ArticleInternational journal of molecular sciences2020
Structural Basis for Design of New Purine-Based Inhibitors Targeting the Hydrophobic Binding Pocket of Hsp90.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Trastuzumab-TKI combination in HER2-Positive tumors: a FAERS-Based safety profile and multimodal analysis of Tanespimycin's role in enhancing targeting of the HSP90AA1-PI3K-Akt-mTOR axis.Frontiers in pharmacology · 2026Article
- Recent progress and structural insights of potential Hsp90 inhibitors as anticancer agents.Molecular diversity · 2025Review
- Small Molecule Modulation of MHC-I Surface Expression: A Click Chemistry-Based Discovery Approach.Journal of medicinal chemistry · 2025Article
- From molecule to medicine: introducing emerging strategies to synthesize potent anticancer purine scaffolds.RSC advances · 2025Review
- Review
- Geldanamycin treatment does not result in anti-cancer activity in a preclinical model of orthotopic mesothelioma.PloS one · 2023Article
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Inhibition of the molecular chaperone heat shock protein 90 (Hsp90) represents a promising approach for cancer treatment. BIIB021 is a highly potent Hsp90 inhibitor with remarkable anticancer activity; however, its clinical application is limited by lack of potency and response. In this study, we aimed to investigate the impact of replacing the hydrophobic moiety of BIIB021, 4-methoxy-3,5-dimethylpyridine, with various five-membered ring structures on the binding to Hsp90. A focused array of
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