ArticlePorto biomedical journal
Identification of afzelin potential targets in inhibiting triple-negative breast cancer cell migration using reverse docking.
Article in Porto biomedical journal. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- Harnessing AI-driven reverse docking in drug discovery: a comprehensive review of opportunities, challenges, and emerging trends.Journal of molecular modeling · 2025Review
- RPS6KA1 is a histone acetylation-related oncoprotein in acute myeloid leukemia which is targeted by afzelin.BMC cancer · 2024Article
- Exploring the Comprehensive Neuroprotective and Anticancer Potential of Afzelin.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Afzelin induces immunogenic cell death against lung cancer by targeting NQO2.BMC complementary medicine and therapies · 2023Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTriple-negative breast cancer (TNBC) tends to be aggressive and metastatic, characteristics attributable to its cellular migration capabilities. Afzelin is a chemical compound with anti-metastatic potentials. This study aimed to predict proteins involved in TNBC cell migration which could be inhibited by afzelin.
methodsThe protein database was constructed from the Kyoto Encyclopedia of Genes and Genomes pathways collection which related to cell motility, then screened for druggability using SuperTarget and Therapeutic Target Database. The involvement of druggable proteins in the TNBC metastasis process was investigated through existing publications in The National Center for Biotechnology Information PubMed database. Inhibitory potential of afzelin toward target proteins was compared to the proteins' known-inhibitor, using the reverse docking method.
resultsTen proteins identified as potential targets of afzelin, with the top 3 being ERK2, KRas, and FAK, respectively. Afzelin's 3-O-rhamnoside group played a dominant role in forming hydrogen bonds with the target proteins. Further analysis with STRING suggested that afzelin might be able to inhibit chemotaxis and haptotaxis of TNBC cells.
conclusionsAfzelin was predicted to inhibit TNBC cell motility, by targeting ERK2, KRas, and FAK activation.
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Registered trials
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