Evidence map›Paper›PMID 39694339›Full record

ArticleBioorganic & medicinal chemistry letters2025

Docking and structure activity relationship studies of potent and selective thiazolidinethione GSK-3 inhibitors.

Hannah Boesger, Kurtis Williams, Sa Adatu Abdullai, Brianna Hubble, Mahboubeh S Noori, Crina Orac, Deborah K Amesaki, Davoud Ghazanfari, Emily A Fairchild, Opeyemi O Fatunbi and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 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

14 authors.

Hannah BoesgerDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Kurtis WilliamsDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Sa Adatu AbdullaiDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Brianna HubbleDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Mahboubeh S NooriDepartment of Chemical and Biomolecular Engineering, Ohio University, Athens, OH 45701, USA.
Crina OracDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Deborah K AmesakiDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Davoud GhazanfariDepartment of Chemical and Biomolecular Engineering, Ohio University, Athens, OH 45701, USA.
Emily A FairchildDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Opeyemi O FatunbiDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Joshua A PritchardBiomedical Engineering Program, Ohio University, Athens, OH 45701, USA.
Douglas J GoetzDepartment of Chemical and Biomolecular Engineering, Ohio University, Athens, OH 45701, USA; Biomedical Engineering Program, Ohio University, Athens, OH 45701, USA.
Jennifer V HinesDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA.
Stephen C BergmeierDepartment of Chemistry & Biochemistry, Ohio University, Athens, OH 45701, USA. Electronic address: bergmeis@ohio.edu.

Funding

Novel Glycogen Synthase Kinase-3 (GSK-3) Inhibitors as Therapeutic AgentsR15GM110602 · NIGMS · OHIO UNIVERSITY ATHENS · PI GOETZ, DOUGLAS J · 2016 to 2025
$1.5M
NIGMS NIH HHS R15 GM110602
6 · The paper itself

Abstract

Glycogen synthase kinase-3 (GSK-3) plays a key role in several biochemical pathways and is an attractive target for pharmacological intervention. We prepared a series of analogs of a highly selective thiazolidinethione inhibitor of GSK-3. The structure-activity relationship indicated a precise structural requirement for potent inhibition. We used docking and bioinformatic analysis to explore the rationale for the potency and selectivity of this class of GSK-3 inhibitors. These computational studies identified residues unique to GSK-3 likely to play a role in ligand-specific induced fit interactions. Together, these studies highlight the structural stringency of specific kinase inhibition that can be achieved for GSK-3.

Indexed as

Glycogen Synthase Kinase 3Molecular Docking SimulationProtein Kinase InhibitorsThiazolidinesHumansMolecular StructureStructure-Activity RelationshipThionesGlycogen Synthase Kinase 3Protein Kinase InhibitorsThiazolidinesThionesComputational dockingGSK-3InhibitorsThiazolidinethione

Identifiers

PMID39694339
PMCPMC11808539

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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.