Evidence map›Paper›PMID 40588719›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2025

Identification of chemical scaffolds for targeting ubiquitin-specific protease 11 (USP11) through high-throughput virtual screening.

Hobin Lee, Sunghoon Hurh, Soomin Kang, Jihwan Yoon, Jong-Ik Hwang, Derek T Logan, Hong-Rae Kim

Abstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2025. 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

7 authors.

Hobin LeeLaboratory of Discovery Chemistry, Department of Biomedical Sciences, Korea University College of Medicine, Seoul, Republic of Korea.
Sunghoon HurhGPCR & Signal Transduction Laboratory, Department of Biomedical Sciences, Korea University College of Medicine, Seoul, Republic of Korea.
Soomin KangLaboratory of Discovery Chemistry, Department of Biomedical Sciences, Korea University College of Medicine, Seoul, Republic of Korea.
Jihwan YoonLaboratory of Discovery Chemistry, Department of Biomedical Sciences, Korea University College of Medicine, Seoul, Republic of Korea.
Jong-Ik HwangGPCR & Signal Transduction Laboratory, Department of Biomedical Sciences, Korea University College of Medicine, Seoul, Republic of Korea.
Derek T LoganSection for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden.
Hong-Rae KimLaboratory of Discovery Chemistry, Department of Biomedical Sciences, Korea University College of Medicine, Seoul, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

USP11 is a promising therapeutic target implicated in Alzheimer's disease and various cancers; however, no specific inhibitors are currently available, with the only known inhibitor being mitoxantrone, which primarily targets topoisomerase II. To identify novel chemical starting points, we conducted high-throughput virtual screening using a USP11 homology model. Screening over 600,000 compounds yielded five structurally distinct hits with significant inhibitory activity. Biochemical validation highlighted two promising scaffolds: benzoxadiazole derivatives and pyrrolo-phenylamidine analogues, both demonstrating structure-dependent inhibition and tractable SAR profiles. Docking studies further characterised their binding modes, supporting their potential for optimisation. Hydroxyphenyl hydrazone analogues raised PAINS-related concerns, while compounds such as squalamine were deprioritized due to weak binding affinity and structural complexity. Overall, this study provides valuable scaffolds and mechanistic insights that can inform future development of potent, selective USP11 inhibitors.

Indexed as

Enzyme InhibitorsHigh-Throughput Screening AssaysOxadiazolesDose-Response Relationship, DrugHumansMolecular Docking SimulationMolecular StructureStructure-Activity RelationshipEnzyme InhibitorsOxadiazolesinhibitorprotein-ligand interactionsUbiquitin-specific proteasevirtual screening

Identifiers

PMID40588719
PMCPMC12210405

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LicenceCC BY
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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.