ArticleMolecular diversity2021
Identification and molecular modeling of new quinolin-2-one thiosemicarbazide scaffold with antimicrobial urease inhibitory activity.
Article in Molecular diversity, 2021. 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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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Review
- Benzoylselenoureas: A Novel Dual-Action Inhibitor Targeting Fungal Growth and Urease Activity inACS omega · 2025Article
- Environmentally benign synthesis of unsymmetrical ureas and their evaluation as potential HIV-1 protease inhibitors via a computational approach.Molecular diversity · 2024Article
- Stereoselective synthesis and X-ray structure determination of novel 1,2-dihydroquinolinehydrazonopropanoate derivatives.Heliyon · 2024Article
- Exploration of morpholine-thiophene hybrid thiosemicarbazones for the treatment of ureolytic bacterial infections via targeting urease enzyme: Synthesis, biochemical screening and computational analysis.Frontiers in chemistry · 2024Article
- X-ray Structures and Computational Studies of Two Bioactive 2-(Adamantane-1-carbonyl)-Molecules (Basel, Switzerland) · 2022Article
- Synthesis and Identification of NewMolecules (Basel, Switzerland) · 2022Article
- Synthesis of novel amidinesFrontiers in chemistry · 2022Article
- Design and Synthesis of (2-Molecules (Basel, Switzerland) · 2021Article
- Structure- and Ligand-BasedArabian journal of chemistry · 2021Article
- AnRSC advances · 2020Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new series of 6-substituted quinolin-2-one thiosemicarbazides 6a-j has been synthesized. The structure of the target compounds was proved by different spectroscopic and elemental analyses. All the designed final compounds were evaluated for their in vitro activity against the urease-producing R. mucilaginosa and Proteus mirabilis bacteria as fungal and bacterial pathogens, respectively. Moreover, all compounds were in vitro tested as potential urease inhibitors using the cup-plate diffusion method. Compounds 6a and 6b were the most active with (IC
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