Evidence map›Paper›PMID 41957281›Full record

ArticleNature chemical biology2026

The molecular glue CLEO4-88 inhibits the ACAA1 thiolase by induced binding to GID4.

Chetan K Chana, Ines Ben Makhlouf, Jaeyoun Kim, April J Y Yu, Nathalie Moatti, Stephen Orlicky, Cassandra J Wong, Leon Baronijan, XiaoJing Tang, Daniel Mao and 11 more

Abstract read
PubMed Publisher
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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Recruiting without destroying.Nature chemical biology · 2026
    Article
  2. 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

21 authors.

Chetan K ChanaLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada. chana@lunenfeld.ca.ORCID http://orcid.org/0000-0002-1176-0190
Ines Ben Makhlouf *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0008-1960-3748
Jaeyoun Kim *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0001-8809-8054
April J Y Yu *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0005-4973-208X
Nathalie Moatti *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Stephen Orlicky *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Cassandra J Wong *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0009-7292-3780
Leon Baronijan *Department of Immunology, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0002-8259-7885
XiaoJing Tang *Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Daniel MaoLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Brett LarsenLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Laura McGaryLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Brendon SealeLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Pavel MaderLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Derek F CeccarelliLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Philip BarbulescuDepartment of Immunology, University of Toronto, Toronto, Ontario, Canada.
Alberto MartinDepartment of Immunology, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-1260-7710
Daniel DurocherLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.
Laurence PelletierLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0003-1171-4618
Anne-Claude GingrasLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-6090-4437
Frank SicheriLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada. sicheri@lunenfeld.ca.ORCID http://orcid.org/0000-0002-9824-2117

Funding

Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada) FRN-167279Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada) PJT-180338Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada) TFRI-1107-04Terry Fox Research Institute (Institut de Recherche Terry Fox) TFRI-1107-04
6 · The paper itself

Abstract

Molecular glues promote protein-protein interactions by enhancing the surface complementarity between proteins. Those that recruit an E3 ubiquitin ligase to a target can elicit ubiquitination and subsequent destruction of the target protein-a mechanism that underpins the field of targeted protein degradation (TPD). Here we explored whether small-molecule binders to the CTLH E3 ligase subunit GID4 could act as molecular glues. We discovered that CLEO4-88 functions as a molecular glue (EC

Indexed as

Ubiquitin-Protein LigasesHumansModels, MolecularProtein BindingUbiquitinationUbiquitin-Protein Ligases

Identifiers

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.