ArticleSaudi journal of biological sciences2021
High-throughput screening to identify potential inhibitors of the Zα domain of the adenosine deaminase 1 (ADAR1).
Article in Saudi journal of biological sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Orchestrating innate immunity through RNA editing and helicase activity: ADAR1, dsRNA sensors, and tumor immune evasion.Frontiers in cell and developmental biology · 2026Review
- Cromolyn as a novel pharmacophore of the Zα domain of the RNA-editing enzyme ADAR1p150.Protein science : a publication of the Protein Society · 2025Article
- Adenosine-to-inosine RNA editing in cancer: molecular mechanisms and downstream targets.Protein & cell · 2025Review
- ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024Review
- Chemical Modifications in RNA: Elucidating the Chemistry of dsRNA-Specific Adenosine Deaminases (ADARs).Accounts of chemical research · 2023Article
- A-to-I RNA editing by ADAR and its therapeutic applications: From viral infections to cancer immunotherapy.Wiley interdisciplinary reviews. RNA · 2023Review
- RNA modification: mechanisms and therapeutic targets.Molecular biomedicine · 2023Review
- Advances in targeting RNA modifications for anticancer therapy.Trends in cancer · 2023Review
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adenosine deaminases acting on RNA 1 (ADAR1) are enzymes involved in editing adenosine to inosine in the dsRNAs of cells associated with cancer development. The p150 isoform of ADAR1 is the only isoform containing the Zα domain that binds to both Z-DNA and Z-RNA. The Zα domain is suggested to modulate the immune response and could be a suitable target for antiviral treatment and cancer immunotherapy. In this study, we aimed to identify potential inhibitors for ADAR1 protein that bind the Zα domain using molecular docking and simulation tools. Virtual docking and molecular dynamics simulation approaches were used to screen the potential activity of 2115 FDA-approved compounds on the Zα domain of ADAR1 and filtered for to obtain the top-scoring hits. The top three compounds with the best XP Gscore-namely alendronate (-7.045), etidronate (-6.923), and zoledronate (-6.77)-were subjected to 50 ns simulations to characterize complex stability and identify the fundamental interactions that contribute to inhibition of the ADAR1 Zα domain. The three compounds were shown to interact with Lys169, Lys170, Asn173, and Tyr177 of the Zα domain-like helical backbone of Z-RNA. The study provides a comprehensive and novel insights of repurposes drugs for the inhibition of ADAR1 function.
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