ArticleMolecular diversity2025
Identification of potential NUDT5 inhibitors from marine bacterial natural compounds via molecular dynamics and free energy landscape analysis.
Article in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structure-based and machine learning-assisted identification of natural phytochemicals targeting Mycobacterium leprae InhA for anti-mycobacterial therapeutics.Folia microbiologica · 2026Article
- Targeting IDH-driven Oncometabolism in glioblastoma: a computational approach for the identification of potential inhibitors.Frontiers in bioinformatics · 2026Article
- Quercetin and Its Structural Analogs as NUDT5 Inhibitors: A Preliminary In Silico Study.International journal of molecular sciences · 2025Article
- Morin combined with meropenem is a potent inhibitor of NDM-1 against NDM-1-producing E. coli.Scientific reports · 2025Article
- Dual therapeutic potential of Scoparia dulcis in combating hyperglycemia and inflammation in diabetes through network pharmacology and in silico analysis.Scientific reports · 2025Article
- Computational analysis of zoanthamine alkaloids from Zoanthus sp. as potential DKK1 and GSK-3β inhibitors for osteoporosis therapy via Wnt signaling.Scientific reports · 2025Article
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4 authors.
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Abstract
NUDIX hydrolase 5 (NUDT5) is an enzyme involved in the hydrolysis of nucleoside diphosphates linked to other moieties, such as ADP-ribose. This cofactor is vital in redox reactions and is essential for the activity of sirtuins and poly(ADP-ribose) polymerases, which are involved in DNA repair and genomic stability. It has been shown that NUDT5 activity can also influence NAD+ homeostasis, thereby affecting cancer cell metabolism and survival. In this regard, the discovery of NUDT5 inhibitors has emerged as a potential therapeutic approach in cancer treatment. In this study, we conducted a high-throughput virtual screening of marine bacterial compounds against the NUDT5 enzyme and four molecules were selected based on their docking scores. These compounds established strong interactions within the NUDT5 active site, with molecular analysis highlighting the key role of Trp
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