ArticleMolecular diversity2014
Evaluation of the thiazole Schiff bases as β-glucuronidase inhibitors and their in silico studies.
Article in Molecular diversity, 2014. 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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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Novel pyrrole based triazole moiety as therapeutic hybrid: synthesis, characterization and anti-Alzheimer potential with molecular mechanism of protein ligand profile.BMC chemistry · 2024Article
- Synthesis of 2-Aminopyrimidine Derivatives and Their Evaluation asMolecules (Basel, Switzerland) · 2022Article
- Thiazolidin-2-cyanamides derivatives as novel potentJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Therapeutic significance of β-glucuronidase activity and its inhibitors: A review.European journal of medicinal chemistry · 2020Review
- Facile synthesis and biological assays of novel 2,4-disubstituted hydrazinyl-thiazoles analogs.Molecular diversity · 2016Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Twenty eight (28) derivatives 2-29 were synthesized and four analogs were found to exhibit single-digit IC(50) values as β-glucuronidase inhibitors. Molecular modeling indicates that three factors: substituent R, lone pair on the nitrogen of azomethine part, and the interactions made by the main skeleton of the molecule, determined the enzyme inhibitory potential of these compounds. The planar conformation of the molecules allows them to fit deep inside the pocket while blocking the entry of other physiological substrates seems to play an important role in their activity.
Indexed as
Identifiers
24535226What OpenQuestion holds
Registered trials
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