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Structural Insight into PRMT5 Inhibitors through Amalgamating Pharmacophore-Based Virtual Screening, ADME-Toxicity and Binding Energy Studies and Identify New Inhibitors by Molecular Docking.

2021-08-26

Abstract excerpt

<title>Abstract</title> <p>Protein arginine methyltransferase 5 (PRMT5) is a member of the methyltransferases family, a type II arginine enzyme that is crucial for many cellular processes and is associated with many cancer diseases. In this study, pharmacophore-based 3D QSAR modeling, virtual screening and binding free energy studies were carried out from a set of 61 potent compounds reported being inhibitors of...

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Literature Corpus work
811d9838-63f5-5867-a542-17d268dbeb88
DOI
10.21203/rs.3.rs-819089/v1
Open publication

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Structural Insight into PRMT5 Inhibitors through Amalgamating Pharmacophore-Based Virtual Screening, ADME-Toxicity and Binding Energy Studies and Identify New Inhibitors by Molecular Docking.DOI 10.21203/rs.3.rs-819089/v1
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