ArticleMolecular diversity2013
Exploring the chemical space of aromatase inhibitors.
Article in Molecular diversity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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.
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Who cites it
12 citing papers in PubMed, 41 citations in OpenAlex.
- Synthesis, Biological Studies, andComputational and structural biotechnology journal · 2026Article
- Insight into TLR4 receptor inhibitory activityRSC advances · 2023Article
- Synthesis of acetamidosulfonamide derivatives with antioxidative and QSAR studies.EXCLI journal · 2022Article
- In Silico Drug Repurposing for Anti-Inflammatory Therapy: Virtual Search for Dual Inhibitors of Caspase-1 and TNF-Alpha.Biomolecules · 2021Article
- Hip fractures in the elderly without osteoporosis.Journal of frailty, sarcopenia and falls · 2018Article
- Towards understanding aromatase inhibitory activity via QSAR modeling.EXCLI journal · 2018Review
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- Large-scale structure-activity relationship study of hepatitis C virus NS5B polymerase inhibition using SMILES-based descriptors.Molecular diversity · 2015Article
- Prediction of aromatase inhibitory activity using the efficient linear method (ELM).EXCLI journal · 2015Article
- Navigating the chemical space of dipeptidyl peptidase-4 inhibitors.Drug design, development and therapy · 2015Article
- Probing the origins of aromatase inhibitory activity of disubstituted coumarins via QSAR and molecular docking.EXCLI journal · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aromatase, a rate-limiting enzyme catalyzing the conversion of androgen to estrogen, is overexpressed in human breast cancer tissue. Aromatase inhibitors (AIs) have been used for the treatment of estrogen-dependent breast cancer in post-menopausal women by blocking the biosynthesis of estrogen. The undesirable side effects in current AIs have called for continued pursuit for novel candidates with aromatase inhibitory properties. This study explores the chemical space of all known AIs as a function of their physicochemical properties by means of univariate (i.e., statistical and histogram analysis) and multivariate (i.e., decision tree and principal component analysis) approaches in order to understand the origins of aromatase inhibitory activity. Such a non-redundant set of AIs spans a total of 973 compounds encompassing both steroidal and non-steroidal inhibitors. Substructure analysis of the molecular fragments provided pertinent information on the structural features important for ligands providing high and low aromatase inhibition. Analyses were performed on data sets stratified according to their structural scaffolds (i.e., steroids and non-steroids) and bioactivities (i.e., actives and inactives). These analyses have uncover a set of rules characteristic to active and inactive AIs as well as revealing the constituents giving rise to potent aromatase inhibition.
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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.