ArticleEuropean journal of medicinal chemistry2011
Selective and potent agonists for estrogen receptor beta derived from molecular refinements of salicylaldoximes.
Article in European journal of medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Update on the therapeutic significance of estrogen receptor beta in malignant gliomas.Oncotarget · 2017Review
- Cyclic Ketoximes as Estrogen Receptor β Selective Agonists.ChemMedChem · 2016Article
- Estrogen Exhibits a Biphasic Effect on Prostate Tumor Growth through the Estrogen Receptor β-KLF5 Pathway.Molecular and cellular biology · 2016Article
- Salicylketoximes That Target Glucose Transporter 1 Restrict Energy Supply to Lung Cancer Cells.ChemMedChem · 2015Article
- Bioactive heterocycles containing endocyclic N-hydroxy groups.European journal of medicinal chemistry · 2015Review
- Highly selective salicylketoxime-based estrogen receptor β agonists display antiproliferative activities in a glioma model.Journal of medicinal chemistry · 2015Article
- Structural and Functional Diversity of Estrogen Receptor Ligands.Current topics in medicinal chemistry · 2015Review
- Estrogen receptors alpha (ERα) and beta (ERβ): subtype-selective ligands and clinical potential.Steroids · 2014Review
- Triaryl-substituted Schiff bases are high-affinity subtype-selective ligands for the estrogen receptor.Journal of medicinal chemistry · 2014Article
- Nonsteroidal bivalent estrogen ligands: an application of the bivalent concept to the estrogen receptor.ACS chemical biology · 2013Article
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Authors and funding
11 authors.
Funding
Abstract
In a continuing effort to improve the subtype selectivity and agonist potency of estrogen receptor β (ERβ) ligands, we have designed and developed a thus far unexplored structural series obtained by molecular refinements of monoaryl-substituted salicylaldoximes (Salaldox B). The most interesting compounds in this series (2c, d) show remarkably high ERβ-binding affinities, with Ki values reaching the sub-nanomolar range (Ki=0.38 nM for 2c and 0.57 nM for 2d), and have very high levels of ERβ-subtype selectivity. Both compounds show a potent full agonist character on ERβ (EC50=0.23 nM for 2c and 1.3 nM for 2d). Furthermore, 2d shows a remarkable functional subtype selectivity, with a β/α transcription potency ratio 50-fold higher than that of estradiol.
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Registered trials
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.