Evidence map›Paper›PMID 42120501›Full record

ArticleNature chemical biology2026

Dual E3 ligase recruitment by monovalent degraders for tunable SMARCA 2/4 degradation.

Valentina A Spiteri, Dmitri Segal, Alejandro Correa-Sáez, Kentaro Iso, Ryan Casement, Miquel Muñoz I Ordoño, Mark A Nakasone, Gajanan Sathe, Caroline Schätz, Hannah E Peters and 5 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. A tail of two ligases.Nature chemical biology · 2026
    Article
  2. Review
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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

15 authors.

Valentina A Spiteri *Centre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.
Dmitri Segal *CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.
Alejandro Correa-Sáez *Centre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0001-5240-4865
Kentaro IsoCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0001-5417-3642
Ryan CasementCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0001-8075-0757
Miquel Muñoz I OrdoñoCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.ORCID http://orcid.org/0009-0003-4391-6393
Mark A NakasoneCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-1362-191X
Gajanan SatheCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-6239-5365
Caroline SchätzCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.ORCID http://orcid.org/0000-0002-8391-8778
Hannah E PetersCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.
Mark DowardCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0001-5765-0926
Lisa KainacherCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.
Angus D CowanCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-9702-7319
Alessio CiulliCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee, UK. a.ciulli@dundee.ac.uk.ORCID http://orcid.org/0000-0002-8654-1670
Georg E WinterCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria. gwinter@aithyra.at.ORCID http://orcid.org/0000-0001-6606-1437

Funding

Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung) P7909, P36746 and P5918723EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 101170771EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 851478EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 875510 (EUbOPEN project)EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) H2020-MSCA-IF-2020-101024945 DELETEREuropean Molecular Biology Organization (EMBO) EMBO ALTF 283-2023Vienna Science and Technology Fund (Wiener Wissenschafts-, Forschungs- und Technologiefonds) LS21-015Wellcome Trust
6 · The paper itself

Abstract

Proteolysis-targeting chimeras (PROTACs) and molecular glue degraders (MGDs) target proteins for degradation by co-opting an E3 ligase. While heterotrivalent PROTACs that can recruit multiple E3 ligases have been described, all MGDs reported to date depend on a single E3. Using orthogonal genetic screening, biophysical and structural analyses, we show that a monovalent MGD can recruit CUL4

Indexed as

Transcription FactorsUbiquitin-Protein LigasesHEK293 CellsHumansProteolysisProteolysis Targeting ChimeraProteolysis Targeting ChimeraTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID42120501
PMCPMC13612222

What OpenQuestion 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 OpenQuestion graph.