ArticleActa crystallographica. Section F, Structural biology communications2020
Crystallization and structure of ebselen bound to Cys141 of human inositol monophosphatase.
Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
The trial behind it
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Ebselen restores mitochondrial function through metabolic rewiring in Barth syndrome and related mitochondrial diseases.EMBO molecular medicine · 2026Article
- The Potential Use of Ebselen in Treatment-Resistant Depression.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Selenium-Catalyzed Reduction of Hydroperoxides in Chemistry and Biology.Antioxidants (Basel, Switzerland) · 2021Review
- Ebselen and Analogues: Pharmacological Properties and Synthetic Strategies for Their Preparation.Molecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Inositol monophosphatase (IMPase) is inhibited by lithium, which is the most efficacious treatment for bipolar disorder. Several therapies have been approved, or are going through clinical trials, aimed at the replacement of lithium in the treatment of bipolar disorder. One candidate small molecule is ebselen, a selenium-containing antioxidant, which has been demonstrated to produce lithium-like effects both in a murine model and in clinical trials. Here, the crystallization and the first structure of human IMPase covalently complexed with ebselen, a 1.47 Å resolution crystal structure (PDB entry 6zk0), are presented. In the complex with human IMPase, ebselen in a ring-opened conformation is covalently attached to Cys141, a residue located away from the active site. IMPase is a dimeric enzyme and in the crystal structure two adjacent dimers share four ebselen molecules, creating a tetramer with approximate 222 symmetry. In the crystal structure presented in this publication, the active site in the tetramer is still accessible, suggesting that ebselen may function as an allosteric inhibitor or may block the binding of partner proteins.
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Registered trials
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