ArticleJournal of enzyme inhibition and medicinal chemistry2019
Synthesis and biological evaluation of thiazole derivatives as LbSOD inhibitors.
Article in Journal of enzyme inhibition and medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Recent Advances in Di-, Tri-Substituted Mono-Thiazoles, and Bis-Thiazoles: Factors Affecting Biological Activities, Future Aspects, and Challenges.Current topics in medicinal chemistry · 2025Review
- The repertoire of iron superoxide dismutases fromJournal of enzyme inhibition and medicinal chemistry · 2024Article
- Computational design, molecular properties, ADME, and toxicological analysis of substituted 2,6-diarylidene cyclohexanone analogs as potent pyridoxal kinase inhibitors.In silico pharmacology · 2023Article
- Synthesis and Antimicrobial Activity of New Heteroaryl(aryl) Thiazole Derivatives Molecular Docking Studies.Antibiotics (Basel, Switzerland) · 2022Article
- Thiazole Ring-A Biologically Active Scaffold.Molecules (Basel, Switzerland) · 2021Review
- Antitrichomonal activity and docking analysis of thiazole derivatives as TvMP50 protease inhibitors.Parasitology research · 2021Article
- Benzonate derivatives of acetophenone as potent α-glucosidase inhibitors: synthesis, structure-activity relationship and mechanism.Journal of enzyme inhibition and medicinal chemistry · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leishmaniasis is considered as one of the major neglected tropical diseases due to its magnitude and wide geographic distribution. Leishmania braziliensis, responsible for cutaneous leishmaniasis, is the most prevalent species in Brazil. Superoxide dismutase (SOD) belongs to the antioxidant pathway of the parasites and human host. Despite the differences between SOD of Leishmania braziliensis and human make this enzyme a promising target for drug development efforts. No medicinal chemistry effort has been made to identify LbSOD inhibitors. Herein, we show that thermal shift assays (TSA) and fluorescent protein-labeled assays (FPLA) can be employed as primary and secondary screens to achieve this goal. Moreover, we show that thiazole derivatives bind to LbSOD with micromolar affinity.
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Registered trials
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