorylated Tau residues pS214 and pS324. Here, we report the stabilization of this Tau/14-3-3 protein-protein interaction (PPI) using reversible-covalent small-molecule molecular glues. By strengthening the 14-3-3/Tau interaction the molecular glues enhance the effect of 14-3-3 on Tau solubility in LLPS. This demonstrates the potential of modulating the 14-3-3/Tau PPI for novel drug discovery efforts in neurodegenerative diseases.

Identifiers

PMID42712752
PMCPMC13551062

What Socratic holds

Textmetadata
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 Socratic graph.